Effect of Aggregation and Molecular Size on the Ice Nucleation Efficiency of ProteinsClick to copy article linkArticle link copied!
- Alyssa N. AlsanteAlyssa N. AlsanteDepartment of Oceanography, Texas A&M University, College Station, Texas 77843, United StatesMore by Alyssa N. Alsante
- Daniel C. O. Thornton*Daniel C. O. Thornton*E-mail: [email protected]Department of Oceanography, Texas A&M University, College Station, Texas 77843, United StatesMore by Daniel C. O. Thornton
- Sarah D. Brooks*Sarah D. Brooks*E-mail: [email protected]Department of Atmospheric Sciences, Texas A&M University, College Station, Texas 77843, United StatesMore by Sarah D. Brooks
Abstract
Aerosol acts as ice-nucleating particles (INPs) by catalyzing the formation of ice crystals in clouds at temperatures above the homogeneous nucleation threshold (−38 °C). In this study, we show that the immersion mode ice nucleation efficiency of the environmentally relevant protein, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), occurs at temperatures between −6.8 and −31.6 °C. Further, we suggest that this range is controlled by the RuBisCO concentration and protein aggregation. The warmest median nucleation temperature (−7.9 ± 0.8 °C) was associated with the highest concentration of RuBisCO (2 × 10–1 mg mL–1) and large aggregates with a hydrodynamic diameter of ∼103 nm. We investigated four additional chemically and structurally diverse proteins, plus the tripeptide glutathione, and found that each of them was a less effective INP than RuBisCO. Ice nucleation efficiency of the proteins was independent of the size (molecular weight) for the five proteins investigated in this study. In contrast to previous work, increasing the concentration and degree of aggregation did not universally increase ice nucleation efficiency. RuBisCO was the exception to this generalization, although the underlying molecular mechanism determining why aggregated RuBisCO is such an effective INP remains elusive.
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You are free to share(copy and redistribute) this article in any medium or format and to adapt(remix, transform, and build upon) the material for any purpose, even commercially within the parameters below:
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Attribution (BY): Credit must be given to the creator.
*Disclaimer
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License Summary*
You are free to share(copy and redistribute) this article in any medium or format and to adapt(remix, transform, and build upon) the material for any purpose, even commercially within the parameters below:
Creative Commons (CC): This is a Creative Commons license.
Attribution (BY): Credit must be given to the creator.
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Synopsis
Atmospheric ice nucleation remains a major uncertainty in understanding cloud processes and climate. This study reports the effects of molecular size and aggregation on the immersion mode ice nucleation efficiency of proteins.
Introduction
Methods
Sample Choice and Preparation for Ice Nucleation and DLS Experiments
compound | size (kDa) | diameter (nm) | level of protein structure | secondary structural features | reference |
---|---|---|---|---|---|
RuBisCO | 550 | 13.2 | quaternary | β-helix/β-strand/β-turn | Andersson (45) |
pyruvate kinase | 233 | 12.5 | quaternary | β-helix/β-strand/β-turn | Ramirez-Silva et al. (46) |
alkaline phosphatase | 140 | 10.5 | quaternary | β-helix/β-strand/β-turn | Stec et al. (47) |
lipase | 63 | 0.787 | tertiary | β-strand/β-turn | Wang et al. (48) |
insulin | 5.8 | 0.435 | quaternary | β-helix/β-strand/β-turn | Frankaer et al. (49) |
glutathione | 0.307 | no data | primary | not applicable | not applicable |
Figure 1
Figure 1. 3D structures of proteins investigated in this study from the Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank (PDB) (https://www.rcsb.org/; Berman et al. (42)) of (a) RuBisCO (PDB ID 8RUC; Andersson (43)), (b) pyruvate kinase (PDB ID 7R6Y; Ramirez-Silva et al. (44)), (c) alkaline phosphatase (PDB ID 1ELX; Stec et al. (45)), (d) lipase (PDB ID 1AKN; Wang et al. (46)), and (e) insulin (PDB ID 4M4L; Frankaer et al. (47)). Each protein is shown from a front view. Each color represents a distinct protein subunit. 3D structures were reproduced under the Creative Commons CC0 1.0 Universal Public Domain Dedication.
Ice Nucleation
Dynamic Light Scattering (DLS)
Results and Discussion
Figure 2
Figure 2. Fraction of droplets frozen as a function of the temperature for each protein and peptide (n = 70–110) of (a) RuBisCO, (b) pyruvate kinase, (c) alkaline phosphatase, (d) lipase, (e) insulin, and (f) glutathione at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red) and the UHPLC water procedural blank (black). Data points represent the mean fraction frozen of the pooled data sets ± the 95% confidence limits.
Figure 3
Figure 3. Median freezing temperatures of each protein and peptide at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red) and the UHPLC water procedural blank (black). Data points show the median ± pooled standard deviation (n = 70–110).
Figure 4
Figure 4. Cumulative number of active sites per mass in milligrams as a function of the temperature [nm(T)] (n = 70–110) of RuBisCO (solid line) at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), and 2 × 10–3 mg mL–1 (green), pyruvate kinase (dashed line) at a concentration of 2 × 10–2 mg mL–1 (blue), alkaline phosphatase (dotted line) at a concentration of 2 × 10–1 mg mL–1 (purple), and insulin (dotted–dashed line) at a concentration of 2 × 10–4 mg mL–1 (orange). Only samples that were statistically warmer than the procedural blank are shown.
Figure 5
Figure 5. DLS spectra of protein solutions. Hydrodynamic diameter (Dh) distribution by intensity of (a) RuBisCO, (b) pyruvate kinase, (c) alkaline phosphatase, (d) lipase, and (e) insulin at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red). The dashed black line refers to the diameter of the protein molecule. Glutathione is too small to be detected by DLS. Note that the y-axis scale is different for each graph.
Figure 6
Figure 6. DLS spectra of protein solutions. Hydrodynamic diameter (Dh) distribution by volume-derived intensity of (a) RuBisCO, (b) pyruvate kinase, (c) alkaline phosphatase, (d) lipase, and (e) insulin at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red). The dashed black line refers to the diameter of the protein molecule. Glutathione is too small to be detected by DLS. Note that the y-axis scale is different for each graph.
Supporting Information
The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.est.3c06835.
Immersion mode ice nucleation data (Supporting Table 1), non-parametric ANOVA of the nucleation temperature (Supporting Table 2), freezing temperature of RuBisCO (2 × 10–1) and the procedural blank over repeated freeze–thaw cycles (Supporting Figure 1), hydrodynamic diameter distribution by number-derived intensity (Supporting Figure 2), fraction of droplets frozen of RuBisCO from this study from 2 × 10–1 to 2 × 10–5 mg mL–1 and Alsante et al. (33) at 5 × 10–1 mg mL–1 (Supporting Figure 3), relative frequency of the 20 amino acids from each protein (Supporting Figure 4), and relative frequency of amino acid functional groups for each protein (Supporting Figure 5) (PDF)
Terms & Conditions
Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.
INP | ice-nucleating particle |
RuBisCO | ribulose-1,5-bisphosphate carboxylase/oxygenase |
SSA | sea spray aerosol |
DLS | dynamic light scattering |
SPP | subpollen particle.3 |
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This article references 88 other publications.
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- 8Murray, B. J.; O’Sullivan, D.; Atkinson, J. D.; Webb, M. E. Ice Nucleation by Particles Immersed in Supercooled Cloud Droplets. Chem. Soc. Rev. 2012, 41 (19), 6519– 6554, DOI: 10.1039/c2cs35200aGoogle Scholar8https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38Xhtlaktr7L&md5=5a331f4c83c33d5d7a99d6dca8cf9b3fIce nucleation by particles immersed in supercooled cloud dropletsMurray, B. J.; O'Sullivan, D.; Atkinson, J. D.; Webb, M. E.Chemical Society Reviews (2012), 41 (19), 6519-6554CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. The formation of ice particles in the Earth's atm. strongly affects the properties of clouds and their impact on climate. Despite the importance of ice formation in detg. the properties of clouds, the Intergovernmental Panel on Climate Change (IPCC, 2007) was unable to assess the impact of atm. ice formation in their most recent report because our basic knowledge is insufficient. Part of the problem is the paucity of quant. information on the ability of various atm. aerosol species to initiate ice formation. Here we review and assess the existing quant. knowledge of ice nucleation by particles immersed within supercooled water droplets. We introduce aerosol species which have been identified in the past as potentially important ice nuclei and address their ice-nucleating ability when immersed in a supercooled droplet. We focus on mineral dusts, biol. species (pollen, bacteria, fungal spores and plankton), carbonaceous combustion products and volcanic ash. In order to make a quant. comparison we first introduce several ways of describing ice nucleation and then summarise the existing information according to the time-independent (singular) approxn. Using this approxn. in combination with typical atm. loadings, we est. the importance of ice nucleation by different aerosol types. According to these ests. we find that ice nucleation below about -15 °C is dominated by soot and mineral dusts. Above this temp. the only materials known to nucleate ice are biol., with quant. data for other materials absent from the literature. We conclude with a summary of the challenges our community faces.
- 9Gute, E.; Abbatt, J. P. D. Oxidative Processing Lowers the Ice Nucleation Activity of Birch and Alder Pollen. Geophys. Res. Lett. 2018, 45 (3), 1647– 1653, DOI: 10.1002/2017GL076357Google Scholar9https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXjsV2gtbg%253D&md5=9f493b50784831ba6c9eadcfa7b44ee8Oxidative Processing Lowers the Ice Nucleation Activity of Birch and Alder PollenGute, Ellen; Abbatt, Jonathan P. D.Geophysical Research Letters (2018), 45 (3), 1647-1653CODEN: GPRLAJ; ISSN:1944-8007. (Wiley-Blackwell)Pollen carry water extractable compds. with ice nucleating (IN) activity. This study investigates whether the hydroxyl radical, as the major atm. oxidant, can affect the IN activity of silver birch and gray alder subpollen particles under in-cloud conditions for deposition freezing mode conditions at 234 K. It is found that oxidn. increases the supersatn. ratio with respect to ice necessary for the onset of ice nucleation and decreases the fraction of particles which initiate ice nucleation. This redn. of IN activity under equiv. oxidn. conditions does not occur with a mineral dust sample (Arizona Test Dust). Chem. anal. of fresh and oxidized pollen material indicates a change of mol. structure with a loss of conjugation and an increase in oxidized functional groups, such as carbonyls. This is the first demonstration that in-cloud oxidn. may lower the IN abilities of biol. particles such as pollen.
- 10Matthews, B. H.; Alsante, A. N.; Brooks, S. D. Pollen Emissions of Subpollen Particles and Ice Nucleating Particles. ACS Earth Space Chem. 2023, 7 (6), 1207– 1218, DOI: 10.1021/acsearthspacechem.3c00014Google Scholar10https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3sXosFyks78%253D&md5=68ba49c1080130e06765bb2ddf308b6dPollen Emissions of Subpollen Particles and Ice Nucleating ParticlesMatthews, Brianna H.; Alsante, Alyssa N.; Brooks, Sarah D.ACS Earth and Space Chemistry (2023), 7 (6), 1207-1218CODEN: AESCCQ; ISSN:2472-3452. (American Chemical Society)Pollen grains significantly contribute to the aerosol population, and levels are predicted to increase in the future. Under humid atm. conditions, pollen grains can rupture creating pollen grain fragments referred to as subpollen particles (SPPs) which are dispersed into the atm. with wind. In this lab. study, SPP emission factors were detd. for ryegrass, Lolium sp., and giant ragweed,Ambrosia trifida, in terms of the no. of SPPs produced per pollen grain and the no. of SPPs produced per m2, which were compared to previously measured live oak,Quercus virginiana, emission factors. The SPP emission factors were 4.9 x 1013 ± 4.3 x 1013 SPPs per m2 for ryegrass, 1.3 x 1015 ± 1.1 x 1015 SPPs per m2 for giant ragweed, and 1.1 x 1015 ± 1.6 x 1015 SPPs per m2 for live oak. SPPs and whole pollen grains from these species were evaluated for their ice nucleation efficiency in immersion and contact mode freezing. Measurements of the ice nucleation efficiency indicate that SPPs are weakly effective INPs in immersion mode, but that pollen grains represent a source of moderately efficient INPs in immersion and contact modes.
- 11Burkart, J.; Gratzl, J.; Seifried, T. M.; Bieber, P.; Grothe, H. Isolation of Subpollen Particles (SPPs) of Birch: SPPs Are Potential Carriers of Ice Nucleating Macromolecules. Biogeosciences 2021, 18 (20), 5751– 5765, DOI: 10.5194/bg-18-5751-2021Google ScholarThere is no corresponding record for this reference.
- 12Pummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H. Suspendable macromolecules are responsible for ice nucleation activity of birch and conifer pollen. Atmos. Chem. Phys. 2012, 12 (5), 2541– 2550, DOI: 10.5194/acp-12-2541-2012Google Scholar12https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38Xpt12iurg%253D&md5=70cd2ea58dc1a2321693e52dde19b124Suspendable macromolecules are responsible for ice nucleation activity of birch and conifer pollenPummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H.Atmospheric Chemistry and Physics (2012), 12 (5), 2541-2550CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)The ice nucleation of bioaerosols (bacteria, pollen, spores, etc.) is a topic of growing interest, since their impact on ice cloud formation and thus on radiative forcing, an important parameter in global climate, is not yet fully understood. Here we show that pollen of different species strongly differ in their ice nucleation behavior. The av. freezing temps. in lab. expts. range from 240 to 255 K. As the most efficient nuclei (silver birch, Scots pine and common juniper pollen) have a distribution area up to the Northern timberline, their ice nucleation activity might be a cryoprotective mechanism. Far more intriguingly, it has turned out that water, which has been in contact with pollen and then been sepd. from the bodies, nucleates as good as the pollen grains themselves. The ice nuclei have to be easily-suspendable macromols. located on the pollen. Once extd., they can be distributed further through the atm. than the heavy pollen grains and so presumably augment the impact of pollen on ice cloud formation even in the upper troposphere. Our expts. lead to the conclusion that pollen ice nuclei, in contrast to bacterial and fungal ice nucleating proteins, are non-proteinaceous compds.
- 13Augustin, S.; Wex, H.; Niedermeier, D.; Pummer, B.; Grothe, H.; Hartmann, S.; Tomsche, L.; Clauss, T.; Voigtländer, J.; Ignatius, K.; Stratmann, F. Immersion freezing of birch pollen washing water. Atmos. Chem. Phys. 2013, 13 (21), 10989– 11003, DOI: 10.5194/acp-13-10989-2013Google Scholar13https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXjtlKktA%253D%253D&md5=f8bd68e665963b756c0c5859a67c4206Immersion freezing of birch pollen washing waterAugustin, S.; Wex, H.; Niedermeier, D.; Pummer, B.; Grothe, H.; Hartmann, S.; Tomsche, L.; Clauss, T.; Voigtlaender, J.; Ignatius, K.; Stratmann, F.Atmospheric Chemistry and Physics (2013), 13 (21), 10989-11003CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Birch pollen grains are known to be ice nucleating active biol. particles. The ice nucleating activity has previously been tracked down to biol. macromols. that can be easily extd. from the pollen grains in water. In the present study, we investigated the immersion freezing behavior of these ice nucleating active (INA) macromols. Therefore we measured the frozen fractions of particles generated from birch pollen washing water as a function of temp. at the Leipzig Aerosol Cloud Interaction Simulator (LACIS). Two different birch pollen samples were considered, with one originating from Sweden and one from the Czech Republic. For the Czech and Swedish birch pollen samples, freezing was obsd. to start at -19 and -17 °C, resp. The fraction of frozen droplets increased for both samples down to -24°C. Further cooling did not increase the frozen fractions any more. Instead, a plateau formed at frozen fractions below 1. This fact could be used to det. the amt. of INA macromols. in the droplets examd. here, which in turn allowed for the detn. of nucleation rates for single INA macromols. The main differences between the Swedish birch pollen and the Czech birch pollen were obvious in the temp. range between -17 and -24 °C. In this range, a second plateau region could be seen for Swedish birch pollen. As we assume INA macromols. to be the reason for the ice nucleation, we concluded that birch pollen is able to produce at least two different types of INA macromols. We were able to derive parameterizations for the heterogeneous nucleation rates for both INA macromol. types, using two different methods: a simple exponential fit and the Soccer ball model. With these parameterization methods we were able to describe the ice nucleation behavior of single INA macromols. from both the Czech and the Swedish birch pollen.
- 14Knopf, D. A.; Alpert, P. A.; Wang, B.; Aller, J. Y. Stimulation of Ice Nucleation by Marine Diatoms. Nat. Geosci. 2011, 4 (2), 88– 90, DOI: 10.1038/ngeo1037Google Scholar14https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXht1Wgt78%253D&md5=be00c72f42d6c1302c333bc0d13d07b9Stimulation of ice nucleation by marine diatomsKnopf, D. A.; Alpert, P. A.; Wang, B.; Aller, J. Y.Nature Geoscience (2011), 4 (2), 88-90CODEN: NGAEBU; ISSN:1752-0894. (Nature Publishing Group)Atm. aerosol particles serve as nuclei for ice-crystal formation. As such, these particles are crit. to the generation of cirrus clouds, which form from gas and liq. water. Atm. aerosols also initiate ice formation in warmer, mixed-phase clouds, where ice crystals coexist with aq. droplets. Biogenic aerosol particles of terrestrial origin, including bacteria and pollen, can act as ice nuclei. Whether biogenic particles of marine origin also act as ice nuclei has remained uncertain. We exposed the cosmopolitan planktonic diatom species Thalassiosira pseudonana to water vapor and supercooled aq. sodium chloride under typical tropospheric conditions conducive to cirrus-cloud formation. Ice nucleation was detd. using a controlled vapor cooling-stage microscope system. Under all conditions, diatoms initiated ice formation. The presence of diatoms in water increased the temp. for ice formation up to 13 K, and in aq. sodium chloride, ice formed at temps. up to 30 K higher than when diatoms were not present. In addn., diatoms initiated ice formation from water vapor at relative humidities as low as 65%. The rate of ice nucleation was rapid and independent of surface area. We suggest that marine biogenic particles such as diatoms help explain high values and seasonal variations in ice-nuclei concns. in subpolar regions.
- 15Wilbourn, E. K.; Thornton, D. C. O.; Ott, C.; Graff, J.; Quinn, P. K.; Bates, T. S.; Betha, R.; Russell, L. M.; Behrenfeld, M. J.; Brooks, S. D. Ice Nucleation by Marine Aerosols Over the North Atlantic Ocean in Late Spring. J. Geophys Res.: Atmos. 2020, 125 (4), e2019JD030913 DOI: 10.1029/2019JD030913Google ScholarThere is no corresponding record for this reference.
- 16Wilson, T. W.; Ladino, L. A.; Alpert, P. A.; Breckels, M. N.; Brooks, I. M.; Browse, J.; Burrows, S. M.; Carslaw, K. S.; Huffman, J. A.; Judd, C.; Kilthau, W. P.; Mason, R. H.; McFiggans, G.; Miller, L. A.; Najera, J. J.; Polishchuk, E.; Rae, S.; Schiller, C. L.; Si, M.; Temprado, J. V.; Whale, T. F.; Wong, J. P. S.; Wurl, O.; Yakobi-Hancock, J. D.; Abbatt, J. P. D.; Aller, J. Y.; Bertram, A. K.; Knopf, D. A.; Murray, B. J. A Marine Biogenic Source of Atmospheric Ice-Nucleating Particles. Nature 2015, 525 (7568), 234– 238, DOI: 10.1038/nature14986Google Scholar16https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXhsVyrtb%252FK&md5=2712b8caacd91d6435cc8b1e99cf2504A marine biogenic source of atmospheric ice-nucleating particlesWilson, Theodore W.; Ladino, Luis A.; Alpert, Peter A.; Breckels, Mark N.; Brooks, Ian M.; Browse, Jo; Burrows, Susannah M.; Carslaw, Kenneth S.; Huffman, J. Alex; Judd, Christopher; Kilthau, Wendy P.; Mason, Ryan H.; McFiggans, Gordon; Miller, Lisa A.; Najera, Juan J.; Polishchuk, Elena; Rae, Stuart; Schiller, Corinne L.; Si, Meng; Temprado, Jesus Vergara; Whale, Thomas F.; Wong, Jenny P. S.; Wurl, Oliver; Yakobi-Hancock, Jacqueline D.; Abbatt, Jonathan P. D.; Aller, Josephine Y.; Bertram, Allan K.; Knopf, Daniel A.; Murray, Benjamin J.Nature (London, United Kingdom) (2015), 525 (7568), 234-238CODEN: NATUAS; ISSN:0028-0836. (Nature Publishing Group)The amt. of ice present in clouds can affect cloud lifetime, pptn. and radiative properties. The formation of ice in clouds is facilitated by the presence of airborne ice-nucleating particles. Sea spray is one of the major global sources of atm. particles, but it is unclear to what extent these particles are capable of nucleating ice. Sea-spray aerosol contains large amts. of org. material that is ejected into the atm. during bubble bursting at the organically enriched sea-air interface or sea surface microlayer. Here we show that org. material in the sea surface microlayer nucleates ice under conditions relevant for mixed-phase cloud and high-altitude ice cloud formation. The ice-nucleating material is probably biogenic and less than approx. 0.2 μm in size. We find that exudates sepd. from cells of the marine diatom Thalassiosira pseudonana nucleate ice, and propose that org. material assocd. with phytoplankton cell exudates is a likely candidate for the obsd. ice-nucleating ability of the microlayer samples. Global model simulations of marine org. aerosol, in combination with our measurements, suggest that marine org. material may be an important source of ice-nucleating particles in remote marine environments such as the Southern Ocean, North Pacific Ocean and North Atlantic Ocean.
- 17Tesson, S. V.; Šantl-Temkiv, T. Ice nucleation activity and aeolian dispersal success in airborne and aquatic microalgae. Front. Microbiol. 2018, 9, 2681, DOI: 10.3389/fmicb.2018.02681Google Scholar17https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BB3crlsVOjsA%253D%253D&md5=f724891fabb1f0031495291e16b77075Ice Nucleation Activity and Aeolian Dispersal Success in Airborne and Aquatic MicroalgaeTesson Sylvie V M; Santl-Temkiv Tina; Santl-Temkiv Tina; Santl-Temkiv TinaFrontiers in microbiology (2018), 9 (), 2681 ISSN:1664-302X.Microalgae are common members of the atmospheric microbial assemblages. Diverse airborne microorganisms are known to produce ice nucleation active (INA) compounds, which catalyze cloud and rain formation, and thus alter cloud properties and their own deposition patterns. While the role of INA bacteria and fungi in atmospheric processes receives considerable attention, the numerical abundance and the capacity for ice nucleation in atmospheric microalgae are understudied. We isolated 81 strains of airborne microalgae from snow samples and determined their taxonomy by sequencing their ITS markers, 18S rRNA genes or 23S rRNA genes. We studied ice nucleation activity of airborne isolates, using droplet freezing assays, and their ability to withstand freezing. For comparison, we investigated 32 strains of microalgae from a culture collection, which were isolated from polar and temperate aqueous habitats. We show that ∼17% of airborne isolates, which belonged to taxa Trebouxiphyceae, Chlorophyceae and Stramenopiles, were INA. A large fraction of INA strains (over 40%) had ice nucleation activity at temperatures ≥-6°C. We found that 50% of aquatic microalgae were INA, but the majority were active at temperatures <-12°C. Most INA compounds produced by microalgae were proteinaceous and associated with the cells. While there were no deleterious effects of freezing on the viability of airborne microalgae, some of the aquatic strains were killed by freezing. In addition, the effect of desiccation was investigated for the aquatic strains and was found to constitute a limiting factor for their atmospheric dispersal. In conclusion, airborne microalgae possess adaptations to atmospheric dispersal, in contrast to microalgae isolated from aquatic habitats. We found that widespread taxa of both airborne and aquatic microalgae were INA at warm, sub-zero temperatures (>-15°C) and may thus participate in cloud and precipitation formation.
- 18Failor, K. C.; Schmale, D. G.; Vinatzer, B. A.; Monteil, C. L. Ice Nucleation Active Bacteria in Precipitation Are Genetically Diverse and Nucleate Ice by Employing Different Mechanisms. ISME J. 2017, 11 (12), 2740– 2753, DOI: 10.1038/ismej.2017.124Google Scholar18https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC1cfitV2isg%253D%253D&md5=cdde9817415ab4cdf085132adf4cfbeeIce nucleation active bacteria in precipitation are genetically diverse and nucleate ice by employing different mechanismsFailor K C; Schmale D G 3rd; Vinatzer B A; Monteil C L; Monteil C L; Monteil C LThe ISME journal (2017), 11 (12), 2740-2753 ISSN:.A growing body of circumstantial evidence suggests that ice nucleation active (Ice(+)) bacteria contribute to the initiation of precipitation by heterologous freezing of super-cooled water in clouds. However, little is known about the concentration of Ice(+) bacteria in precipitation, their genetic and phenotypic diversity, and their relationship to air mass trajectories and precipitation chemistry. In this study, 23 precipitation events were collected over 15 months in Virginia, USA. Air mass trajectories and water chemistry were determined and 33 134 isolates were screened for ice nucleation activity (INA) at -8 °C. Of 1144 isolates that tested positive during initial screening, 593 had confirmed INA at -8 °C in repeated tests. Concentrations of Ice(+) strains in precipitation were found to range from 0 to 13 219 colony forming units per liter, with a mean of 384±147. Most Ice(+) bacteria were identified as members of known and unknown Ice(+) species in the Pseudomonadaceae, Enterobacteriaceae and Xanthomonadaceae families, which nucleate ice employing the well-characterized membrane-bound INA protein. Two Ice(+) strains, however, were identified as Lysinibacillus, a Gram-positive genus not previously known to include Ice(+) bacteria. INA of the Lysinibacillus strains is due to a nanometer-sized molecule that is heat resistant, lysozyme and proteinase resistant, and secreted. Ice(+) bacteria and the INA mechanisms they employ are thus more diverse than expected. We discuss to what extent the concentration of culturable Ice(+) bacteria in precipitation and the identification of a new heat-resistant biological INA mechanism support a role for Ice(+) bacteria in the initiation of precipitation.
- 19Ladino, L. A.; Yakobi-Hancock, J. D.; Kilthau, W. P.; Mason, R. H.; Si, M.; Li, J.; Miller, L. A.; Schiller, C. L.; Huffman, J. A.; Aller, J. Y.; Knopf, D. A.; Bertram, A. K.; Abbatt, J. P. D. Addressing the Ice Nucleating Abilities of Marine Aerosol: A Combination of Deposition Mode Laboratory and Field Measurements. Atmos. Environ. 2016, 132, 1– 10, DOI: 10.1016/j.atmosenv.2016.02.028Google Scholar19https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XjtlCgu7c%253D&md5=02b56d9f5bbe2687ee3fbba03e663c14Addressing the ice nucleating abilities of marine aerosol: A combination of deposition mode laboratory and field measurementsLadino, L. A.; Yakobi-Hancock, J. D.; Kilthau, W. P.; Mason, R. H.; Si, M.; Li, J.; Miller, L. A.; Schiller, C. L.; Huffman, J. A.; Aller, J. Y.; Knopf, D. A.; Bertram, A. K.; Abbatt, J. P. D.Atmospheric Environment (2016), 132 (), 1-10CODEN: AENVEQ; ISSN:1352-2310. (Elsevier Ltd.)This study addresses, through two types of expts., the potential for the oceans to act as a source of atm. ice-nucleating particles (INPs). The INP concn. via deposition mode nucleation was measured in situ at a coastal site in British Columbia in August 2013. The INP concn. at conditions relevant to cirrus clouds (i.e., -40 °C and relative humidity with respect to ice, RHice = 139%) ranged from 0.2 L-1 to 3.3 L-1. Correlations of the INP concns. with levels of anthropogenic tracers (i.e., CO, SO2, NOx, and black carbon) and nos. of fluorescent particles do not indicate a significant influence from anthropogenic sources or submicron bioaerosols, resp. Addnl., the INPs measured in the deposition mode showed a poor correlation with the concn. of particles with sizes larger than 500 nm, which is in contrast with observations made in the immersion freezing mode. To investigate the nature of particles that could have acted as deposition INP, lab. expts. with potential marine aerosol particles were conducted under the ice-nucleating conditions used in the field. At -40 °C, no deposition activity was obsd. with salt aerosol particles (sodium chloride and two forms of com. sea salt: Sigma-Aldrich and Instant Ocean), particles composed of a com. source of natural org. matter (Suwannee River humic material), or particle mixts. of sea salt and humic material. In contrast, exudates from three phytoplankton (Thalassiosira pseudonana, Nanochloris atomus, and Emiliania huxleyi) and one marine bacterium (Vibrio harveyi) exhibited INP activity at low RHice values, down to below 110%. This suggests that the INPs measured at the field site were of marine biol. origins, although we cannot rule out other sources, including mineral dust.
- 20Maki, L. R.; Galyan, E. L.; Chang-Chien, M. M.; Caldwell, D. R. Ice Nucleation Induced by Pseudomonas Syringae. Appl. Microbiol. 1974, 28 (3), 456– 459, DOI: 10.1128/am.28.3.456-459.1974Google Scholar20https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADyaE2M%252FivFGqtA%253D%253D&md5=ae0521124cc7fbba3e20bbf344a43d0fIce nucleation induced by pseudomonas syringaeMaki L R; Galyan E L; Chang-Chien M M; Caldwell D RApplied microbiology (1974), 28 (3), 456-9 ISSN:0003-6919.Broth cultures of suspensions of Pseudomonas syringae isolated from decaying alder leaves (Alnus tenuifolia) were found to freeze at very warm (-1.8 to -3.8 C) temperatures. The initiation of freezing appears associated with the intact cell and not with extracellular material. Chemical treatments and physical destruction of the cell destroy activity. Bacteria must be in concentrations of approximately 10(6)/ml before freezing at warm temperatures occurs.
- 21Šantl-Temkiv, T.; Sahyoun, M.; Finster, K.; Hartmann, S.; Augustin-Bauditz, S.; Stratmann, F.; Wex, H.; Clauss, T.; Nielsen, N. W.; Sørensen, J. H.; Korsholm, U. S.; Wick, L. Y.; Karlson, U. G. Characterization of airborne ice-nucleation-active bacteria and bacterial fragments. Atmos. Environ. 2015, 109, 105– 117, DOI: 10.1016/j.atmosenv.2015.02.060Google Scholar21https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXjsFWru7o%253D&md5=8a7d5ff5a4f29ea8bc4a21a19b21f91cCharacterization of airborne ice-nucleation-active bacteria and bacterial fragmentsSantl-Temkiv, Tina; Sahyoun, Maher; Finster, Kai; Hartmann, Susan; Augustin-Bauditz, Stefanie; Stratmann, Frank; Wex, Heike; Clauss, Tina; Nielsen, Niels Woetmann; Soerensen, Jens Havskov; Korsholm, Ulrik Smith; Wick, Lukas Y.; Karlson, Ulrich GosewinkelAtmospheric Environment (2015), 109 (), 105-117CODEN: AENVEQ; ISSN:1352-2310. (Elsevier Ltd.)Some bacteria have the unique capacity of synthesizing ice-nucleation-active (INA) proteins and exposing them at their outer membrane surface. As INA bacteria enter the atm., they may impact the formation of clouds and pptn. We studied members of airborne bacterial communities for their capacity to catalyze ice formation and we report on the excretion of INA proteins by airborne Pseudomonas sp. We also obsd. for the first time that INA biol. fragments <220 nm were present in pptn. samples (199 and 482 INA fragments per L of pptn.), which confirms the presence of submicron INA biol. fragments in the atm. During 14 pptn. events, strains affiliated with the genus Pseudomonas, which are known to carry ina genes, were dominant. A screening for INA properties revealed that ∼12% of the cultivable bacteria caused ice formation at ≤-7 °C. They had likely been emitted to the atm. from terrestrial surfaces, e.g. by convective transport. We tested the ability of isolated INA strains to produce outer membrane vesicles and found that two isolates could do so. However, only very few INA vesicles were released per INA cell. Thus, the source of the submicron INA proteinaceous particles that we detected in the atm. remains to be elucidated.
- 22Creamean, J. M.; Ceniceros, J. E.; Newman, L.; Pace, A. D.; Hill, T. C. J.; Demott, P. J.; Rhodes, M. E. Evaluating the Potential for Haloarchaea to Serve as Ice Nucleating Particles. Biogeosciences 2021, 18 (12), 3751– 3762, DOI: 10.5194/bg-18-3751-2021Google Scholar22https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXis1ynsrjO&md5=e379fb956036c55e014dd5ccd2a8c354Evaluating the potential for Haloarchaea to serve as ice nucleating particlesCreamean, Jessie M.; Ceniceros, Julio E.; Newman, Lilyanna; Pace, Allyson D.; Hill, Thomas C. J.; DeMott, Paul J.; Rhodes, Matthew E.Biogeosciences (2021), 18 (12), 3751-3762CODEN: BIOGGR; ISSN:1726-4189. (Copernicus Publications)Aerosols play a crucial role in cloud formation. Biol. derived materials from bacteria, fungi, pollen, lichen, viruses, algae, and diatoms can serve as ice nucleating particles (INPs), some of which initiate glaciation in clouds at relatively warm freezing temps. However, detg. the magnitude of the interactions between clouds and biol. derived INPs remains a significant challenge due to the diversity and complexity of bioaerosols and limited observations of such aerosols facilitating cloud ice formation. Addnl., microorganisms from the domain Archaea have, to date, not been evaluated as INPs. Here, we present the first results reporting the ice nucleation activity of four species in the class Haloarchaea. Intact cells of Halococcus morrhuae and Haloferax sulfurifontis demonstrated the ability to induce immersion freezing at temps. up to -18 °C, while lysed cells of Haloquadratum walsbyi and Natronomonas pharaonis were unable to serve as immersion INPs. Exposure to heat and peroxide digestion indicated that the INPs of intact cells were driven by org. (H. morrhuae and H. sulfurifontis) and possibly also heat labile materials (H. sulfurifontis only). While halophiles are prominent in hypersaline environments such as the Great Salt Lake and the Dead Sea, other members of the Archaea, such as methanogens and thermophiles, are prevalent in anoxic systems in seawater, sea ice, marine sediments, glacial ice, permafrost, and other cold niches. Archaeal extremophiles are both diverse and highly abundant. Thus, it is important to assess their ability to serve as INPs as it may lead to an improved understanding of biol. impacts on clouds.
- 23Hill, T. C. J.; DeMott, P. J.; Tobo, Y.; Fröhlich-Nowoisky, J.; Moffett, B. F.; Franc, G. D.; Kreidenweis, S. M. Sources of Organic Ice Nucleating Particles in Soils. Atmos. Chem. Phys. 2016, 16 (11), 7195– 7211, DOI: 10.5194/acp-16-7195-2016Google Scholar23https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhslKqt77I&md5=3196772bd5761b3adbd4da0d67f32ae4Sources of organic ice nucleating particles in soilsHill, Tom C. J.; DeMott, Paul J.; Tobo, Yutaka; Frohlich-Nowoisky, Janine; Moffett, Bruce F.; Franc, Gary D.; Kreidenweis, Sonia M.Atmospheric Chemistry and Physics (2016), 16 (11), 7195-7211CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Soil org. matter (SOM) may be a significant source of atm. ice nucleating particles (INPs), esp. of those active >-15 °C. However, due to both a lack of investigations and the complexity of the SOM itself, the identities of these INPs remain unknown. To more comprehensively characterize org. INPs we tested locally representative soils in Wyoming and Colorado for total org. INPs, INPs in the heat-labile fraction, ice nucleating (IN) bacteria, IN fungi, IN fulvic and humic acids, IN plant tissue, and ice nucleation by monolayers of aliph. alcs. All soils contained ≈106 to ≈5×107 INPs g-1 dry soil active at -10 °C. Removal of SOM with H2O2 removed ≥99% of INPs active >-18 °C (the limit of testing), while heating of soil suspensions to 105 °C showed that labile INPs increasingly predominated >-12 °C and comprised ≥90%of INPs active >-9 °C. Papain protease, which inactivates IN proteins produced by the fungus Mortierella alpina, common in the region's soils, lowered INPs active at ≥-11 °C by _75% in two arable soils and in sagebrush shrubland soil. By contrast, lysozyme, which digests bacterial cell walls, only reduced INPs active at ≥-7.5 or ≥-6 °C, depending on the soil. The known IN bacteria were not detected in any soil, using PCR for the ina gene that codes for the active protein. We directly isolated and photographed two INPs from soil, using repeated cycles of freeze testing and subdivision of droplets of dil. soil suspensions; they were complex and apparently org. entities. Ice nucleation activity was not affected by digestion of Proteinase K-susceptible proteins or the removal of entities composed of fulvic and humic acids, sterols, or aliph. alc. monolayers. Org. INPs active colder than -10 to -12 °C were resistant to all investigations other than heat, oxidn. with H2O2, and, for some, digestion with papain. They may originate from decompg. plant material, microbial biomass, and/or the humin component of the SOM. In the case of the latter then they are most likely to be a carbohydrate. Reflecting the diversity of the SOM itself, soil INPs have a range of sources which occur with differing relative abundances.
- 24Pouleur, S.; Richard, C.; Martin, J.-G.; Antoun, H. Ice Nucleation Activity in Fusarium acuminatum and Fusarium avenaceum. Appl. Environ. Microbiol. 1992, 58 (9), 2960– 2964, DOI: 10.1128/aem.58.9.2960-2964.1992Google Scholar24https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC3crot1Wksw%253D%253D&md5=2a088d316c12f4b6f53e99b9588f55c0Ice Nucleation Activity in Fusarium acuminatum and Fusarium avenaceumPouleur S; Richard C; Martin J G; Antoun HApplied and environmental microbiology (1992), 58 (9), 2960-4 ISSN:0099-2240.Twenty fungal genera, including 14 Fusarium species, were examined for ice nucleation activity at -5.0 degrees C, and this activity was found only in Fusarium acuminatum and Fusarium avenaceum. This characteristic is unique to these two species. Ice nucleation activity of F. avenaceum was compared with ice nucleation activity of a Pseudomonas sp. strain. Cumulative nucleus spectra are similar for both microorganisms, while the maximum temperatures of ice nucleation were -2.5 degrees C for F. avenaceum and -1.0 degrees C for the bacteria. Ice nucleation activity of F. avenaceum was stable at pH levels from 1 to 13 and tolerated temperature treatments up to 60 degrees C, suggesting that these ice nuclei are more similar to lichen ice nuclei than to bacterial ones. Ice nuclei of F. avenaceum, unlike bacterial ice nuclei, pass through a 0.22-mum-pore-size filter. Fusarial nuclei share some characteristics with the so-called leaf-derived nuclei with which they might be identified: they are cell free and stable up to 60 degrees C, and they are found in the same kinds of environment. Highly stable ice nuclei produced by fast-growing microorganisms have potential applications in biotechnology. This is the first report of ice nucleation activity in free-living fungi.
- 25Fröhlich-Nowoisky, J.; Hill, T. C.; Pummer, B. G.; Yordanova, P.; Franc, G. D.; Pöschl, U. Ice nucleation activity in the widespread soil fungus Mortierella alpina. Biogeosciences 2015, 12 (4), 1057– 1071, DOI: 10.5194/bg-12-1057-2015Google ScholarThere is no corresponding record for this reference.
- 26Cascajo-Castresana, M.; David, R. O.; Iriarte-Alonso, M. A.; Bittner, A. M.; Marcolli, C. Protein Aggregates Nucleate Ice: The Example of Apoferritin. Atmos. Chem. Phys. 2020, 20 (6), 3291– 3315, DOI: 10.5194/acp-20-3291-2020Google Scholar26https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXps1aktbg%253D&md5=19298ee52a75e27c35867e5d39f05b91Protein aggregates nucleate ice: the example of apoferritinCascajo-Castresana, Maria; David, Robert O.; Iriarte-Alonso, Maiara A.; Bittner, Alexander M.; Marcolli, ClaudiaAtmospheric Chemistry and Physics (2020), 20 (6), 3291-3315CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Biol. material has gained increasing attention recently as a source of ice-nucleating particles that may account for cloud glaciation at moderate supercooling. While the ice-nucleation (IN) ability of some bacteria can be related to membrane-bound proteins with epitaxial fit to ice, little is known about the IN-active entities present in biol. material in general. To elucidate the potential of proteins and viruses to contribute to the IN activity of biol. material, we performed bulk freezing expts. with the newly developed drop freezing assay DRoplet Ice Nuclei Counter Zurich (DRINCZ), which allows the simultaneous cooling of 96 sample aliquots in a chilled ethanol bath. We performed a screening of common proteins, namely the iron storage protein ferritin and its iron-free counterpart apoferritin, the milk protein casein, the egg protein ovalbumin, two hydrophobins, and a yeast ice-binding protein, all of which revealed IN activity with active site densities > 0.1 mg-1 at -10 °C. The tobacco mosaic virus, a plant virus based on helically assembled proteins, also proved to be IN active with active site densities increasing from 100 mg-1 at -14 °C to 10 000 mg-1 at -20 °C. Among the screened proteins, the IN activity of horse spleen ferritin and apoferritin, which form cages of 24 co-assembled protein subunits, proved to be outstanding with active site densities > 10 mg-1 at -5 °C. Investigation of the pH dependence and heat resistance of the apoferritin sample confirmed the proteinaceous nature of its IN-active entities but excluded the correctly folded cage monomer as the IN-active species. A diln. series of apoferritin in water revealed two distinct freezing ranges, an upper one from -4 to -11 °C and a lower one from -11 to -21 °C. Dynamic light scattering measurements related the upper freezing range to ice-nucleating sites residing on aggregates and the lower freezing range to sites located on misfolded cage monomers or oligomers. The sites proved to persist during several freeze-thaw cycles performed with the same sample aliquots. Based on these results, IN activity seems to be a common feature of diverse proteins, irresp. of their function, but arising only rarely, most probably through defective folding or aggregation to structures that are IN active.
- 27Adams, M. P.; Atanasova, N. S.; Sofieva, S.; Ravantti, J.; Heikkinen, A.; Brasseur, Z.; Duplissy, J.; Bamford, D. H.; Murray, B. J. Ice Nucleation by Viruses and Their Potential for Cloud Glaciation. Biogeosciences 2021, 18 (14), 4431– 4444, DOI: 10.5194/bg-18-4431-2021Google Scholar27https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXis1yns77L&md5=1b39e64a52811f9a15358518ac5b1786Ice nucleation by viruses and their potential for cloud glaciationAdams, Michael P.; Atanasova, Nina S.; Sofieva, Svetlana; Ravantti, Janne; Heikkinen, Aino; Brasseur, Zoe; Duplissy, Jonathan; Bamford, Dennis H.; Murray, Benjamin J.Biogeosciences (2021), 18 (14), 4431-4444CODEN: BIOGGR; ISSN:1726-4189. (Copernicus Publications)In order to effectively predict the formation of ice in clouds we need to know which subsets of aerosol particles are effective at nucleating ice, how they are distributed and where they are from. A large proportion of ice-nucleating particles (INPs) in many locations are likely of biol. origin, and some INPs are extremely small, being just tens of nanometers in size. The identity and sources of such INPs are not well characterized. Here, we show that several different types of virus particles can nucleate ice, with up to about 1 in 20 million virus particles able to nucleate ice at -20 °C. In terms of the impact on cloud glaciation, the ice-nucleating ability (the fraction which are ice nucleation active as a function of temp.) taken together with typical virus particle concns. in the atm. leads to the conclusion that virus particles make a minor contribution to the atm. ice-nucleating particle population in the terrestrial-influenced atm. However, they cannot be ruled out as being important in the remote marine atm. It is striking that virus particles have an ice-nucleating activity, and further work should be done to explore other types of viruses for both their ice-nucleating potential and to understand the mechanism by which viruses nucleate ice.
- 28Alpert, P. A.; Aller, J. Y.; Knopf, D. A. Ice Nucleation from Aqueous NaCl Droplets with and without Marine Diatoms. Atmos. Chem. Phys. 2011, 11 (12), 5539– 5555, DOI: 10.5194/acp-11-5539-2011Google Scholar28https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXht1WjtrrO&md5=b1267c0528d6017d98040fbee83928e4Ice nucleation from aqueous NaCl droplets with and without marine diatomsAlpert, P. A.; Aller, J. Y.; Knopf, D. A.Atmospheric Chemistry and Physics (2011), 11 (12), 5539-5555CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)Ice formation in the atm. by homogeneous and heterogeneous nucleation is one of the least understood processes in cloud microphysics and climate. Here we describe our investigation of the marine environment as a potential source of atm. IN by exptl. observing homogeneous ice nucleation from aq. NaCl droplets and comparing against heterogeneous ice nucleation from aq. NaCl droplets contg. intact and fragmented diatoms. Homogeneous and heterogeneous ice nucleation are studied as a function of temp. and water activity, aw. Addnl. analyses are presented on the dependence of diatom surface area and aq. vol. on heterogeneous freezing temps., ice nucleation rates, ωhet, ice nucleation rate coeffs., Jhet, and differential and cumulative ice nuclei spectra, k(T) and K(T), resp. Homogeneous freezing temps. and corresponding nucleation rate coeffs. are in agreement with the water activity based homogeneous ice nucleation theory within exptl. and predictive uncertainties. Our results confirm, as predicted by classical nucleation theory, that a stochastic interpretation can be used to describe the homogeneous ice nucleation process. Heterogeneous ice nucleation initiated by intact and fragmented diatoms can be adequately represented by a modified water activity based ice nucleation theory. A horizontal shift in water activity, Δaw,het = 0.2303, of the ice melting curve can describe median heterogeneous freezing temps. Individual freezing temps. showed no dependence on available diatom surface area and aq. vol. Detd. at median diatom freezing temps. for aw from 0.8 to 0.99, ωhet≃0.11+0.06-0.05 s-1, Jhet≃1.0+1.16-0.61 × 104 cm-2 s-1, and K≃6.2+3.5-4.1 × 104 cm-2. The exptl. derived ice nucleation rates and nuclei spectra allow us to est. ice particle prodn. which we subsequently use for a comparison with obsd. ice crystal concns. typically found in cirrus and polar marine mixed-phase clouds. Differences in application of time-dependent and time-independent analyses to predict ice particle prodn. are discussed.
- 29Ickes, L.; Porter, G. C. E.; Wagner, R.; Adams, M. P.; Bierbauer, S.; Bertram, A. K.; Bilde, M.; Christiansen, S.; Ekman, A. M. L.; Gorokhova, E.; Höhler, K.; Kiselev, A. A.; Leck, C.; Möhler, O.; Murray, B. J.; Schiebel, T.; Ullrich, R.; Salter, M. E. The Ice-Nucleating Activity of Arctic Sea Surface Microlayer Samples and Marine Algal Cultures. Atmos. Chem. Phys. 2020, 20 (18), 11089– 11117, DOI: 10.5194/acp-20-11089-2020Google Scholar29https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXitVyltL3P&md5=c5c9b8c7e0f0e823d26c01029b4efaa2The ice-nucleating activity of Arctic sea surface microlayer samples and marine algal culturesIckes, Luisa; Porter, Grace C. E.; Wagner, Robert; Adams, Michael P.; Bierbauer, Sascha; Bertram, Allan K.; Bilde, Merete; Christiansen, Sigurd; Ekman, Annica M. L.; Gorokhova, Elena; Hoehler, Kristina; Kiselev, Alexei A.; Leck, Caroline; Moehler, Ottmar; Murray, Benjamin J.; Schiebel, Thea; Ullrich, Romy; Salter, Matthew E.Atmospheric Chemistry and Physics (2020), 20 (18), 11089-11117CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)In recent years, sea spray as well as the biol. material it contains has received increased attention as a source of ice-nucleating particles (INPs). Such INPs may play a role in remote marine regions, where other sources of INPs are scarce or absent. In the Arctic, these INPs can influence water-ice partitioning in low-level clouds and thereby the cloud lifetime, with consequences for the surface energy budget, sea ice formation and melt, and climate. Marine aerosol is of a diverse nature, so identifying sources of INPs is challenging. One fraction of marine bioaerosol (phytoplankton and their exudates) has been a particular focus of marine INP research. Firstly, we compare the ice-nucleating ability of two common phytoplankton species with Arctic seawater microlayer samples using the same instrumentation to see if these phytoplankton species produce ice-nucleating material with sufficient activity to account for the ice nucleation obsd. in Arctic microlayer samples. We present the first measurements of the ice-nucleating ability of two predominant phytoplankton species: Melosira arctica, a common Arctic diatom species, and Skeletonema marinoi, a ubiquitous diatom species across oceans worldwide. To det. the potential effect of nutrient conditions and characteristics of the algal culture, such as the amt. of org. carbon assocd. with algal cells, on the ice nucleation activity, Skeletonema marinoi was grown under different nutrient regimes.
- 30Bogler, S.; Borduas-Dedekind, N. Lignin’s Ability to Nucleate Ice via Immersion Freezing and Its Stability towards Physicochemical Treatments and Atmospheric Processing. Atmos. Chem. Phys. 2020, 20 (23), 14509– 14522, DOI: 10.5194/acp-20-14509-2020Google Scholar30https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXis1antbzL&md5=0178f8463d4f87656ea1ff9aee2b9f68Lignin's ability to nucleate ice via immersion freezing and its stability towards physicochemical treatments and atmospheric processingBogler, Sophie; Borduas-Dedekind, NadineAtmospheric Chemistry and Physics (2020), 20 (23), 14509-14522CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Aerosol-cloud interactions dominate the uncertainties in current predictions of the atm.'s radiative balance. Specifically, the ice phase remains difficult to predict in mixed-phase clouds, where liq. water and ice co-exist. The formation of ice in these clouds originates from heterogeneous ice nucleation processes, of which immersion freezing is a dominant pathway. Among atm. surfaces capable of forming a template for ice, mineral dust, biol. material and more recently org. matter are known to initiate freezing. To further our understanding of the role of org. matter in ice nucleation, we chose to investigate the ice nucleation (IN) ability of a specific subcomponent of atm. org. matter, the biopolymer lignin. Ice nucleation expts. were conducted in our custom-built freezing ice nuclei counter (FINC) to measure freezing temps. in the immersion freezing mode. We find that lignin acts as an ice-active macromol. at temps. relevant for mixed-phase cloud processes (e.g. 50% activated fraction up to -18.8°C at 200 mg C L-1). Within a diln. series of lignin solns., we obsd. a non-linear effect in freezing temps.; the no. of IN sites per mg of carbon increased with decreasing lignin concn. We attribute this change to a concn.-dependant aggregation of lignin in soln. We further investigated the effect of physicochem. treatments on lignin's IN activity, including expts. with sonication, heating and reaction with hydrogen peroxide. Only harsh conditions such as heating to 260°C and addn. of a mixt. with a ratio of 1 : 750 of grams of lignin to millilitres of hydrogen peroxide were able to decrease lignin's IN activity to the instrument's background level. Next, photochem. and ozone bubbling expts. were conducted to test the effect of atm. processing on lignin's IN activity. We showed that this activity was not susceptible to changes under atmospherically relevant conditions, despite chem. changes obsd. by UV-Vis absorbance. Our results present lignin as a recalcitrant IN-active subcomponent of org. matter within, for example, biomass burning aerosols and brown carbon. They further contribute to the understanding of how sol. org. material in the atm. can nucleate ice.
- 31Hiranuma, N.; Möhler, O.; Yamashita, K.; Tajiri, T.; Saito, A.; Kiselev, A.; Hoffmann, N.; Hoose, C.; Jantsch, E.; Koop, T.; Murakami, M. Ice Nucleation by Cellulose and Its Potential Contribution to Ice Formation in Clouds. Nat. Geosci. 2015, 8 (4), 273– 277, DOI: 10.1038/ngeo2374Google Scholar31https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXjs1GqsL8%253D&md5=4b9b7fcd57b1a6c80c53f584a3838c1dIce nucleation by cellulose and its potential contribution to ice formation in cloudsHiranuma, N.; Moehler, O.; Yamashita, K.; Tajiri, T.; Saito, A.; Kiselev, A.; Hoffmann, N.; Hoose, C.; Jantsch, E.; Koop, T.; Murakami, M.Nature Geoscience (2015), 8 (4), 273-277CODEN: NGAEBU; ISSN:1752-0894. (Nature Publishing Group)Ice particles in the atm. influence clouds, pptn. and climate, and often form with help from aerosols that serve as ice-nucleating particles. Biol. particles, including non-proteinaceous ones, contribute to the diverse spectrum of ice-nucleating particles. However, little is known about their atm. abundance and ice nucleation efficiency, and their role in clouds and the climate system is poorly constrained. One biol. particle type, cellulose, has been shown to exist in an airborne form that is prevalent throughout the year even at remote and elevated locations. Here we report expts. in a cloud simulation chamber to demonstrate that microcryst. cellulose particles can act as efficient ice-nucleating particles in simulated supercooled clouds. In six immersion mode freezing expts., we measured the ice nucleation active surface-site densities of aerosolized cellulose across a range of temps. Using these active surface-site densities, we developed parameters describing the ice nucleation ability of these particles and applied them to obsd. atm. cellulose and plant debris concns. in a global aerosol model. We find that ice nucleation by cellulose becomes significant (>0.1 l-1) below about -21 °C, temps. relevant to mixed-phase clouds. We conclude that the ability of cellulose to act as ice-nucleating particles requires a revised quantification of their role in cloud formation and pptn.
- 32Hiranuma, N.; Adachi, K.; Bell, D. M.; Belosi, F.; Beydoun, H.; Bhaduri, B.; Bingemer, H.; Budke, C.; Clemen, H.-C.; Conen, F.; Cory, K. M.; Curtius, J.; DeMott, P. J.; Eppers, O.; Grawe, S.; Hartmann, S.; Hoffmann, N.; Höhler, K.; Jantsch, E.; Kiselev, A.; Koop, T.; Kulkarni, G.; Mayer, A.; Murakami, M.; Murray, B. J.; Nicosia, A.; Petters, M. D.; Piazza, M.; Polen, M.; Reicher, N.; Rudich, Y.; Saito, A.; Santachiara, G.; Schiebel, T.; Schill, G. P.; Schneider, J.; Segev, L.; Stopelli, E.; Sullivan, R. C.; Suski, K.; Szakáll, M.; Tajiri, T.; Taylor, H.; Tobo, Y.; Ullrich, R.; Weber, D.; Wex, H.; Whale, T. F.; Whiteside, C. L.; Yamashita, K.; Zelenyuk, A.; Möhler, O. A Comprehensive Characterization of Ice Nucleation by Three Different Types of Cellulose Particles Immersed in Water. Atmos. Chem. Phys. 2019, 19 (7), 4823– 4849, DOI: 10.5194/acp-19-4823-2019Google Scholar32https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXps1aks7k%253D&md5=28b62af8c11cec554e97e21e1a9aea5cA comprehensive characterization of ice nucleation by three different types of cellulose particles immersed in waterHiranuma, Naruki; Adachi, Kouji; Bell, David M.; Belosi, Franco; Beydoun, Hassan; Bhaduri, Bhaskar; Bingemer, Heinz; Budke, Carsten; Clemen, Hans-Christian; Conen, Franz; Cory, Kimberly M.; Curtius, Joachim; Demott, Paul J.; Eppers, Oliver; Grawe, Sarah; Hartmann, Susan; Hoffmann, Nadine; Hohler, Kristina; Jantsch, Evelyn; Kiselev, Alexei; Koop, Thomas; Kulkarni, Gourihar; Mayer, Amelie; Murakami, Masataka; Murray, Benjamin J.; Nicosia, Alessia; Petters, Markus D.; Piazza, Matteo; Polen, Michael; Reicher, Naama; Rudich, Yinon; Saito, Atsushi; Santachiara, Gianni; Schiebel, Thea; Schill, Gregg P.; Schneider, Johannes; Segev, Lior; Stopelli, Emiliano; Sullivan, Ryan C.; Suski, Kaitlyn; Szakall, Miklos; Tajiri, Takuya; Taylor, Hans; Tobo, Yutaka; Ullrich, Romy; Weber, Daniel; Wex, Heike; Whale, Thomas F.; Whiteside, Craig L.; Yamashita, Katsuya; Zelenyuk, Alla; Mohler, OttmarAtmospheric Chemistry and Physics (2019), 19 (7), 4823-4849CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)We present the lab. results of immersion freezing efficiencies of cellulose particles at supercooled temp. (T) conditions. Three types of chem. homogeneous cellulose samples are used as surrogates that represent supermicron and submicron ice-nucleating plant structural polymers. These samples include microcryst. cellulose (MCC), fibrous cellulose (FC) and nanocryst. cellulose (NCC). Our immersion freezing dataset includes data from various ice nucleation measurement techniques available at 17 different institutions, including nine dry dispersion and 11 aq. suspension techniques. With a total of 20 methods, we performed systematic accuracy and precision anal. of measurements from all 20 measurement techniques by evaluating T -binned (1 °C) data over a wide range (-36 °C < T < -4 °C). Specifically, we intercompared the geometric surface area-based ice nucleation active surface site (INAS) d. data derived from our measurements as a function of T, ns,geo(T). Addnl., we also compared the ns,geo(T) values and the freezing spectral slope parameter (1log(ns,geo)/ Δ T) from our measurements to previous literature results. Results show all three cellulose materials are reasonably ice active. The freezing efficiencies of NCC samples agree reasonably well, whereas the diversity for the other two samples spans ≈ 10 °C. Despite given uncertainties within each instrument technique, the overall trend of the ns,geo(T) spectrum traced by the T -binned av. of measurements suggests that predominantly supermicron-sized cellulose particles (MCC and FC) generally act as more efficient ice-nucleating particles (INPs) than NCC with about 1 order of magnitude higher ns,geo(T).
- 33Alsante, A. N.; Thornton, D. C. O.; Brooks, S. D. Ice Nucleation Catalyzed by the Photosynthesis Enzyme RuBisCO and Other Abundant Biomolecules. Commun. Earth Environ. 2023, 4 (1), 51, DOI: 10.1038/s43247-023-00707-7Google ScholarThere is no corresponding record for this reference.
- 34Wolf, M. J.; Coe, A.; Dove, L. A.; Zawadowicz, M. A.; Dooley, K.; Biller, S. J.; Zhang, Y.; Chisholm, S. W.; Cziczo, D. J. Investigating the Heterogeneous Ice Nucleation of Sea Spray Aerosols Using Prochlorococcus as a Model Source of Marine Organic Matter. Environ. Sci. Technol. 2019, 53 (3), 1139– 1149, DOI: 10.1021/acs.est.8b05150Google Scholar34https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXis1SktrrO&md5=dcb8b0d4eef55066f8f1929f628cd69fInvestigating the Heterogeneous Ice Nucleation of Sea Spray Aerosols Using Prochlorococcus as a Model Source of Marine Organic MatterWolf, Martin J.; Coe, Allison; Dove, Lilian A.; Zawadowicz, Maria A.; Dooley, Keven; Biller, Steven J.; Zhang, Yue; Chisholm, Sallie W.; Cziczo, Daniel J.Environmental Science & Technology (2019), 53 (3), 1139-1149CODEN: ESTHAG; ISSN:0013-936X. (American Chemical Society)Sea spray is the largest aerosol source on Earth. Bubble bursting mechanisms at the ocean surface create smaller film burst and larger jet drop particles. This study quantified the effects of particle chem. on the depositional ice nucleation efficiency of lab.-generated sea spray aerosols under the cirrus-relevant conditions. Cultures of Prochlorococcus, the most abundant phytoplankton species in the global ocean, were used as a model source of org. sea spray aerosols. We show that smaller particles generated from lyzed Prochlorococcus cultures are organically enriched and nucleate more effectively than larger particles generated from the same cultures. We then quantified the ice nucleation efficiency of single component org. mols. that mimic Prochlorococcus proteins, lipids, and saccharides. Amylopectin, agarose, and aspartic acid exhibited similar crit. ice saturations, fractional activations, and ice nucleation active site no. densities to particles generated from Prochlorococcus cultures. These findings indicate that saccharides and proteins with numerous and well-ordered hydrophilic functional groups may det. the ice nucleation abilities of org. sea spray aerosols.
- 35Pummer, B. G.; Budke, C.; Augustin-Bauditz, S.; Niedermeier, D.; Felgitsch, L.; Kampf, C. J.; Huber, R. G.; Liedl, K. R.; Loerting, T.; Moschen, T.; Schauperl, M.; Tollinger, M.; Morris, C. E.; Wex, H.; Grothe, H.; Pöschl, U.; Koop, T.; Fröhlich-Nowoisky, J. Ice Nucleation by Water-Soluble Macromolecules. Atmos. Chem. Phys. 2015, 15 (8), 4077– 4091, DOI: 10.5194/acp-15-4077-2015Google Scholar35https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXns1ahsL4%253D&md5=b851059d5ff5097c39d6cdc4a27914aaIce nucleation by water-soluble macromoleculesPummer, B. G.; Budke, C.; Augustin-Bauditz, S.; Niedermeier, D.; Felgitsch, L.; Kampf, C. J.; Huber, R. G.; Liedl, K. R.; Loerting, T.; Moschen, T.; Schauperl, M.; Tollinger, M.; Morris, C. E.; Wex, H.; Grothe, H.; Poeschl, U.; Koop, T.; Froehlich-Nowoisky, J.Atmospheric Chemistry and Physics (2015), 15 (8), 4077-4091CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Cloud glaciation is critically important for the global radiation budget (albedo) and for initiation of pptn. But the freezing of pure water droplets requires cooling to temps. as low as 235 K. Freezing at higher temps. requires the presence of an ice nucleator, which serves as a template for arranging water mols. in an ice-like manner. It is often assumed that these ice nucleators have to be insol. particles. We point out that also free macromols. which are dissolved in water can efficiently induce ice nucleation: the size of such ice nucleating macromols. (INMs) is in the range of nanometers, corresponding to the size of the crit. ice embryo. As the latter is temp.-dependent, we see a correlation between the size of INMs and the ice nucleation temp. as predicted by classical nucleation theory. Different types of INMs have been found in a wide range of biol. species and comprise a variety of chem. structures including proteins, saccharides, and lipids. Our investigation of the fungal species Acremonium implicatum, Isaria farinosa, and Mortierella alpina shows that their ice nucleation activity is caused by proteinaceous water-sol. INMs. We combine these new results and literature data on INMs from fungi, bacteria, and pollen with theor. calcns. to develop a chem. interpretation of ice nucleation and water-sol. INMs. This has atm. implications since many of these INMs can be released by fragmentation of the carrier cell and subsequently may be distributed independently. Up to now, this process has not been accounted for in atm. models.
- 36Wex, H.; Augustin-Bauditz, S.; Boose, Y.; Budke, C.; Curtius, J.; Diehl, K.; Dreyer, A.; Frank, F.; Hartmann, S.; Hiranuma, N.; Jantsch, E.; Kanji, Z. A.; Kiselev, A.; Koop, T.; Möhler, O.; Niedermeier, D.; Nillius, B.; Rösch, M.; Rose, D.; Schmidt, C.; Steinke, I.; Stratmann, F. Intercomparing Different Devices for the Investigation of Ice Nucleating Particles Using Snomax® as Test Substance. Atmos. Chem. Phys. 2015, 15 (3), 1463– 1485, DOI: 10.5194/acp-15-1463-2015Google Scholar36https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXivFOgsr4%253D&md5=40d4551c82cf2eb8f98389a4bcd243e3Intercomparing different devices for the investigation of ice nucleating particles using Snomax as test substanceWex, H.; Augustin-Bauditz, S.; Boose, Y.; Budke, C.; Curtius, J.; Diehl, K.; Dreyer, A.; Frank, F.; Hartmann, S.; Hiranuma, N.; Jantsch, E.; Kanji, Z. A.; Kiselev, A.; Koop, T.; Moehler, O.; Niedermeier, D.; Nillius, B.; Roesch, M.; Rose, D.; Schmidt, C.; Steinke, I.; Stratmann, F.Atmospheric Chemistry and Physics (2015), 15 (3), 1463-1485, 23 pp.CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Seven different instruments and measurement methods were used to examine the immersion freezing of bacterial ice nuclei from Snomax (hereafter Snomax), a product contg. ice-active protein complexes from nonviable Pseudomonas syringae bacteria. The exptl. conditions were kept as similar as possible for the different measurements. Of the participating instruments, some examd. droplets which had been made from suspensions directly, and the others examd. droplets activated on previously generated Snomax particles, with particle diams. of mostly a few hundred nanometers and up to a few micrometers in some cases. Data were obtained in the temp. range from -2 to -38 °C, and it was found that all ice-active protein complexes were already activated above -12 °C. Droplets with different Snomax mass concns. covering 10 orders of magnitude were examd. Some instruments had very short ice nucleation times down to below 1 s, while others had comparably slow cooling rates around 1 Kmin-1. Displaying data from the different instruments in terms of nos. of ice-active protein complexes per dry mass of Snomax, nm, showed that within their uncertainty, the data agree well with each other as well as to previously reported literature results. Two parameterizations were taken from literature for a direct comparison to our results, and these were a time-dependent approach based on a contact angle distribution (Niedermeier et al., 2014) and a modification of the parameterization presented in Hartmann et al. (2013) representing a time-independent approach. The agreement between these and the measured data were good; i.e., they agreed within a temp. range of 0.6K or equivalently a range in nm of a factor of 2. From the results presented herein, we propose that Snomax, at least when carefully shared and prepd., is a suitable material to test and compare different instruments for their accuracy of measuring immersion freezing.
- 37Hartmann, S.; Ling, M.; Dreyer, L. S. A.; Zipori, A.; Finster, K.; Grawe, S.; Jensen, L. Z.; Borck, S.; Reicher, N.; Drace, T.; Niedermeier, D.; Jones, N. C.; Hoffmann, S. V.; Wex, H.; Rudich, Y.; Boesen, T.; Šantl-Temkiv, T. Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity. Front. Microbiol. 2022, 13, 872306, DOI: 10.3389/fmicb.2022.872306Google Scholar37https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BB2Mfjtlyjtg%253D%253D&md5=80ab0ba31518c87430496235534fd938Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their ActivityHartmann Susan; Grawe Sarah; Niedermeier Dennis; Wex Heike; Ling Meilee; Finster Kai; Jensen Lasse Z; Borck Stella; Santl-Temkiv Tina; Ling Meilee; Finster Kai; Jensen Lasse Z; Borck Stella; Santl-Temkiv Tina; Ling Meilee; Dreyer Lasse S A; Jensen Lasse Z; Borck Stella; Drace Taner; Boesen Thomas; Zipori Assaf; Reicher Naama; Rudich Yinon; Jones Nykola C; Hoffmann Soren V; Boesen ThomasFrontiers in microbiology (2022), 13 (), 872306 ISSN:1664-302X.Microbially-produced ice nucleating proteins (INpro) are unique molecular structures with the highest known catalytic efficiency for ice formation. Airborne microorganisms utilize these proteins to enhance their survival by reducing their atmospheric residence times. INpro also have critical environmental effects including impacts on the atmospheric water cycle, through their role in cloud and precipitation formation, as well as frost damage on crops. INpro are ubiquitously present in the atmosphere where they are emitted from diverse terrestrial and marine environments. Even though bacterial genes encoding INpro have been discovered and sequenced decades ago, the details of how the INpro molecular structure and oligomerization foster their unique ice-nucleation activity remain elusive. Using machine-learning based software AlphaFold 2 and trRosetta, we obtained and analysed the first ab initio structural models of full length and truncated versions of bacterial INpro. The modeling revealed a novel beta-helix structure of the INpro central repeat domain responsible for ice nucleation activity. This domain consists of repeated stacks of two beta strands connected by two sharp turns. One beta-strand is decorated with a TxT amino acid sequence motif and the other strand has an SxL[T/I] motif. The core formed between the stacked beta helix-pairs is unusually polar and very distinct from previous INpro models. Using synchrotron radiation circular dichroism, we validated the β-strand content of the central repeat domain in the model. Combining the structural model with functional studies of purified recombinant INpro, electron microscopy and modeling, we further demonstrate that the formation of dimers and higher-order oligomers is key to INpro activity. Using computational docking of the new INpro model based on rigid-body algorithms we could reproduce a previously proposed homodimer structure of the INpro CRD with an interface along a highly conserved tyrosine ladder and show that the dimer model agrees with our functional data. The parallel dimer structure creates a surface where the TxT motif of one monomer aligns with the SxL[T/I] motif of the other monomer widening the surface that interacts with water molecules and therefore enhancing the ice nucleation activity. This work presents a major advance in understanding the molecular foundation for bacterial ice-nucleation activity.
- 38Lukas, M.; Schwidetzky, R.; Eufemio, R. J.; Bonn, M.; Meister, K. Toward Understanding Bacterial Ice Nucleation. J. Phys. Chem. B 2022, 126 (9), 1861– 1867, DOI: 10.1021/acs.jpcb.1c09342Google Scholar38https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XitFWjsb8%253D&md5=6629df0508ec4794b199fe434acd50bfToward Understanding Bacterial Ice NucleationLukas, Max; Schwidetzky, Ralph; Eufemio, Rosemary J.; Bonn, Mischa; Meister, KonradJournal of Physical Chemistry B (2022), 126 (9), 1861-1867CODEN: JPCBFK; ISSN:1520-5207. (American Chemical Society)A review. Bacterial ice nucleators (INs) are among the most effective ice nucleators known and relevant for freezing processes in agriculture, the atm., and the biosphere. Their ability to facilitate ice formation is due to specialized ice-nucleating proteins (INPs) anchored to the outer bacterial cell membrane and enabling the crystn. of water at temps. up to -2°. In this Perspective, the authors highlight the importance of functional aggregation of INPs for the exceptionally high ice nucleation activity of bacterial ice nucleators. The authors emphasize that the bacterial cell membrane, as well as environmental conditions, are crucial for a precise functional INP aggregation. Interdisciplinary approaches combining high-throughput droplet freezing assays with advanced physicochem. tools and protein biochem. are needed to link changes in protein structure or protein-water interactions with changes on the functional level.
- 39Valegård, K.; Hasse, D.; Andersson, I.; Gunn, L. H. Structure of Rubisco from Arabidopsis thaliana in Complex with 2-Carboxyarabinitol-1,5-Bisphosphate. Acta Crystallogr., Sect. D: Struct. Biol. 2018, 74 (1), 1– 9, DOI: 10.1107/S2059798317017132Google Scholar39https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC1MvksF2quw%253D%253D&md5=6f330bf5a9353bf87b49a7db82c3bc9fStructure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bisphosphateValegard Karin; Hasse Dirk; Andersson Inger; Gunn Laura HActa crystallographica. Section D, Structural biology (2018), 74 (Pt 1), 1-9 ISSN:.The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Arabidopsis thaliana is reported at 1.5 ÅA resolution. In light of the importance of A. thaliana as a model organism for understanding higher plant biology, and the pivotal role of Rubisco in photosynthetic carbon assimilation, there has been a notable absence of an A. thaliana Rubisco crystal structure. A. thaliana Rubisco is an L8S8 hexadecamer comprising eight plastome-encoded catalytic large (L) subunits and eight nuclear-encoded small (S) subunits. A. thaliana produces four distinct small-subunit isoforms (RbcS1A, RbcS1B, RbcS2B and RbcS3B), and this crystal structure provides a snapshot of A. thaliana Rubisco containing the low-abundance RbcS3B small-subunit isoform. Crystals were obtained in the presence of the transition-state analogue 2-carboxy-D-arabinitol-1,5-bisphosphate. A. thaliana Rubisco shares the overall fold characteristic of higher plant Rubiscos, but exhibits an interesting disparity between sequence and structural relatedness to other Rubisco isoforms. These results provide the structural framework to understand A. thaliana Rubisco and the potential catalytic differences that could be conferred by alternative A. thaliana Rubisco small-subunit isoforms.
- 40Bar-On, Y. M.; Milo, R. The Global Mass and Average Rate of Rubisco. Proc. Natl. Acad. Sci. U. S. A. 2019, 116 (10), 4738– 4743, DOI: 10.1073/pnas.1816654116Google Scholar40https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXktFeit7g%253D&md5=063c6eaf419c513d9b543716359efa10The global mass and average rate of rubiscoBar-On, Yinon M.; Milo, RonProceedings of the National Academy of Sciences of the United States of America (2019), 116 (10), 4738-4743CODEN: PNASA6; ISSN:0027-8424. (National Academy of Sciences)Photosynthetic carbon assimilation enables energy storage in the living world and produces most of the biomass in the biosphere. Rubisco (d-ribulose 1,5-bisphosphate carboxylase/oxygenase) is responsible for the vast majority of global carbon fixation and has been claimed to be the most abundant protein on Earth. Here we provide an updated and rigorous est. for the total mass of Rubisco on Earth, concluding it is 0.7 Gt, more than an order of magnitude higher than previously thought. We find that >90% of Rubisco enzymes are found in the 2 A~, 1014 m2 of leaves of terrestrial plants, and that Rubisco accounts for 3% of the total mass of leaves, which we est. at 30 Gt dry wt. We use our est. for the total mass of Rubisco to derive the effective time-averaged catalytic rate of Rubisco of 0.03 s1 on land and 0.6 s1 in the ocean. Compared with the maximal catalytic rate obsd. in vitro at 25°C, the effective rate in the wild is 100-fold slower on land and sevenfold slower in the ocean. The lower ambient temp., and Rubisco not working at night, can explain most of the difference from lab. conditions in the ocean but not on land, where quantification of many more factors on a global scale is needed. Our anal. helps sharpen the dramatic difference between lab. and wild environments and between the terrestrial and marine environments.
- 41Tabita, F. R.; Satagopan, S.; Hanson, T. E.; Kreel, N. E.; Scott, S. S. Distinct Form I, II, III, and IV Rubisco Proteins from the Three Kingdoms of Life Provide Clues about Rubisco Evolution and Structure/Function Relationships. J. Exp. Bot. 2007, 59 (7), 1515– 1524, DOI: 10.1093/jxb/erm361Google ScholarThere is no corresponding record for this reference.
- 42Berman, H. M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T. N.; Weissig, H.; Shindyalov, I. N.; Bourne, P. E. The Protein Data Bank. Nucleic Acids Res. 2000, 28 (1), 235– 242, DOI: 10.1093/nar/28.1.235Google Scholar42https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3cXhvVKjt7w%253D&md5=227fb393f754be2be375ab727bfd05dcThe Protein Data BankBerman, Helen M.; Westbrook, John; Feng, Zukang; Gilliland, Gary; Bhat, T. N.; Weissig, Helge; Shindyalov, Ilya N.; Bourne, Philip E.Nucleic Acids Research (2000), 28 (1), 235-242CODEN: NARHAD; ISSN:0305-1048. (Oxford University Press)The Protein Data Bank (PDB; http://www.rcsb.org/pdb/)is the single worldwide archive of structural data of biol. macromols. This paper describes the goals of the PDB, the systems in place for data deposition and access, how to obtain further information, and near-term plans for the future development of the resource.
- 43Andersson, I. Large Structures at High Resolution: The 1.6 Å Crystal Structure of Spinach Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase Complexed with 2-Carboxyarabinitol Bisphosphate. J. Mol. Biol. 1996, 259 (1), 160– 174, DOI: 10.1006/jmbi.1996.0310Google Scholar43https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADyaK283ktVKrtQ%253D%253D&md5=16132eef90ab69dde6a5aaf021aae450Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphateAndersson IJournal of molecular biology (1996), 259 (1), 160-74 ISSN:0022-2836.Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) from spinach is a hexadecamer (L8S8, Mr = 550,000) consisting of eight large (L, 475 residues) and eight small subunits (S, 123 residues). High-resolution data collection on crystals with large unit cells is not a trivial task due to the effect of radiation damage and the large number of overlapping reflections when conventional data collection methods are used. In order to minimise these effects, data on rubisco were collected with a giant Weissenberg camera at long crystal to image-plate distances at the synchrotron of the Photon Factory, Japan. Relative to conventional data sets, this experimental arrangement allowed a 20 to 30-fold reduction of the X-ray dose/exposure time for data collection. This paper describes the refined 1.6 A crystal structure of activated rubisco complexed with a transition state analogue, 2-carboxyarabinitol-bisphosphate. The crystallographic asymmetric unit contains an L4S4 unit, representing half of the molecule. The structure presented here is currently the highest resolution structure for any protein of comparable size. Refinement of the model was carried out by restrained least squares techniques without non-crystallographic symmetry averaging. The results show that all L and S subunits have identical three-dimensional structures, and their arrangement within the hexadecamer has no intrinsic asymmetry. A detailed analysis of the high-resolution maps identified 30 differences in the sequence of the small subunit, indicating a larger than usual heterogeneity for this nuclear encoded protein in spinach. No such differences were found in the sequence of the chloroplast encoded large subunit. The transition state analogue is in the cis conformation at the active site suggesting a key role for the carbamate of Lys201 in catalysis. Analysis of the active site around the catalytically essential magnesium ion further indicates that residues in the second liganding sphere of the metal play a role in fine-tuning the acid-base character and the position of the residues directly liganded to the metal.
- 44Ramírez-Silva, L.; Hernández-Alcántara, G.; Guerrero-Mendiola, C.; González-Andrade, M.; Rodríguez-Romero, A.; Rodríguez-Hernández, A.; Lugo-Munguía, A.; Gómez-Coronado, P. A.; Rodríguez-Méndez, C.; Vega-Segura, A. The K+-Dependent and-Independent Pyruvate Kinases Acquire the Active Conformation by Different Mechanisms. Int. J. Mol. Sci. 2022, 23 (3), 1347, DOI: 10.3390/ijms23031347Google Scholar44https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XktFWgsr4%253D&md5=5e32d323774dcee725fd51a51e591659The K+-Dependent and -Independent Pyruvate Kinases Acquire the Active Conformation by Different MechanismsRamirez-Silva, Leticia; Hernandez-Alcantara, Gloria; Guerrero-Mendiola, Carlos; Gonzalez-Andrade, Martin; Rodriguez-Romero, Adela; Rodriguez-Hernandez, Annia; Lugo-Munguia, Alan; Gomez-Coronado, Paul A.; Rodriguez-Mendez, Cristina; Vega-Segura, AliciaInternational Journal of Molecular Sciences (2022), 23 (3), 1347CODEN: IJMCFK; ISSN:1422-0067. (MDPI AG)Eukarya pyruvate kinases possess glutamate at position 117 (numbering of rabbit muscle enzyme), whereas bacteria have either glutamate or lysine. Those with E117 are K+-dependent, whereas those with K117 are K+-independent. In a phylogenetic tree, 80% of the sequences with E117 are occupied by T113/K114/T120 and 77% of those with K117 possess L113/Q114/(L,I,V)120. This work aims to understand these residues' contribution to the K+-independent pyruvate kinases using the K+-dependent rabbit muscle enzyme. Residues 117 and 120 are crucial in the differences between the K+-dependent and -independent mutants. K+-independent activity increased with L113 and Q114 to K117, but L120 induced structural differences that inactivated the enzyme. T120 appears to be key in folding the protein and closure of the lid of the active site to acquire its active conformation in the K+-dependent enzymes. E117K mutant was K+-independent and the enzyme acquired the active conformation by a different mechanism. In the K+-independent apoenzyme of Mycobacterium tuberculosis, K72 (K117) flips out of the active site; in the holoenzyme, K72 faces toward the active site bridging the substrates through water mols. The results provide evidence that two different mechanisms have evolved for the catalysis of this reaction.
- 45Stec, B.; Hehir, M. J.; Brennan, C.; Nolte, M.; Kantrowitz, E. R. Kinetic and X-ray Structural Studies of Three Mutant E. coli Alkaline Phosphatases: Insights into the Catalytic Mechanism without the Nucleophile Ser102. J. Mol. Biol. 1998, 277 (3), 647– 662, DOI: 10.1006/jmbi.1998.1635Google Scholar45https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaK1cXjtFKlt7o%253D&md5=490c008bbf73d3cee60a1efde7e044fcKinetic and x-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102Stec, Boguslaw; Hehir, Michael J.; Brennan, Christopher; Nolte, Matthias; Kantrowitz, Evan R.Journal of Molecular Biology (1998), 277 (3), 647-662CODEN: JMOBAK; ISSN:0022-2836. (Academic Press Ltd.)Escherichia coli alk. phosphatase (EC 3.1.3.1) is a non-specific phosphomonoesterase that catalyzes the hydrolysis reaction via a phosphoseryl intermediate to produce inorg. phosphate and the corresponding alc. We investigated the nature of the primary nucleophile, fulfilled by the deprotonated Ser102, in the catalytic mechanism by mutating this residue to glycine, alanine and cysteine. The efficiencies of the S102G, S102A and S102C enzymes were 6 × 105-fold, 105-fold and 104-fold lower than the wild-type enzyme, resp., as measured by the kcat/Km ratio, still substantially higher than the non-catalyzed reaction. In order to investigate the structural details of the altered active site, the enzymes were crystd. and their structures detd. The enzymes crystd. in a new crystal form corresponding to the space group P6322. Each structure has phosphate at each active site and shows little departure from the wild-type model. For the S102G and S102A enzymes, the phosphate occupies the same position as in the wild-type enzyme, while in the S102C enzyme it is displaced by 2.5 Å. This kinetic and structural study suggests an explanation for differences in catalytic efficiency of the mutant enzymes and provides a means to study the nature and strength of different nucleophiles in the same environment. The anal. of these results provides insight into the mechanisms of other classes of phosphatases that do not utilize a serine nucleophile.
- 46Wang, X.; Wang, C.; Tang, J.; Dyda, F.; Zhang, X. C. The Crystal Structure of Bovine Bile Salt Activated Lipase: Insights into the Bile Salt Activation Mechanism. Structure 1997, 5 (9), 1209– 1218, DOI: 10.1016/S0969-2126(97)00271-2Google Scholar46https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaK2sXmslOnt7s%253D&md5=2f54b31d683f266ba7aa1fbadbb08624The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanismWang, Xiaoqiang; Wang, Chi-Sun; Tang, Jordan; Dyda, Fred; Zhang, Xuejun C.Structure (London) (1997), 5 (9), 1209-1218CODEN: STRUE6; ISSN:0969-2126. (Current Biology)The intestinally located pancreatic enzyme, bile-salt activated lipase (I), possesses unique activities for digesting different kinds of lipids. It also differs from other lipases in a requirement of bile salts for activity. A structure-based explanation for these unique properties has not been reached so far due to the absence of a 3-dimensional structure. Here, the crystal structures of bovine I and its complex with taurocholate were detd. at 2.8 Å resoln. The overall structure of I belonged to the α/β hydrolase fold family. Two bile salt binding sites were found in each I mol. within the I-taurocholate complex structure. One of these sites was located close to a hairpin loop near the active site. Upon the binding of taurocholate, this loop became less mobile and assumed a different conformation. The other bile salt binding site was located remote from the active site. In both structures, I formed similar dimers with the active sites facing each other. Bile salts activated I by binding to a relatively short 10-residue loop near the active site, and stabilized the loop in an open conformation. Presumably, this conformational change leads to the formation of the substrate-binding site, as suggested from kinetic data. The I dimer obsd. in the crystal structure may also play a functional role under physiol. conditions.
- 47Frankaer, C. G.; Mossin, S.; Ståhl, K.; Harris, P. Towards Accurate Structural Characterization of Metal Centres in Protein Crystals: The Structures of Ni and Cu T6 Bovine Insulin Derivatives. Acta Crystallogr., Sect. D Biol. Crystallogr. 2014, 70 (1), 110– 122, DOI: 10.1107/S1399004713029040Google Scholar47https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXlvFymsQ%253D%253D&md5=eef4a17dc83586ec0d2aa1a2a18cba40Towards accurate structural characterization of metal centres in protein crystals: the structures of Ni and Cu T6 bovine insulin derivativesFrankaer, Christian Grundahl; Mossin, Susanne; Stahl, Kenny; Harris, PernilleActa Crystallographica, Section D: Biological Crystallography (2014), 70 (1), 110-122CODEN: ABCRE6; ISSN:1399-0047. (International Union of Crystallography)Using synchrotron radiation (SR), the crystal structures of T6 bovine insulin complexed with Ni2+ and Cu2+ were solved to 1.50 and 1.45 Å resoln., resp. The level of detail around the metal centers in these structures was highly limited, and the coordination of water in Cu site II of the copper insulin deriv. was deteriorated as a consequence of radiation damage. To provide more detail, x-ray absorption spectroscopy (XAS) was used to improve the information level about metal coordination in each deriv. The nickel deriv. contains hexacoordinated Ni2+ with trigonal symmetry, whereas the copper deriv. contains tetragonally distorted hexacoordinated Cu2+ as a result of the Jahn-Teller effect, with a significantly longer coordination distance for one of the three water mols. in the coordination sphere. That the copper center is of type II was further confirmed by EPR. The coordination distances were refined from EXAFS with std. deviations within 0.01 Å. The insulin deriv. contg. Cu2+ is sensitive towards photoredn. when exposed to SR. During the redn. of Cu2+ to Cu+, the coordination geometry of copper changes towards lower coordination nos. Primary damage, i.e. photoredn., was followed directly by XANES as a function of radiation dose, while secondary damage as structural changes around the Cu atoms after exposure to different radiation doses was studied by crystallog. using a lab. diffractometer. Protection against photoredn. and subsequent radiation damage was carried out by solid embedment of Cu insulin in a saccharose matrix. At 100 K the photoredn. was suppressed by ∼15%, and it was suppressed by a further ∼30% on cooling the samples to 20 K.
- 48Fornea, A. P.; Brooks, S. D.; Dooley, J. B.; Saha, A. Heterogeneous Freezing of Ice on Atmospheric Aerosols Containing Ash, Soot, and Soil. J. Geophys. Res.: Atmos. 2009, 114 (13), D13201 DOI: 10.1029/2009JD011958Google ScholarThere is no corresponding record for this reference.
- 49Budke, C.; Koop, T. BINARY: An Optical Freezing Array for Assessing Temperature and Time Dependence of Heterogeneous Ice Nucleation. Atmos. Meas. Tech. 2015, 8 (2), 689– 703, DOI: 10.5194/amt-8-689-2015Google ScholarThere is no corresponding record for this reference.
- 50Alsante, A. N. Characterization of Marine Biogenic Atmospheric Ice Nucleating Particles. Doctoral Dissertation, Texas A&M University, College Station, TX, 2023.Google ScholarThere is no corresponding record for this reference.
- 51Vali, G. Quantitative Evaluation of Experimental Results and the Heterogeneous Freezing Nucleation of Supercooled Droplets. J. Atmos. Sci. 1971, 28 (3), 402– 409, DOI: 10.1175/1520-0469(1971)028<0402:QEOERA>2.0.CO;2Google ScholarThere is no corresponding record for this reference.
- 52Li, Y.; Lubchenko, V.; Vekilov, P. G. The Use of Dynamic Light Scattering and Brownian Microscopy to Characterize Protein Aggregation. Rev. Sci. Instrum. 2011, 82 (5), 053106, DOI: 10.1063/1.3592581Google Scholar52https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXms1Sltbo%253D&md5=284050378c4ea13c15105138dec78c8aThe use of dynamic light scattering and Brownian microscopy to characterize protein aggregationLi, Ye; Lubchenko, Vassiliy; Vekilov, Peter G.Review of Scientific Instruments (2011), 82 (5), 053106/1-053106/8CODEN: RSINAK; ISSN:0034-6748. (American Institute of Physics)Dynamic light scattering (DLS) is often used to monitor aggregation in protein solns. Here, the authors explore the veracity of the aggregate sizes, size distribution widths, concns., and lifetime resulting from DLS. The authors use as an example a soln. of the protein lysozyme in which dense liq. clusters of radius about 100 nm reproducibly exist. The authors compare the results of DLS to those of Brownian microscopy. The authors show that because of the 6th power dependence of the scattered light intensity on the size of the scatterers, DLS overestimates the mean size of the clusters. The factor of overestimation depends on the shape of the size distribution and is ∼1.6 × in the studied soln. The related underestimate of the cluster concn. is ∼10 ×. The CONTIN algorithm, often employed to process DLS data, may, in some instances, produce non-phys. results. The authors put forth an alternative method to det. the aggregates' sizes, concns., and vol. fractions. The authors show that DLS yields a reliable width of the cluster size distribution only if the cluster concn. is above 109 cm-3 and their vol. fraction is above 10-6. DLS yields a lower bound of the cluster lifetime, which may be orders of magnitude lower than the real one. (c) 2011 American Institute of Physics.
- 53Stetefeld, J.; McKenna, S. A.; Patel, T. R. Dynamic Light Scattering: A Practical Guide and Applications in Biomedical Sciences. Biophys. Rev. 2016, 8, 409– 427, DOI: 10.1007/s12551-016-0218-6Google Scholar53https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28Xhs1Gqs7bP&md5=468714b5413c92edb45e985fc32e8164Dynamic light scattering: a practical guide and applications in biomedical sciencesStetefeld, Jorg; McKenna, Sean A.; Patel, Trushar R.Biophysical Reviews (2016), 8 (4), 409-427CODEN: BRIECG; ISSN:1867-2450. (Springer)Dynamic light scattering (DLS), also known as photon correlation spectroscopy (PCS), is a very powerful tool for studying the diffusion behavior of macromols. in soln. The diffusion coeff., and hence the hydrodynamic radii calcd. from it, depends on the size and shape of macromols. In this review, we provide evidence of the usefulness of DLS to study the homogeneity of proteins, nucleic acids, and complexes of protein-protein or protein-nucleic acid prepns., as well as to study protein-small mol. interactions. Further, we provide examples of DLS's application both as a complementary method to anal. ultracentrifugation studies and as a screening tool to validate soln. scattering models using detd. hydrodynamic radii.
- 54Bhattacharjee, S. DLS and Zeta Potential─What They Are and What They Are Not?. J. Controlled Release 2016, 235, 337– 351, DOI: 10.1016/j.jconrel.2016.06.017Google Scholar54https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhtFOgt73O&md5=50555ae8bc84aff2dc92b1c2d24dcf80DLS and zeta potential - What they are and what they are not?Bhattacharjee, SouravJournal of Controlled Release (2016), 235 (), 337-351CODEN: JCREEC; ISSN:0168-3659. (Elsevier B.V.)A review. Adequate characterization of NPs (nanoparticles) is of paramount importance to develop well defined nanoformulations of therapeutic relevance. Detn. of particle size and surface charge of NPs are indispensable for proper characterization of NPs. DLS (dynamic light scattering) and ZP (zeta potential) measurements have gained popularity as simple, easy and reproducible tools to ascertain particle size and surface charge. Unfortunately, on practical grounds plenty of challenges exist regarding these two techniques including inadequate understanding of the operating principles and dealing with crit. issues like sample prepn. and interpretation of the data. As both DLS and ZP have emerged from the realms of phys. colloid chem. - it is difficult for researchers engaged in nanomedicine research to master these two techniques. Addnl., there is little literature available in drug delivery research which offers a simple, concise account on these techniques. This review tries to address this issue while providing the fundamental principles of these techniques, summarizing the core math. principles and offering practical guidelines on tackling commonly encountered problems while running DLS and ZP measurements. Finally, the review tries to analyze the relevance of these two techniques from translatory perspective.
- 55Worthy, S. E.; Kumar, A.; Xi, Y.; Yun, J.; Chen, J.; Xu, C.; Irish, V. E.; Amato, P.; Bertram, A. K. The effect of (NH4)2SO4 on the freezing properties of non-mineral dust ice-nucleating substances of atmospheric relevance. Atmos. Chem. Phys. 2021, 21 (19), 14631– 14648, DOI: 10.5194/acp-21-14631-2021Google Scholar55https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXitlKjur7M&md5=0ff59829015b7508e61d1ee215605fd0The effect of (NH4)2SO4 on the freezing properties of non-mineral dust ice-nucleating substances of atmospheric relevanceWorthy, Soleil E.; Kumar, Anand; Xi, Yu; Yun, Jingwei; Chen, Jessie; Xu, Cuishan; Irish, Victoria E.; Amato, Pierre; Bertram, Allan K.Atmospheric Chemistry and Physics (2021), 21 (19), 14631-14648CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)A wide range of materials including mineral dust, soil dust, and bioaerosols have been shown to act as ice nuclei in the atm. During atm. transport, these materials can become coated with inorg. and org. solutes which may impact their ability to nucleate ice. While a no. of studies have investigated the impact of solutes at low concns. on ice nucleation by mineral dusts, very few studies have examd. their impact on non-mineral dust ice nuclei. We studied the effect of dil. (NH4)2SO4 solns. (0.05 M) on immersion freezing of a variety of non-mineral dust ice-nucleating substances (INSs) including bacteria, fungi, sea ice diatom exudates, sea surface microlayer substances, and humic substances using the droplet-freezing technique. We also studied the effect of (NH4)2SO4 solns. (0.05 M) on the immersion freezing of several types of mineral dust particles for comparison purposes. (NH4)2SO4 had no effect on the median freezing temp. (ΔT50) of 9 of the 10 non-mineral dust materials tested. There was a small but statistically significant decrease in ΔT50 (-0.43 ± 0.19°C) for the bacteria Xanthomonas campestris in the presence of (NH4)2SO4 compared to pure water. Conversely, (NH4)2SO4 increased the median freezing temp. of four different mineral dusts (potassium-rich feldspar, Arizona Test Dust, kaolinite, montmorillonite) by 3 to 9°C and increased the ice nucleation active site d. per g of material (nm(T)) by a factor of ∼ 10 to ∼ 30. This significant difference in the response of mineral dust and non-mineral dust ice-nucleating substances when exposed to (NH4)2SO4 suggests that they nucleate ice and/or interact with (NH4)2SO4 via different mechanisms. This difference suggests that the relative importance of mineral dust to non-mineral dust particles for ice nucleation in mixed-phase clouds could potentially increase as these particles become coated with (NH4)2SO4 in the atm. This difference also suggests that the addn. of (NH4)2SO4 (0.05 M) to atm. samples of unknown compn. could potentially be used as an indicator or assay for the presence of mineral dust ice nuclei, although addnl. studies are still needed as a function of INS concn. to confirm the same trends are obsd. for different INS concns. than those used here. A comparison with results in the literature does suggest that our results may be applicable to a range of mineral dust and non-mineral dust INS concns.
- 56Forman, H. J.; Zhang, H.; Rinna, A. Glutathione: Overview of Its Protective Roles, Measurement, and Biosynthesis. Mol. Aspects Med. 2009, 30 (1), 1– 12, DOI: 10.1016/j.mam.2008.08.006Google Scholar56https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD1MXltFelurY%253D&md5=c1b1aa2b03389bf1434af0762df78fe1Glutathione: Overview of its protective roles, measurement, and biosynthesisForman, Henry Jay; Zhang, Hongqiao; Rinna, AlessandraMolecular Aspects of Medicine (2009), 30 (1-2), 1-12CODEN: MAMED5; ISSN:0098-2997. (Elsevier B.V.)This review is the introduction to a special issue concerning, glutathione (GSH), the most abundant low mol. wt. thiol compd. synthesized in cells. GSH plays crit. roles in protecting cells from oxidative damage and the toxicity of xenobiotic electrophiles, and maintaining redox homeostasis. Here, the functions and GSH and the sources of oxidants and electrophiles, the elimination of oxidants by redn. and electrophiles by conjugation with GSH are briefly described. Methods of assessing GSH status in the cells are also described. GSH synthesis and its regulation are addressed along with therapeutic approaches for manipulating GSH content that have been proposed. The purpose here is to provide a brief overview of some of the important aspects of glutathione metab. as part of this special issue that will provide a more comprehensive review of the state of knowledge regarding this essential mol.
- 57Pummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H. Suspendable Macromolecules Are Responsible for Ice Nucleation Activity of Birch and Conifer Pollen. Atmos Chem. Phys. 2012, 12 (5), 2541– 2550, DOI: 10.5194/acp-12-2541-2012Google Scholar57https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38Xpt12iurg%253D&md5=70cd2ea58dc1a2321693e52dde19b124Suspendable macromolecules are responsible for ice nucleation activity of birch and conifer pollenPummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H.Atmospheric Chemistry and Physics (2012), 12 (5), 2541-2550CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)The ice nucleation of bioaerosols (bacteria, pollen, spores, etc.) is a topic of growing interest, since their impact on ice cloud formation and thus on radiative forcing, an important parameter in global climate, is not yet fully understood. Here we show that pollen of different species strongly differ in their ice nucleation behavior. The av. freezing temps. in lab. expts. range from 240 to 255 K. As the most efficient nuclei (silver birch, Scots pine and common juniper pollen) have a distribution area up to the Northern timberline, their ice nucleation activity might be a cryoprotective mechanism. Far more intriguingly, it has turned out that water, which has been in contact with pollen and then been sepd. from the bodies, nucleates as good as the pollen grains themselves. The ice nuclei have to be easily-suspendable macromols. located on the pollen. Once extd., they can be distributed further through the atm. than the heavy pollen grains and so presumably augment the impact of pollen on ice cloud formation even in the upper troposphere. Our expts. lead to the conclusion that pollen ice nuclei, in contrast to bacterial and fungal ice nucleating proteins, are non-proteinaceous compds.
- 58Eickhoff, L.; Dreischmeier, K.; Zipori, A.; Sirotinskaya, V.; Adar, C.; Reicher, N.; Braslavsky, I.; Rudich, Y.; Koop, T. Contrasting Behavior of Antifreeze Proteins: Ice Growth Inhibitors and Ice Nucleation Promoters. J. Phys. Chem. Lett. 2019, 10 (5), 966– 972, DOI: 10.1021/acs.jpclett.8b03719Google Scholar58https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXivVOgtLg%253D&md5=e02f7d07b2094deefd6766805a619f95Contrasting Behavior of Antifreeze Proteins: Ice Growth Inhibitors and Ice Nucleation PromotersEickhoff, Lukas; Dreischmeier, Katharina; Zipori, Assaf; Sirotinskaya, Vera; Adar, Chen; Reicher, Naama; Braslavsky, Ido; Rudich, Yinon; Koop, ThomasJournal of Physical Chemistry Letters (2019), 10 (5), 966-972CODEN: JPCLCD; ISSN:1948-7185. (American Chemical Society)Several types of natural mols. interact specifically with ice crystals. Small antifreeze proteins (AFPs) adsorb to particular facets of ice crystals, thus inhibiting their growth, whereas larger ice-nucleating proteins (INPs) can trigger the formation of new ice crystals at temps. much higher than the homogeneous ice nucleation temp. of pure water. It has been proposed that both types of proteins interact similarly with ice and that, in principle, they may be able to exhibit both functions. Here we investigated two naturally occurring antifreeze proteins, one from fish, type-III AFP, and one from beetles, TmAFP. We show that in addn. to ice growth inhibition, both can also trigger ice nucleation above the homogeneous freezing temp., providing unambiguous exptl. proof for their contrasting behavior. Our anal. suggests that the predominant difference between AFPs and INPs is their mol. size, which is a very good predictor of their ice nucleation temp.
- 59Govindarajan, A. G.; Lindow, S. E. Size of Bacterial Ice-Nucleation Sites Measured in Situ by Radiation Inactivation Analysis. Proc. Natl. Acad. Sci. U. S. A. 1988, 85 (5), 1334– 1338, DOI: 10.1073/pnas.85.5.1334Google Scholar59https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaL1cXhs1ClsLk%253D&md5=4e45a4bda6b45a7fa1d505943c820ff1Size of bacterial ice-nucleation sites measured in situ by radiation inactivation analysisGovindarajan, Arepura G.; Lindow, Steven E.Proceedings of the National Academy of Sciences of the United States of America (1988), 85 (5), 1334-8CODEN: PNASA6; ISSN:0027-8424.Four bacterial species are known to catalyze ice formation at temps. just below 0°. To better understand the relation between the mol. structure of bacterial ice-nucleation site(s) and the quant. qual. features of the ice-nucleation-active phenotype, γ-radiation anal. was used to det. the in situ size of ice-nucleation sites in strains of Pseudomonas syringae and Erwinia herbicola and in Escherichia coli HB101 carrying the plasmid pICE1.1 (contg. a 4-kilobase DNA insert from P. syringae that confers ice-nucleation activity). Lyophilized cells of each bacterial strain were irradiated with a flux of γ-radiation from 0 to 10.2 Mrad (1 Mrad = 106 J/kg). Differential concns. of active ice nuclei decreased as a 1st-order function of radiation dose in all strains as temp. was decreased from -2° to -14° in 1° intervals. Sizes of ice nuclei were calcd. from the γ-radiation flux at which 37% of initial ice nuclei active within each 1° temp. interval remained. The min. mass of a functional ice nucleus, active only between -12° and -13°, was ∼150 kDa for all strains. The size of ice nuclei increased logarithmically with increasing temp. from -12° to -2°, where the estd. nucleant mass was 19,000 kDa. The ice nucleant in these 3 bacterial species may represent an oligomeric structure, composed at least in part of an ice gene product that can self-assoc. to assume many possible sizes.
- 60Vali, G.; DeMott, P. J.; Möhler, O.; Whale, T. F. Technical Note: A Proposal for Ice Nucleation Terminology. Atmos. Chem. Phys. 2015, 15 (18), 10263– 10270, DOI: 10.5194/acp-15-10263-2015Google Scholar60https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXhsFKjtLzM&md5=ab033699b6722f56dad8ab77b8a55399Technical note: a proposal for ice nucleation terminologyVali, G.; DeMott, P. J.; Mohler, O.; Whale, T. F.Atmospheric Chemistry and Physics (2015), 15 (18), 10263-10270CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Terminol. dealing with ice nucleation in the atm., in biol. systems, and in other areas has not kept pace with the growth of empirical evidence and the development of new ideas over recent decades. Ambiguities and misinterpretations could be seen in the literature. This paper offers a set of definitions for various terms in common use, adds some qualifications, and introduces some new ones. Input has been received on the interpretation of various terms from a fair no. of researchers; diverse views have been accommodated with some success. It is anticipated that the terminol. proposed here will be helpful both to those who adopt it and to those who wish to explain a different perspective.
- 61Marcolli, C.; Gedamke, S.; Peter, T.; Zobrist, B. Efficiency of Immersion Mode Ice Nucleation on Surrogates of Mineral Dust. Atmos. Chem. Phys. 2007, 7 (19), 5081– 5091, DOI: 10.5194/acp-7-5081-2007Google Scholar61https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD2sXhtlOnsrvO&md5=5ee33d2e099533fd3799da8e96465b80Efficiency of immersion mode ice nucleation on surrogates of mineral dustMarcolli, C.; Gedamke, S.; Peter, T.; Zobrist, B.Atmospheric Chemistry and Physics (2007), 7 (19), 5081-5091CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)A differential scanning calorimeter (DSC) was used to explore heterogeneous ice nucleation of emulsified aq. suspensions of two Arizona test dust (ATD) samples with particle diams. of nominally 0-3 and 0-7 μm, resp. Aq. suspensions with ATD concns. of 0.01-20 wt% have been investigated. The DSC thermograms exhibit a homogeneous and a heterogeneous freezing peak whose intensity ratios vary with the ATD concn. in the aq. suspensions. Homogeneous freezing temps. are in good agreement with recent measurements by other techniques. Depending on ATD concn., heterogeneous ice nucleation occurred at temps. as high as 256 K or down to the onset of homogeneous ice nucleation (237 K). For ATD-induced ice formation Classical Nucleation Theory (CNT) offers a suitable framework to parameterize nucleation rates as a function of temp., exptl. detd. ATD size, and emulsion droplet vol. distributions. The latter two quantities serve to est. the total heterogeneous surface area present in a droplet, whereas the suitability of an individual heterogeneous site to trigger nucleation is described by the compatibility function (or contact angle) in CNT. The intensity ratio of homogeneous to heterogeneous freezing peaks is in good agreement with the assumption that the ATD particles are randomly distributed amongst the emulsion droplets. The obsd. dependence of the heterogeneous freezing temps. on ATD concns. cannot be described by assuming a const. contact angle for all ATD particles, but requires the ice nucleation efficiency of ATD particles to be (log)normally distributed amongst the particles. Best quant. agreement is reached when explicitly assuming that high-compatibility sites are rare and that therefore larger particles have on av. more and better active sites than smaller ones. This anal. suggests that a particle has to have a diam. of at least 0.1 μm to exhibit on av. one active site.
- 62Wang, W.; Nema, S.; Teagarden, D. Protein Aggregation─Pathways and Influencing Factors. Int. J. Pharm. 2010, 390 (2), 89– 99, DOI: 10.1016/j.ijpharm.2010.02.025Google Scholar62https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3cXksFShtL8%253D&md5=bfd8e132dcfbe9d2fcaed1dd013c87c3Protein aggregation-Pathways and influencing factorsWang, Wei; Nema, Sandeep; Teagarden, DirkInternational Journal of Pharmaceutics (2010), 390 (2), 89-99CODEN: IJPHDE; ISSN:0378-5173. (Elsevier B.V.)A review. Proteins generally will tend to aggregate under a variety of environmental conditions in comparison with small drug mols. The extent of aggregation is dependent on many factors that can be broadly classified as intrinsic (primary, secondary, tertiary or quaternary structure) or extrinsic (environment in which protein is present, processing conditions, etc). These protein aggregates may exhibit less desirable characteristics like reduced or no biol. activity, potential for immunogenicity or other side effects. Protein aggregation remains one of the major challenges in the development and commercialization of biotechnol. products. This article is intended to review and discuss the latest understandings in protein aggregation pathways and the possible extrinsic factors that affect or control the protein aggregation process.
- 63Metskas, L. A.; Ortega, D.; Oltrogge, L. M.; Blikstad, C.; Lovejoy, D. R.; Laughlin, T. G.; Savage, D. F.; Jensen, G. J. Rubisco Forms a Lattice inside Alpha-Carboxysomes. Nat. Commun. 2022, 13 (1), 4863, DOI: 10.1038/s41467-022-32584-7Google Scholar63https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38Xit1Sltb%252FI&md5=e92fcf3bc8662a6d4d9e3a313d95bfd0Rubisco forms a lattice inside alpha-carboxysomesMetskas, Lauren Ann; Ortega, Davi; Oltrogge, Luke M.; Blikstad, Cecilia; Lovejoy, Derik R.; Laughlin, Thomas G.; Savage, David F.; Jensen, Grant J.Nature Communications (2022), 13 (1), 4863CODEN: NCAOBW; ISSN:2041-1723. (Nature Portfolio)Abstr.: Despite the importance of microcompartments in prokaryotic biol. and bioengineering, structural heterogeneity has prevented a complete understanding of their architecture, ultrastructure, and spatial organization. Here, we employ cryo-electron tomog. to image α-carboxysomes, a pseudo-icosahedral microcompartment responsible for carbon fixation. We have solved a high-resoln. subtomogram av. of the Rubisco cargo inside the carboxysome, and detd. the arrangement of the enzyme. We find that the H. neapolitanus Rubisco polymerizes in vivo, mediated by the small Rubisco subunit. These fibrils can further pack to form a lattice with six-fold pseudo-symmetry. This arrangement preserves freedom of motion and accessibility around the Rubisco active site and the binding sites for two other carboxysome proteins, CsoSCA (a carbonic anhydrase) and the disordered CsoS2, even at Rubisco concns. exceeding 800 μM. This characterization of Rubisco cargo inside the α-carboxysome provides insight into the balance between order and disorder in microcompartment organization.
- 64Guerrero-Mendiola, C.; Oria-Hernández, J.; Ramírez-Silva, L. Kinetics of the Thermal Inactivation and Aggregate Formation of Rabbit Muscle Pyruvate Kinase in the Presence of Trehalose. Arch. Biochem. Biophys. 2009, 490 (2), 129– 136, DOI: 10.1016/j.abb.2009.08.012Google Scholar64https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD1MXht1Ggt77E&md5=f7fc1331a659c91ff2338c0302150094Kinetics of the thermal inactivation and aggregate formation of rabbit muscle pyruvate kinase in the presence of trehaloseGuerrero-Mendiola, Carlos; Oria-Hernandez, Jesus; Ramirez-Silva, LeticiaArchives of Biochemistry and Biophysics (2009), 490 (2), 129-136CODEN: ABBIA4; ISSN:0003-9861. (Elsevier B.V.)In a previous study, the authors found that 30-40% DMSO induces the active conformation of rabbit muscle pyruvate kinase (PK). Because DMSO is known to perturb the structure and function of many proteins, the authors explored the effect of trehalose (I) on the kinetics of thermal inactivation and stability of PK; this is because I, in contrast to DMSO, is totally excluded from the hydration shell of proteins. The results showed that 600 mM I inhibited the activity of PK by ∼20% at 25°; however, I protected PK from thermal inactivation at 60°, increased the apparent Tm of unfolding by 7.2°, induced a more compact state, and stabilized its tetrameric structure. The inactivation process was irreversible due to the formation of protein aggregates. I diminished the rate of formation of intermediates with propensity to aggregate, but did not affect the extent of aggregation. Remarkably, I affected the aggregation process by inducing aggregates with amyloid-like characteristics.
- 65Jiménez, J. L.; Nettleton, E. J.; Bouchard, M.; Robinson, C. V.; Dobson, C. M.; Saibil, H. R. The Protofilament Structure of Insulin Amyloid Fibrils. Proc. Natl. Acad. Sci. U. S. A. 2002, 99 (14), 9196– 9201, DOI: 10.1073/pnas.142459399Google Scholar65https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD38XlsVGgsrc%253D&md5=7e8d178ee6fdb7966f63361cac817d88The protofilament structure of insulin amyloid fibrilsJimenez, Jose L.; Nettleton, Ewan J.; Bouchard, Mario; Robinson, Carol V.; Dobson, Christopher M.; Saibil, Helen R.Proceedings of the National Academy of Sciences of the United States of America (2002), 99 (14), 9196-9201CODEN: PNASA6; ISSN:0027-8424. (National Academy of Sciences)Under soln. conditions where the native state is destabilized, the largely helical polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-β structure. However, there is a lack of information relating the 4.8 Å β-strand repeat to the higher order assembly of amyloid fibrils. We have used cryo-electron microscopy (EM), combining single particle anal. and helical reconstruction, to characterize these fibrils and to study the three-dimensional (3D) arrangement of their component protofilaments. Low-resoln. 3D structures of fibrils contg. 2, 4, and 6 protofilaments reveal a characteristic, compact shape of the insulin protofilament. Considerations of protofilament packing indicate that the cross-β ribbon is composed of relatively flat β-sheets rather than being the highly twisted, β-coil structure previously suggested by anal. of globular protein folds. Comparison of the various fibril structures suggests that very small, local changes in β-sheet twist are important in establishing the long-range coiling of the protofilaments into fibrils of diverse morphol.
- 66Kallberg, Y.; Gustafsson, M.; Persson, B.; Thyberg, J.; Johansson, J. Prediction of Amyloid Fibril-Forming Proteins. J. Biol. Chem. 2001, 276 (16), 12945– 12950, DOI: 10.1074/jbc.M010402200Google Scholar66https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3MXjtFymsro%253D&md5=2a96d3ac44fdd2dd50e026ce51042b14Prediction of amyloid fibril-forming proteinsKallberg, Yvonne; Gustafsson, Magnus; Persson, Bengt; Thyberg, Johan; Johansson, JanJournal of Biological Chemistry (2001), 276 (16), 12945-12950CODEN: JBCHA3; ISSN:0021-9258. (American Society for Biochemistry and Molecular Biology)In Alzheimer's disease and spongiform encephalopathies proteins transform from their native states into fibrils. The authors find that several amyloid-forming proteins harbor an α-helix in a polypeptide segment that should form a β-strand according to secondary structure predictions. In 1324 nonredundant protein structures, 37 β-strands with ≥7 residues were predicted in segments where the exptl. detd. structures show helixes. These discordances include the prion protein (helix 2, positions 179-191), the Alzheimer amyloid β-peptide (Aβ, positions 16-23), and lung surfactant protein C (SP-C, positions 12-27). In addn., human coagulation factor XIII (positions 258-266), triacylglycerol lipase from Candida antarctica (positions 256-266), and D-alanyl-D-alanine transpeptidase from Streptomyces R61 (positions 92-106) contain a discordant helix. These proteins have not been reported to form fibrils but in this study were found to form fibrils in buffered saline at pH 7.4. By replacing valines in the discordant helical part of SP-C with leucines, an α-helix is found exptl. and by secondary structure predictions. This analog does not form fibrils under conditions where SP-C forms abundant fibrils. Likewise, when Aβ residues 14-23 are removed or changed to a nondiscordant sequence, fibrils are no longer formed. The authors propose that α-helix/β-strand-discordant stretches are assocd. with amyloid fibril formation.
- 67Zhou, X.-M.; Entwistle, A.; Zhang, H.; Jackson, A. P.; Mason, T. O.; Shimanovich, U.; Knowles, T. P. J.; Smith, A. T.; Sawyer, E. B.; Perrett, S. Self-Assembly of Amyloid Fibrils That Display Active Enzymes. ChemCatChem 2014, 6 (7), 1961– 1968, DOI: 10.1002/cctc.201402125Google Scholar67https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXptl2ksro%253D&md5=a4150f83efb8e92e82bdbd33aea526ecSelf-Assembly of Amyloid Fibrils That Display Active EnzymesZhou, Xiao-Ming; Entwistle, Aiman; Zhang, Hong; Jackson, Antony P.; Mason, Thomas O.; Shimanovich, Ulyana; Knowles, Tuomas P. J.; Smith, Andrew T.; Sawyer, Elizabeth B.; Perrett, SarahChemCatChem (2014), 6 (7), 1961-1968CODEN: CHEMK3; ISSN:1867-3880. (Wiley-VCH Verlag GmbH & Co. KGaA)Enzyme immobilization is an important strategy to enhance the stability and recoverability of enzymes and to facilitate the sepn. of enzymes from reaction products. However, enzyme purifn. followed by sep. chem. steps to allow immobilization on a solid support reduces the efficiency and yield of the active enzyme. Here we describe polypeptide constructs that self-assemble spontaneously into nanofibrils with fused active enzyme subunits displayed on the amyloid fibril surface. We measured the steady-state kinetic parameters for the appended enzymes in situ within fibrils and compare these with the identical protein constructs in soln. Finally, we demonstrated that the fibrils can be recycled and reused in functional assays both in conventional batch processes and in a continuous-flow microreactor.
- 68Garnham, C. P.; Campbell, R. L.; Walker, V. K.; Davies, P. L. Novel Dimeric β-Helical Model of an Ice Nucleation Protein with Bridged Active Sites. BMC Struct. Biol. 2011, 11 (1), 1– 12, DOI: 10.1186/1472-6807-11-36Google ScholarThere is no corresponding record for this reference.
- 69Qiu, Y.; Hudait, A.; Molinero, V. How Size and Aggregation of Ice-Binding Proteins Control Their Ice Nucleation Efficiency. J. Am. Chem. Soc. 2019, 141 (18), 7439– 7452, DOI: 10.1021/jacs.9b01854Google Scholar69https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXntlehsb0%253D&md5=69f5e714689808c09543511275bd615aHow Size and Aggregation of Ice-Binding Proteins Control Their Ice Nucleation EfficiencyQiu, Yuqing; Hudait, Arpa; Molinero, ValeriaJournal of the American Chemical Society (2019), 141 (18), 7439-7452CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)Organisms that thrive at cold temps. produce ice-binding proteins to manage the nucleation and growth of ice. Bacterial ice-nucleating proteins (INP) are typically large and form aggregates in the cell membrane, while insect hyperactive antifreeze proteins (AFP) are sol. and generally small. Expts. indicate that larger ice-binding proteins and their aggregates nucleate ice at warmer temps. Nevertheless, a quant. understanding of how size and aggregation of ice-binding proteins det. the temp. Thet at which proteins nucleate ice is still lacking. Here, we address this question using mol. simulations and nucleation theory. The simulations indicate that the 2.5 nm long antifreeze protein TmAFP nucleates ice at 2 ± 1 °C above the homogeneous nucleation temp., in good agreement with recent expts. We predict that the addn. of ice-binding loops to TmAFP increases Thet, but not enough to compete in efficiency with the bacterial INP. We implement an accurate procedure to det. Thet of surfaces of finite size using classical nucleation theory, and, after validating the theory against Thet of the proteins in mol. simulations, we use it to predict Thet of the INP of Ps. syringae as a function of the length and no. of proteins in the aggregates. We conclude that assemblies with at most 34 INP already reach the Thet = -2 °C characteristic of this bacterium. Interestingly, we find that Thet is a strongly varying nonmonotonic function of the distance between proteins in the aggregates. This indicates that, to achieve max. freezing efficiency, bacteria must exert exquisite, subangstrom control of the distance between INP in their membrane.
- 70Hudait, A.; Odendahl, N.; Qiu, Y.; Paesani, F.; Molinero, V. Ice-Nucleating and Antifreeze Proteins Recognize Ice through a Diversity of Anchored Clathrate and Ice-like Motifs. J. Am. Chem. Soc. 2018, 140 (14), 4905– 4912, DOI: 10.1021/jacs.8b01246Google Scholar70https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXlt1Kku7g%253D&md5=ede99e9416d945280adcc57d6453911aIce-Nucleating and Antifreeze Proteins Recognize Ice through a Diversity of Anchored Clathrate and Ice-like MotifsHudait, Arpa; Odendahl, Nathan; Qiu, Yuqing; Paesani, Francesco; Molinero, ValeriaJournal of the American Chemical Society (2018), 140 (14), 4905-4912CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)Cold-adapted organisms produce antifreeze proteins (AFPs) and ice-nucleating proteins (INPs) to prevent and promote ice formation. The crystal structure of hyperactive bacterial (Marinomonas primoryensis) MpAFP, suggested that this protein binds ice through an anchored clathrate motif. It is not known whether other hyperactive AFPs and INPs use the same motif to recognize or nucleate ice. Here, we used mol. dynamics (MD) simulations to elucidate the ice-binding motifs of hyperactive insect AFPs and a model INP of Pseudomonas syringae (Ps). We found that insect AFPs recognized ice through anchored clathrate motifs distinct from that of MpAFP. By performing MD simulations of ice nucleation by PsINP, we identified 2 distinct ice-binding sites on opposite sides of the β-helix. The ice-nucleating sequences identified in the MD simulations agreed with those previously proposed for the closely related INP of Pseudomonas borealis based on the structure of the protein. The MD simulations indicated that these sites have comparable ice nucleating efficiency, but distinct binding motifs, controlled by the amino acid sequence: one is anchored clathrate and the other ice-like. We conclude that anchored clathrate and ice-like motifs can be equally effective for binding proteins to ice and promoting ice nucleation.
- 71Pandey, R.; Usui, K.; Livingstone, R. A.; Fischer, S. A.; Pfaendtner, J.; Backus, E. H. G.; Nagata, Y.; Fröhlich-Nowoisky, J.; Schmüser, L.; Mauri, S.; Scheel, J. F.; Knopf, D. A.; Pöschl, U.; Bonn, M.; Weidner, T. Ice-Nucleating Bacteria Control the Order and Dynamics of Interfacial Water. Sci. Adv. 2016, 2 (4), e1501630 DOI: 10.1126/sciadv.1501630Google ScholarThere is no corresponding record for this reference.
- 72Roeters, S. J.; Golbek, T. W.; Bregnhøj, M.; Drace, T.; Alamdari, S.; Roseboom, W.; Kramer, G.; Šantl-Temkiv, T.; Finster, K.; Pfaendtner, J.; Woutersen, S.; Boesen, T.; Weidner, T. Ice-Nucleating Proteins Are Activated by Low Temperatures to Control the Structure of Interfacial Water. Nat. Commun. 2021, 12 (1), 1183, DOI: 10.1038/s41467-021-21349-3Google Scholar72https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXltFyju7o%253D&md5=d6c85611953ef60940e328827610e4ccIce-nucleating proteins are activated by low temperatures to control the structure of interfacial waterRoeters, Steven J.; Golbek, Thaddeus W.; Bregnhoej, Mikkel; Drace, Taner; Alamdari, Sarah; Roseboom, Winfried; Kramer, Gertjan; Santl-Temkiv, Tina; Finster, Kai; Pfaendtner, Jim; Woutersen, Sander; Boesen, Thomas; Weidner, TobiasNature Communications (2021), 12 (1), 1183CODEN: NCAOBW; ISSN:2041-1723. (Nature Research)Abstr.: Ice-nucleation active (INA) bacteria can promote the growth of ice more effectively than any other known material. Using specialized ice-nucleating proteins (INPs), they obtain nutrients from plants by inducing frost damage and, when airborne in the atm., they drive ice nucleation within clouds, which may affect global pptn. patterns. Despite their evident environmental importance, the mol. mechanisms behind INP-induced freezing have remained largely elusive. We investigate the structural basis for the interactions between water and the ice-nucleating protein InaZ from the INA bacterium Pseudomonas syringae. Using vibrational sum-frequency generation (SFG) and two-dimensional IR spectroscopy, we demonstrate that the ice-active repeats of InaZ adopt a β-helical structure in soln. and at water surfaces. In this configuration, interaction between INPs and water mols. imposes structural ordering on the adjacent water network. The obsd. order of water increases as the interface is cooled to temps. close to the m.p. of water. Exptl. SFG data combined with mol.-dynamics simulations and spectral calcns. show that InaZ reorients at lower temps. This reorientation can enhance water interactions, and thereby the effectiveness of ice nucleation.
- 73Aller, J. Y.; Radway, J. C.; Kilthau, W. P.; Bothe, D. W.; Wilson, T. W.; Vaillancourt, R. D.; Quinn, P. K.; Coffman, D. J.; Murray, B. J.; Knopf, D. A. Size-Resolved Characterization of the Polysaccharidic and Proteinaceous Components of Sea Spray Aerosol. Atmos. Environ. 2017, 154, 331– 347, DOI: 10.1016/j.atmosenv.2017.01.053Google Scholar73https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2sXislKjsrY%253D&md5=38679c7dc06d69fc4cc6413e090d3d97Size-resolved characterization of the polysaccharidic and proteinaceous components of sea spray aerosolAller, Josephine Y.; Radway, JoAnn C.; Kilthau, Wendy P.; Bothe, Dylan W.; Wilson, Theodore W.; Vaillancourt, Robert D.; Quinn, Patricia K.; Coffman, Derek J.; Murray, Benjamin J.; Knopf, Daniel A.Atmospheric Environment (2017), 154 (), 331-347CODEN: AENVEQ; ISSN:1352-2310. (Elsevier Ltd.)Dissolved org. polymers released by phytoplankton and bacteria abiol. self-assemble in surface ocean waters into nano-to micro-sized gels contg. polysaccharides, proteins, lipids and other components. These gels conc. in the sea surface microlayer (SML), where they can potentially contribute to sea spray aerosol (SSA). Sea spray is a major source of atm. aerosol mass over much of the earth's surface, and knowledge of its properties (including the amt. and nature of the org. content), size distributions and fluxes are fundamental for detg. its role in atm. chem. and climate. Using a cascade impactor, we collected size-fractionated aerosol particles from ambient air and from freshly generated Sea Sweep SSA in the western North Atlantic Ocean together with biol. and chem. characterization of subsurface and SML waters. Spectrophotometric methods were applied to quantify the polysaccharide-contg. transparent exopolymer (TEP) and protein-contg. Coomassie stainable material (CSM) in these particles and waters. This study demonstrates that both TEP and CSM in surface ocean waters are aerosolized with sea spray with the greatest total TEP assocd. with particles <180 nm in diam. and >5 000 nm. The higher concns. of TEP and CSM in particles >5 000 nm most likely reflects collection of microorganism cells and/or fragments. The greater concn. of CSM in larger size particles may also reflect greater stability of proteinaceous gels compared to polysaccharide-rich gels in surface waters and the SML. Both TEP and CSM were measured in the ambient marine air sample with concns. of 2.1 ± 0.16μg xanthan gum equiv. (XG eq.) m-3 and 14 ± 1.0μg bovine serum albumin equiv. (BSA eq.) m-3. TEP in Sea Sweep SSA averaged 4.7 ± 3.1μg XG eq. m-3 and CSM 8.6 ± 7.3μg BSA eq. m-3. This work shows the transport of marine biogenic material across the air-sea interface through primary particle emission and the first demonstration of particle size discriminated TEP and CSM characterization of SSA and ambient aerosol under field conditions.
- 74Alsante, A. N.; Thornton, D. C. O.; Brooks, S. D. Ocean Aerobiology. Front. Microbiol. 2021, 12, 764178 DOI: 10.3389/fmicb.2021.764178Google Scholar74https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BB2cfjtVSmtQ%253D%253D&md5=dabf1d381f8d0f3b7f021cccf8f3b194Ocean AerobiologyAlsante Alyssa N; Thornton Daniel C O; Brooks Sarah DFrontiers in microbiology (2021), 12 (), 764178 ISSN:1664-302X.Ocean aerobiology is defined here as the study of biological particles of marine origin, including living organisms, present in the atmosphere and their role in ecological, biogeochemical, and climate processes. Hundreds of trillions of microorganisms are exchanged between ocean and atmosphere daily. Within a few days, tropospheric transport potentially disperses microorganisms over continents and between oceans. There is a need to better identify and quantify marine aerobiota, characterize the time spans and distances of marine microorganisms' atmospheric transport, and determine whether microorganisms acclimate to atmospheric conditions and remain viable, or even grow. Exploring the atmosphere as a microbial habitat is fundamental for understanding the consequences of dispersal and will expand our knowledge of biodiversity, biogeography, and ecosystem connectivity across different marine environments. Marine organic matter is chemically transformed in the atmosphere, including remineralization back to CO2. The magnitude of these transformations is insignificant in the context of the annual marine carbon cycle, but may be a significant sink for marine recalcitrant organic matter over long (∼10(4) years) timescales. In addition, organic matter in sea spray aerosol plays a significant role in the Earth's radiative budget by scattering solar radiation, and indirectly by affecting cloud properties. Marine organic matter is generally a poor source of cloud condensation nuclei (CCN), but a significant source of ice nucleating particles (INPs), affecting the formation of mixed-phase and ice clouds. This review will show that marine biogenic aerosol plays an impactful, but poorly constrained, role in marine ecosystems, biogeochemical processes, and the Earth's climate system. Further work is needed to characterize the connectivity and feedbacks between the atmosphere and ocean ecosystems in order to integrate this complexity into Earth System models, facilitating future climate and biogeochemical predictions.
- 75Choi, J. H.; Jang, E.; Yoon, Y. J.; Park, J. Y.; Kim, T.-W.; Becagli, S.; Caiazzo, L.; Cappelletti, D.; Krejci, R.; Eleftheriadis, K.; Park, K.-T.; Jang, K. S. Influence of Biogenic Organics on the Chemical Composition of Arctic Aerosols. Global Biogeochem. Cycles 2019, 33 (10), 1238– 1250, DOI: 10.1029/2019GB006226Google Scholar75https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXhvFKrsbnK&md5=c1ad390ba5cd44c45d01c06f75345e3aInfluence of Biogenic Organics on the Chemical Composition of Arctic AerosolsChoi, J. H.; Jang, E.; Yoon, Y. J.; Park, J. Y.; Kim, T.-W.; Becagli, S.; Caiazzo, L.; Cappelletti, D.; Krejci, R.; Eleftheriadis, K.; Park, K.-T.; Jang, K. S.Global Biogeochemical Cycles (2019), 33 (10), 1238-1250CODEN: GBCYEP; ISSN:1944-9224. (Wiley-Blackwell)We use an ultrahigh-resoln. 15-T Fourier transform ion cyclotron resonance mass spectrometer to elucidate the compositional changes in Arctic org. aerosols collected at Ny-Ålesund, Svalbard, in May 2015. The Fourier transform ion cyclotron resonance mass spectrometer anal. of airborne org. matter provided information on the mol. compns. of aerosol particles collected during the Arctic spring period. The air mass transport history, combined with satellite-derived geog. information and chlorophyll concn. data, revealed that the mol. compns. of org. aerosols drastically differed depending on the origin of the potential source region. The protein and lignin compd. populations contributed more than 70% of the total intensity of assigned mols. when the air masses mainly passed over the ocean region. Interestingly, the intensity of microbe-derived orgs. (protein and carbohydrate compds.) was pos. correlated with the air mass exposure to phytoplankton biomass proxied as chlorophyll. Furthermore, the intensities of lignin and unsatd. hydrocarbon compds., typically derived from terrestrial vegetation, increased with an increase in the advection time of the air mass over the ocean domain. These results suggest that the accumulation of dissolved biogenic orgs. in the Arctic Ocean possibly derived from both phytoplankton and terrestrial vegetation could significantly influence the chem. properties of Arctic org. aerosols during a productive spring period. The interpretation of mol. changes in org. aerosols using an ultrahigh-resoln. mass spectrometer could provide deep insight for understanding org. aerosols in the atm. over the Arctic and the relationship of org. aerosols with biogeochem. processes in terms of aerosol formation and environmental changes.
- 76O’Sullivan, D.; Murray, B. J.; Ross, J. F.; Webb, M. E. The Adsorption of Fungal Ice-Nucleating Proteins on Mineral Dusts: A Reservoir of Atmospheric Ice-Nucleating Particles. Atmos. Chem. Phys. 2016, 16 (12), 7879– 7887, DOI: 10.5194/acp-16-7879-2016Google Scholar76https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28Xhs1Oqu7jJ&md5=ccbaf214158cfd675a663064c979c46bThe adsorption of fungal ice-nucleating proteins on mineral dusts: a terrestrial reservoir of atmospheric ice-nucleating particlesO'Sullivan, Daniel; Murray, Benjamin J.; Ross, James F.; Webb, Michael E.Atmospheric Chemistry and Physics (2016), 16 (12), 7879-7887CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)The occurrence of ice-nucleating particles (INPs) in our atm. has a profound impact on the properties and lifetime of supercooled clouds. To date, the identities, sources and abundances of particles capable of nucleating ice at relatively low supercoolings (T >-15 °C) remain enigmatic. While biomols. such as proteins and carbohydrates have been implicated as important high-temp. INPs, the lack of knowledge on the environmental fates of these species makes it difficult to assess their potential atm. impacts. Here we show that such nanoscale ice-nucleating proteins from a common soil-borne fungus (Fusarium avenaceum) preferentially bind to and confer their ice-nucleating properties to kaolinite. The ice-nucleating activity of the proteinaceous INPs is unaffected by adsorption to the clay, and once bound the proteins do not readily desorb, retaining much of the activity even after multiple washings with pure water. The atm. implications of the finding that biol. residues can confer their ice-nucleating ability to dust particles are discussed.
- 77Roulston, T. H.; Cane, J. H.; Buchmann, S. L. What Governs Protein Content of Pollen: Preferences, Pollen-Pistil Interactions, or Phylogeny?. Ecol. Monogr. 2000, 70 (4), 617– 643, DOI: 10.1890/0012-9615(2000)070[0617:WGPCOP]2.0.CO;2Google ScholarThere is no corresponding record for this reference.
- 78Hendrickson, B. N.; Alsante, A. N.; Brooks, S. D. Live Oak Pollen as a Source of Atmospheric Particles. Aerobiologia 2023, 39 (1), 51– 67, DOI: 10.1007/s10453-022-09773-4Google ScholarThere is no corresponding record for this reference.
- 79Orellana, M. V.; Matrai, P. A.; Leck, C.; Rauschenberg, C. D.; Lee, A. M.; Coz, E. Marine Microgels as a Source of Cloud Condensation Nuclei in the High Arctic. Proc. Natl. Acad. Sci. U. S. A. 2011, 108 (33), 13612– 13617, DOI: 10.1073/pnas.1102457108Google Scholar79https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXhtV2ms7jN&md5=c0c445fdccb5f9cf22ab0b0c6c3dcc19Marine microgels as a source of cloud condensation nuclei in the high ArcticOrellana, Monica V.; Matrai, Patricia A.; Leck, Caroline; Rauschenberg, Carlton D.; Lee, Allison M.; Coz, EstherProceedings of the National Academy of Sciences of the United States of America (2011), 108 (33), 13612-13617, S13612/1-S13612/4CODEN: PNASA6; ISSN:0027-8424. (National Academy of Sciences)Marine microgels play an important role in regulating ocean basin-scale biogeochem. dynamics. In this paper, we demonstrate that, in the high Arctic, marine gels with unique physicochem. characteristics originate in the org. material produced by ice algae and/or phytoplankton in the surface water. The polymers in this dissolved org. pool assembled faster and with higher microgel yields than at other latitudes. The reversible phase transitions shown by these Arctic marine gels, as a function of pH, dimethylsulfide, and dimethylsulfoniopropionate concns., stimulate the gels to attain sizes below 1 μm in diam. These marine gels were identified with an antibody probe specific toward material from the surface waters, sized, and quantified in airborne aerosol, fog, and cloud water, strongly suggesting that they dominate the available cloud condensation nuclei no. population in the high Arctic (north of 80° N) during the summer season. Knowledge about emergent properties of marine gels provides important new insights into the processes controlling cloud formation and radiative forcing, and links the biol. at the ocean surface with cloud properties and climate over the central Arctic Ocean and, probably, all oceans.
- 80Jassey, V. E. J.; Walcker, R.; Kardol, P.; Geisen, S.; Heger, T.; Lamentowicz, M.; Hamard, S.; Lara, E. Contribution of Soil Algae to the Global Carbon Cycle. New Phytol. 2022, 234 (1), 64– 76, DOI: 10.1111/nph.17950Google Scholar80https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XhtFektb%252FL&md5=5ee47536aa139ab6c9000c9e0bd92593Contribution of soil algae to the global carbon cycleJassey, Vincent E. J.; Walcker, Romain; Kardol, Paul; Geisen, Stefan; Heger, Thierry; Lamentowicz, Mariusz; Hamard, Samuel; Lara, EnriqueNew Phytologist (2022), 234 (1), 64-76CODEN: NEPHAV; ISSN:0028-646X. (Wiley-Blackwell)A review. Soil photoautotrophic prokaryotes and micro-eukaryotes - known as soil algae - are, together with heterotrophic microorganisms, a constitutive part of the microbiome in surface soils. Similar to plants, they fix atm. carbon (C) through photosynthesis for their own growth, yet their contribution to global and regional biogeochem. C cycling still remains quant. elusive. Here, we compiled an extensive dataset on soil algae to generate a better understanding of their distribution across biomes and predict their productivity at a global scale by means of machine learning modeling. We found that, on av., (5.5 ± 3.4) x 106 algae inhabit each gram of surface soil. Soil algal abundance esp. peaked in acidic, moist and vegetated soils. We est. that, globally, soil algae take up around 3.6 Pg C per yr, which corresponds to c. 6% of the net primary prodn. of terrestrial vegetation. We demonstrate that the C fixed by soil algae is crucial to the global C cycle and should be integrated into land-based efforts to mitigate C emissions.
- 81Rastelli, E.; Corinaldesi, C.; Dell’anno, A.; Lo Martire, M.; Greco, S.; Cristina Facchini, M.; Rinaldi, M.; O’Dowd, C.; Ceburnis, D.; Danovaro, R. Transfer of Labile Organic Matter and Microbes from the Ocean Surface to the Marine Aerosol: An Experimental Approach. Sci. Rep. 2017, 7 (1), 1– 10, DOI: 10.1038/s41598-017-10563-zGoogle Scholar81https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXhtlyhtrrK&md5=9cf1be99ffe93fc0dccc5566069f3519Transfer of labile organic matter and microbes from the ocean surface to the marine aerosol: an experimental approachRastelli, Eugenio; Corinaldesi, Cinzia; Dell'Anno, Antonio; Lo Martire, Marco; Greco, Silvestro; Cristina Facchini, Maria; Rinaldi, Matteo; O'Dowd, Colin; Ceburnis, Darius; Danovaro, RobertoScientific Reports (2017), 7 (1), 1-10CODEN: SRCEC3; ISSN:2045-2322. (Nature Research)Surface ocean bubble-bursting generates aerosols composed of microscopic salt-water droplets, enriched in marine org. matter. The org. fraction profoundly influences aerosols' properties, by scattering solar radiations and nucleating water particles. Still little is known on the biochem. and microbiol. compn. of these org. particles. In the present study, we exptl. simulated the bursting of bubbles at the seawater surface of the North-Eastern Atlantic Ocean, analyzing the org. materials and the diversity of the bacteria in the source-seawaters and in the produced aerosols. We show that, compared with seawater, the sub-micron aerosol particles were highly enriched in org. matter (up to 140,000x for lipids, 120,000x for proteins and 100,000x for carbohydrates). Also DNA, viruses and prokaryotes were significantly enriched (up to 30,000, 250 and 45x, resp.). The relative importance of the org. components in the aerosol did not reflect those in the seawater, suggesting their selective transfer. Mol. analyses indicate the presence of selective transfers also for bacterial genotypes, highlighting higher contribution of less abundant seawater bacterial taxa to the marine aerosol. Overall, our results open new perspectives in the study of microbial dispersal through marine aerosol and provide new insights for a better understanding of climate-regulating processes of global relevance.
- 82Schiffer, J. M.; Luo, M.; Dommer, A. C.; Thoron, G.; Pendergraft, M.; Santander, M. V.; Lucero, D.; Pecora De Barros, E.; Prather, K. A.; Grassian, V. H.; Amaro, R. E. Impacts of Lipase Enzyme on the Surface Properties of Marine Aerosols. J. Phys. Chem. Lett. 2018, 9 (14), 3839– 3849, DOI: 10.1021/acs.jpclett.8b01363Google Scholar82https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXhtFKlsr%252FN&md5=f30afeed06f7821398f3d4025c8fc8b6Impacts of Lipase Enzyme on the Surface Properties of Marine AerosolsSchiffer, J. M.; Luo, M.; Dommer, A. C.; Thoron, G.; Pendergraft, M.; Santander, M. V.; Lucero, D.; Pecora de Barros, E.; Prather, K. A.; Grassian, V. H.; Amaro, R. E.Journal of Physical Chemistry Letters (2018), 9 (14), 3839-3849CODEN: JPCLCD; ISSN:1948-7185. (American Chemical Society)Triacylglycerol lipases have recently been shown to be transferred from the ocean to the atm. in atm. sea spray aerosol (SSA). Lipases have the potential to alter the compn. of SSA, however the structure and properties of enzymes in the high salt, high ionic strength and low pH conditions found in SSA have never been explored. Here, we study the dynamics of Burkholderia cepacia triacylglycerol lipase (BCL) at SSA model surfaces comprised of palmitic acid and dipalmitoylphosphatidic acid (DPPA), two commonly found lipids at SSA surfaces. Surface adsorption Langmuir isotherm expts. and all-atom explicit solvent mol. dynamics simulations together illuminate how and why BCL expands the ordering of lipids at palmitic acid surfaces the most at pH <4 and the least in DPPA surfaces at pH 6. Taken together, these results represent a first glimpse into the complex interplay between lipid surface structure and protein dynamics within enzyme-contg. aerosols.
- 83Orellana, M. V.; Hansell, D. A. Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (RuBisCO): A Long-Lived Protein in the Deep Ocean. Limnol. Oceanogr. 2012, 57 (3), 826– 834, DOI: 10.4319/lo.2012.57.3.0826Google Scholar83https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38XhtVOmt77O&md5=6e4452aea99a0acdd54ab7bd7fb0f061Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): a long-lived protein in the deep oceanOrellana, Monica V.; Hansell, Dennis A.Limnology and Oceanography (2012), 57 (3), 826-834CODEN: LIOCAH; ISSN:0024-3590. (American Society of Limnology and Oceanography)We demonstrate that the distribution of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) in the deep North Pacific is a unique tracer for the accumulation of biochem. identifiable org. residue of the export flux. RuBisCO is found both dissolved and assembled in microgels in a dynamic gel-to-dissolved-to-gel continuum that may protect RuBisCO from degrdn. in the water column. High concns. are located below biol. productive equatorial and subarctic systems, and low concns. are assocd. with the subtropical gyre. RuBisCO tracks the advective transport of export products along deep circulation pathways of the ocean interior, serving as a quantifiable biochem. tracer of modern org. carbon exported to and resident in the deep ocean.
- 84Vlasak, J.; Ionescu, R. Fragmentation of monoclonal antibodies. mAbs 2011, 3 (3), 253– 263, DOI: 10.4161/mabs.3.3.15608Google Scholar84https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC3MnmtVShuw%253D%253D&md5=8dc0db491ca9207313bdd613771a18cbFragmentation of monoclonal antibodiesVlasak Josef; Ionescu RoxanamAbs (2011), 3 (3), 253-63 ISSN:.Fragmentation is a degradation pathway ubiquitously observed in proteins despite the remarkable stability of peptide bond; proteins differ only by how much and where cleavage occurs. The goal of this review is to summarize reports regarding the non-enzymatic fragmentation of the peptide backbone of monoclonal antibodies (mAbs). The sites in the polypeptide chain susceptible to fragmentation are determined by a multitude of factors. Insights are provided on the intimate chemical mechanisms that can make some bonds prone to cleavage due to the presence of specific side-chains. In addition to primary structure, the secondary, tertiary and quaternary structures have a significant impact in modulating the distribution of cleavage sites by altering local flexibility, accessibility to solvent or bringing in close proximity side chains that are remote in sequence. This review focuses on cleavage sites observed in the constant regions of mAbs, with special emphasis on hinge fragmentation. The mechanisms responsible for backbone cleavage are strongly dependent on pH and can be catalyzed by metals or radicals. The distribution of cleavage sites are different under acidic compared to basic conditions, with fragmentation rates exhibiting a minimum in the pH range 5 to 6; therefore, the overall fragmentation pattern observed for a mAb is a complex result of structural and solvent conditions. A critical review of the techniques used to monitor fragmentation is also presented; usually a compromise has to be made between a highly sensitive method with good fragment separation and the capability to identify the cleavage site. The effect of fragmentation on the function of a mAb must be evaluated on a case-by-case basis depending on whether cleavage sites are observed in the variable or constant regions, and on the mechanism of action of the molecule.
- 85Schuster, J.; Mahler, H. C.; Joerg, S.; Huwyler, J.; Mathaes, R. Analytical challenges assessing protein aggregation and fragmentation under physiologic conditions. J. Pharm. Sci. 2021, 110 (9), 3103– 3110, DOI: 10.1016/j.xphs.2021.04.014Google Scholar85https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXhsVKks77J&md5=7a4ca9a1aa06ee046dbb202ce59bc2b5Analytical Challenges Assessing Protein Aggregation and Fragmentation Under Physiologic ConditionsSchuster, Joachim; Mahler, Hanns-Christian; Joerg, Susanne; Huwyler, Joerg; Mathaes, RomanJournal of Pharmaceutical Sciences (Philadelphia, PA, United States) (2021), 110 (9), 3103-3110CODEN: JPMSAE; ISSN:0022-3549. (Elsevier Inc.)A review. Therapeutic proteins are administered by injection or infusion. After administration, the physiol. environment in the desired body compartment - fluid or tissue - can impact protein stability and lead to changes in the safety and/or efficacy profile. For example, protein aggregation and fragmentation are crit. quality attributes of the drug product and can occur after administration to patients. In this context, the in vivo stability of therapeutic proteins has gained increasing attention. However, in vivo protein aggregation and fragmentation are difficult to assess and have been rarely investigated. This mini-review summarizes anal. approaches to assess the stability of therapeutic proteins using simulated physiol. conditions. Furthermore, we discuss factors potentially causing in vivo protein aggregation, pptn., and fragmentation in complex biol. fluids. Different anal. approaches are evaluated with respect to their applicability and possible shortcomings when it comes to these degrdn. events in biol. fluids. Tracking protein stability in biol. fluids typically requires purifying or labeling the protein of interest to circumvent matrix interference of biol. fluids. Improved anal. methods are strongly needed to gain knowledge on in vivo protein aggregation and fragmentation. In vitro models can support the selection of lead candidates and accelerate the pre-clin. development of therapeutic proteins.
- 86Yang, A. S.; Honig, B. On the pH dependence of protein stability. J. Mol. Biol. 1993, 231 (2), 459– 474, DOI: 10.1006/jmbi.1993.1294Google Scholar86https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaK3sXkvV2nsL4%253D&md5=7334f6169de93d04c6168841fc597f4bOn the pH dependence of protein stabilityYang, An Suei; Honig, BarryJournal of Molecular Biology (1993), 231 (2), 459-74CODEN: JMOBAK; ISSN:0022-2836.The free energy contribution of ionizable groups to protein stability is treated here. A method is presented for the calcn. of the pH dependence of the denaturation free energy of a protein, which yields results that can be compared directly to expt. The first step in the treatment is the detn. of the av. charges of all the ionizable groups in both the folded and unfolded protein. An expression due to Tanford then relates the pH dependence of the unfolding free energy to the difference in net charge between the two states. In order to det. abs. rather than relative unfolding free energies, it is necessary to calc. the total contribution of ionizable groups to protein stability at some ref. pH. This is accomplished through a statistical mech. treatment similar to the one used previously in the calcn. of pKas. The treatment itself is rigorous but it suffers from uncertainties in the pKa calcns. Nevertheless, the overall shape of exptl. obsd. plots of denaturation free energy as a function of pH are exptl. well reproduced by the calcns. A no. of general conclusions that arise from the anal. are: (1) knowledge of titrn. curves and/or effective pKa values of ionizable groups in proteins is sufficient to calc. the pH dependence of the denaturation free energy with resp. to some ref. pH value. However, in order to calc. the abs. contribution of ionizable groups to protein stability, it is necessary to also know the intrinsic pKa of each group. This is defined as the pKa of a group in a hypothetical state of the protein where all other groups are neutral. (2) Due to desolvation effects, ionizable groups destabilize proteins, although the effect is strongly dependent on pH. There are however, strongly stabilizing pairwise Coulombic interactions on the surface of proteins. (3) Plots of stability vs. pH should not be interpreted in terms of a group whose pKa corresponds to the titrn. midpoint, but rather to a group with different pKas (that correspond approx. to the titrn. end points) in each state. (4) Any residual structure in the GuHCl-denatured state of proteins appears to have little effect on the pH dependence of stability. (5) PH-dependent unfolding, for example to the "molten globule" state, appears due to individual groups with anomalous pKas whose locations on the protein surface may det. the nature of the unfolded state.
- 87Weids, A. J.; Ibstedt, S.; Tamás, M. J.; Grant, C. M. Distinct Stress Conditions Result in Aggregation of Proteins with Similar Properties. Sci. Rep. 2016, 6 (1), 24554, DOI: 10.1038/srep24554Google Scholar87https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28Xmt1ensLs%253D&md5=b30ca7d5196760f8ec785573d97130ffDistinct stress conditions result in aggregation of proteins with similar propertiesWeids, Alan J.; Ibstedt, Sebastian; Tamas, Markus J.; Grant, Chris M.Scientific Reports (2016), 6 (), 24554CODEN: SRCEC3; ISSN:2045-2322. (Nature Publishing Group)Protein aggregation is the abnormal assocn. of proteins into larger aggregate structures which tend to be insol. This occurs during normal physiol. conditions and in response to age or stress-induced protein misfolding and denaturation. In this present study we have defined the range of proteins that aggregate in yeast cells during normal growth and after exposure to stress conditions including an oxidative stress (hydrogen peroxide), a heavy metal stress (arsenite) and an amino acid analog (azetidine-2-carboxylic acid). Our data indicate that these three stress conditions, which work by distinct mechanisms, promote the aggregation of similar types of proteins probably by lowering the threshold of protein aggregation. The proteins that aggregate during physiol. conditions and stress share several features; however, stress conditions shift the criteria for protein aggregation propensity. This suggests that the proteins in aggregates are intrinsically aggregation-prone, rather than being proteins which are affected in a stress-specific manner. We addnl. identified significant overlaps between stress aggregating yeast proteins and proteins that aggregate during ageing in yeast and C. elegans. We suggest that similar mechanisms may apply in disease- and non-disease settings and that the factors and components that control protein aggregation may be evolutionary conserved.
- 88Mauri, S.; Pandey, R.; Rzeznicka, I.; Lu, H.; Bonn, M.; Weidner, T. Bovine and Human Insulin Adsorption at Lipid Monolayers: A Comparison. Front Phys. 2015, 3, 51, DOI: 10.3389/fphy.2015.00051Google ScholarThere is no corresponding record for this reference.
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Abstract
Figure 1
Figure 1. 3D structures of proteins investigated in this study from the Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank (PDB) (https://www.rcsb.org/; Berman et al. (42)) of (a) RuBisCO (PDB ID 8RUC; Andersson (43)), (b) pyruvate kinase (PDB ID 7R6Y; Ramirez-Silva et al. (44)), (c) alkaline phosphatase (PDB ID 1ELX; Stec et al. (45)), (d) lipase (PDB ID 1AKN; Wang et al. (46)), and (e) insulin (PDB ID 4M4L; Frankaer et al. (47)). Each protein is shown from a front view. Each color represents a distinct protein subunit. 3D structures were reproduced under the Creative Commons CC0 1.0 Universal Public Domain Dedication.
Figure 2
Figure 2. Fraction of droplets frozen as a function of the temperature for each protein and peptide (n = 70–110) of (a) RuBisCO, (b) pyruvate kinase, (c) alkaline phosphatase, (d) lipase, (e) insulin, and (f) glutathione at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red) and the UHPLC water procedural blank (black). Data points represent the mean fraction frozen of the pooled data sets ± the 95% confidence limits.
Figure 3
Figure 3. Median freezing temperatures of each protein and peptide at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red) and the UHPLC water procedural blank (black). Data points show the median ± pooled standard deviation (n = 70–110).
Figure 4
Figure 4. Cumulative number of active sites per mass in milligrams as a function of the temperature [nm(T)] (n = 70–110) of RuBisCO (solid line) at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), and 2 × 10–3 mg mL–1 (green), pyruvate kinase (dashed line) at a concentration of 2 × 10–2 mg mL–1 (blue), alkaline phosphatase (dotted line) at a concentration of 2 × 10–1 mg mL–1 (purple), and insulin (dotted–dashed line) at a concentration of 2 × 10–4 mg mL–1 (orange). Only samples that were statistically warmer than the procedural blank are shown.
Figure 5
Figure 5. DLS spectra of protein solutions. Hydrodynamic diameter (Dh) distribution by intensity of (a) RuBisCO, (b) pyruvate kinase, (c) alkaline phosphatase, (d) lipase, and (e) insulin at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red). The dashed black line refers to the diameter of the protein molecule. Glutathione is too small to be detected by DLS. Note that the y-axis scale is different for each graph.
Figure 6
Figure 6. DLS spectra of protein solutions. Hydrodynamic diameter (Dh) distribution by volume-derived intensity of (a) RuBisCO, (b) pyruvate kinase, (c) alkaline phosphatase, (d) lipase, and (e) insulin at a concentration of 2 × 10–1 mg mL–1 (purple), 2 × 10–2 mg mL–1 (blue), 2 × 10–3 mg mL–1 (green), 2 × 10–4 mg mL–1 (orange), and 2 × 10–5 mg mL–1 (red). The dashed black line refers to the diameter of the protein molecule. Glutathione is too small to be detected by DLS. Note that the y-axis scale is different for each graph.
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- 5DeMott, P. J.; Prenni, A. J.; Liu, X.; Kreidenweis, S. M.; Petters, M. D.; Twohy, C. H.; Richardson, M. S.; Eidhammer, T.; Rogers, D. C. Predicting Global Atmospheric Ice Nuclei Distributions and Their Impacts on Climate. Proc. Natl. Acad. Sci. U. S. A. 2010, 107 (25), 11217– 11222, DOI: 10.1073/pnas.09108181075https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC3crktFOgtg%253D%253D&md5=7f4e5a242e7e2187872e05f413944d95Predicting global atmospheric ice nuclei distributions and their impacts on climateDeMott P J; Prenni A J; Liu X; Kreidenweis S M; Petters M D; Twohy C H; Richardson M S; Eidhammer T; Rogers D CProceedings of the National Academy of Sciences of the United States of America (2010), 107 (25), 11217-22 ISSN:.Knowledge of cloud and precipitation formation processes remains incomplete, yet global precipitation is predominantly produced by clouds containing the ice phase. Ice first forms in clouds warmer than -36 degrees C on particles termed ice nuclei. We combine observations from field studies over a 14-year period, from a variety of locations around the globe, to show that the concentrations of ice nuclei active in mixed-phase cloud conditions can be related to temperature and the number concentrations of particles larger than 0.5 microm in diameter. This new relationship reduces unexplained variability in ice nuclei concentrations at a given temperature from approximately 10(3) to less than a factor of 10, with the remaining variability apparently due to variations in aerosol chemical composition or other factors. When implemented in a global climate model, the new parameterization strongly alters cloud liquid and ice water distributions compared to the simple, temperature-only parameterizations currently widely used. The revised treatment indicates a global net cloud radiative forcing increase of approximately 1 W m(-2) for each order of magnitude increase in ice nuclei concentrations, demonstrating the strong sensitivity of climate simulations to assumptions regarding the initiation of cloud glaciation.
- 6Forster, P.; Storelvmo, T.; Armour, K.; Collins, W.; Dufresne, J.-L.; Frame, D.; Lunt, D. J.; Mauritsen, T.; Palmer, M. D.; Watanabe, M.; Wild, M.; Zhang, H. 2021: The Earth’s Energy Budget, Climate Feedbacks, and Climate Sensitivity. In Climate Change 2021: The Physical Science Basis. Contribution of Working Group I to the Sixth Assessment Report of the Intergovernmental Panel on Climate Change; Masson-Delmotte, V., Zhai, P., Pirani, A., Connors, S. L., Péan, C., Berger, S., Caud, N., Chen, Y., Goldfarb, L., Gomis, M. I., Huang, M., Leitzell, K., Lonnoy, E., Matthews, J. B. R., Maycock, T. K., Waterfield, T., Yelekçi, O., Yu, R., Zhou, B., Eds.; Cambridge University Press: Cambridge, U.K.; Chapter 7, pp 923– 1054, DOI: 10.1017/9781009157896.009 .There is no corresponding record for this reference.
- 7Atkinson, J. D.; Murray, B. J.; Woodhouse, M. T.; Whale, T. F.; Baustian, K. J.; Carslaw, K. S.; Dobbie, S.; O’Sullivan, D.; Malkin, T. L. The Importance of Feldspar for Ice Nucleation by Mineral Dust in Mixed-Phase Clouds. Nature 2013, 498 (7454), 355– 358, DOI: 10.1038/nature122787https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3sXpt1Crsb0%253D&md5=9bd48b451ea3605eca4376ef34ea420dThe importance of feldspar for ice nucleation by mineral dust in mixed-phase cloudsAtkinson, James D.; Murray, Benjamin J.; Woodhouse, Matthew T.; Whale, Thomas F.; Baustian, Kelly J.; Carslaw, Kenneth S.; Dobbie, Steven; O'Sullivan, Daniel; Malkin, Tamsin L.Nature (London, United Kingdom) (2013), 498 (7454), 355-358CODEN: NATUAS; ISSN:0028-0836. (Nature Publishing Group)The amt. of ice present in mixed-phase clouds, which contain both supercooled liq. water droplets and ice particles, affects cloud extent, lifetime, particle size and radiative properties. The freezing of cloud droplets can be catalyzed by the presence of aerosol particles known as ice nuclei. One of the most important ice nuclei is thought to be mineral dust aerosol from arid regions. It is generally assumed that clay minerals, which contribute approx. two-thirds of the dust mass, dominate ice nucleation by mineral dust, and many exptl. studies have therefore focused on these materials. Here we use an established droplet-freezing technique to show that feldspar minerals dominate ice nucleation by mineral dusts under mixed-phase cloud conditions, despite feldspar being a minor component of dust emitted from arid regions. We also find that clay minerals are relatively unimportant ice nuclei. Our results from a global aerosol model study suggest that feldspar ice nuclei are globally distributed and that feldspar particles may account for a large proportion of the ice nuclei in Earth's atm. that contribute to freezing at temps. below about -15 °C.
- 8Murray, B. J.; O’Sullivan, D.; Atkinson, J. D.; Webb, M. E. Ice Nucleation by Particles Immersed in Supercooled Cloud Droplets. Chem. Soc. Rev. 2012, 41 (19), 6519– 6554, DOI: 10.1039/c2cs35200a8https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38Xhtlaktr7L&md5=5a331f4c83c33d5d7a99d6dca8cf9b3fIce nucleation by particles immersed in supercooled cloud dropletsMurray, B. J.; O'Sullivan, D.; Atkinson, J. D.; Webb, M. E.Chemical Society Reviews (2012), 41 (19), 6519-6554CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. The formation of ice particles in the Earth's atm. strongly affects the properties of clouds and their impact on climate. Despite the importance of ice formation in detg. the properties of clouds, the Intergovernmental Panel on Climate Change (IPCC, 2007) was unable to assess the impact of atm. ice formation in their most recent report because our basic knowledge is insufficient. Part of the problem is the paucity of quant. information on the ability of various atm. aerosol species to initiate ice formation. Here we review and assess the existing quant. knowledge of ice nucleation by particles immersed within supercooled water droplets. We introduce aerosol species which have been identified in the past as potentially important ice nuclei and address their ice-nucleating ability when immersed in a supercooled droplet. We focus on mineral dusts, biol. species (pollen, bacteria, fungal spores and plankton), carbonaceous combustion products and volcanic ash. In order to make a quant. comparison we first introduce several ways of describing ice nucleation and then summarise the existing information according to the time-independent (singular) approxn. Using this approxn. in combination with typical atm. loadings, we est. the importance of ice nucleation by different aerosol types. According to these ests. we find that ice nucleation below about -15 °C is dominated by soot and mineral dusts. Above this temp. the only materials known to nucleate ice are biol., with quant. data for other materials absent from the literature. We conclude with a summary of the challenges our community faces.
- 9Gute, E.; Abbatt, J. P. D. Oxidative Processing Lowers the Ice Nucleation Activity of Birch and Alder Pollen. Geophys. Res. Lett. 2018, 45 (3), 1647– 1653, DOI: 10.1002/2017GL0763579https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXjsV2gtbg%253D&md5=9f493b50784831ba6c9eadcfa7b44ee8Oxidative Processing Lowers the Ice Nucleation Activity of Birch and Alder PollenGute, Ellen; Abbatt, Jonathan P. D.Geophysical Research Letters (2018), 45 (3), 1647-1653CODEN: GPRLAJ; ISSN:1944-8007. (Wiley-Blackwell)Pollen carry water extractable compds. with ice nucleating (IN) activity. This study investigates whether the hydroxyl radical, as the major atm. oxidant, can affect the IN activity of silver birch and gray alder subpollen particles under in-cloud conditions for deposition freezing mode conditions at 234 K. It is found that oxidn. increases the supersatn. ratio with respect to ice necessary for the onset of ice nucleation and decreases the fraction of particles which initiate ice nucleation. This redn. of IN activity under equiv. oxidn. conditions does not occur with a mineral dust sample (Arizona Test Dust). Chem. anal. of fresh and oxidized pollen material indicates a change of mol. structure with a loss of conjugation and an increase in oxidized functional groups, such as carbonyls. This is the first demonstration that in-cloud oxidn. may lower the IN abilities of biol. particles such as pollen.
- 10Matthews, B. H.; Alsante, A. N.; Brooks, S. D. Pollen Emissions of Subpollen Particles and Ice Nucleating Particles. ACS Earth Space Chem. 2023, 7 (6), 1207– 1218, DOI: 10.1021/acsearthspacechem.3c0001410https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3sXosFyks78%253D&md5=68ba49c1080130e06765bb2ddf308b6dPollen Emissions of Subpollen Particles and Ice Nucleating ParticlesMatthews, Brianna H.; Alsante, Alyssa N.; Brooks, Sarah D.ACS Earth and Space Chemistry (2023), 7 (6), 1207-1218CODEN: AESCCQ; ISSN:2472-3452. (American Chemical Society)Pollen grains significantly contribute to the aerosol population, and levels are predicted to increase in the future. Under humid atm. conditions, pollen grains can rupture creating pollen grain fragments referred to as subpollen particles (SPPs) which are dispersed into the atm. with wind. In this lab. study, SPP emission factors were detd. for ryegrass, Lolium sp., and giant ragweed,Ambrosia trifida, in terms of the no. of SPPs produced per pollen grain and the no. of SPPs produced per m2, which were compared to previously measured live oak,Quercus virginiana, emission factors. The SPP emission factors were 4.9 x 1013 ± 4.3 x 1013 SPPs per m2 for ryegrass, 1.3 x 1015 ± 1.1 x 1015 SPPs per m2 for giant ragweed, and 1.1 x 1015 ± 1.6 x 1015 SPPs per m2 for live oak. SPPs and whole pollen grains from these species were evaluated for their ice nucleation efficiency in immersion and contact mode freezing. Measurements of the ice nucleation efficiency indicate that SPPs are weakly effective INPs in immersion mode, but that pollen grains represent a source of moderately efficient INPs in immersion and contact modes.
- 11Burkart, J.; Gratzl, J.; Seifried, T. M.; Bieber, P.; Grothe, H. Isolation of Subpollen Particles (SPPs) of Birch: SPPs Are Potential Carriers of Ice Nucleating Macromolecules. Biogeosciences 2021, 18 (20), 5751– 5765, DOI: 10.5194/bg-18-5751-2021There is no corresponding record for this reference.
- 12Pummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H. Suspendable macromolecules are responsible for ice nucleation activity of birch and conifer pollen. Atmos. Chem. Phys. 2012, 12 (5), 2541– 2550, DOI: 10.5194/acp-12-2541-201212https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38Xpt12iurg%253D&md5=70cd2ea58dc1a2321693e52dde19b124Suspendable macromolecules are responsible for ice nucleation activity of birch and conifer pollenPummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H.Atmospheric Chemistry and Physics (2012), 12 (5), 2541-2550CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)The ice nucleation of bioaerosols (bacteria, pollen, spores, etc.) is a topic of growing interest, since their impact on ice cloud formation and thus on radiative forcing, an important parameter in global climate, is not yet fully understood. Here we show that pollen of different species strongly differ in their ice nucleation behavior. The av. freezing temps. in lab. expts. range from 240 to 255 K. As the most efficient nuclei (silver birch, Scots pine and common juniper pollen) have a distribution area up to the Northern timberline, their ice nucleation activity might be a cryoprotective mechanism. Far more intriguingly, it has turned out that water, which has been in contact with pollen and then been sepd. from the bodies, nucleates as good as the pollen grains themselves. The ice nuclei have to be easily-suspendable macromols. located on the pollen. Once extd., they can be distributed further through the atm. than the heavy pollen grains and so presumably augment the impact of pollen on ice cloud formation even in the upper troposphere. Our expts. lead to the conclusion that pollen ice nuclei, in contrast to bacterial and fungal ice nucleating proteins, are non-proteinaceous compds.
- 13Augustin, S.; Wex, H.; Niedermeier, D.; Pummer, B.; Grothe, H.; Hartmann, S.; Tomsche, L.; Clauss, T.; Voigtländer, J.; Ignatius, K.; Stratmann, F. Immersion freezing of birch pollen washing water. Atmos. Chem. Phys. 2013, 13 (21), 10989– 11003, DOI: 10.5194/acp-13-10989-201313https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXjtlKktA%253D%253D&md5=f8bd68e665963b756c0c5859a67c4206Immersion freezing of birch pollen washing waterAugustin, S.; Wex, H.; Niedermeier, D.; Pummer, B.; Grothe, H.; Hartmann, S.; Tomsche, L.; Clauss, T.; Voigtlaender, J.; Ignatius, K.; Stratmann, F.Atmospheric Chemistry and Physics (2013), 13 (21), 10989-11003CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Birch pollen grains are known to be ice nucleating active biol. particles. The ice nucleating activity has previously been tracked down to biol. macromols. that can be easily extd. from the pollen grains in water. In the present study, we investigated the immersion freezing behavior of these ice nucleating active (INA) macromols. Therefore we measured the frozen fractions of particles generated from birch pollen washing water as a function of temp. at the Leipzig Aerosol Cloud Interaction Simulator (LACIS). Two different birch pollen samples were considered, with one originating from Sweden and one from the Czech Republic. For the Czech and Swedish birch pollen samples, freezing was obsd. to start at -19 and -17 °C, resp. The fraction of frozen droplets increased for both samples down to -24°C. Further cooling did not increase the frozen fractions any more. Instead, a plateau formed at frozen fractions below 1. This fact could be used to det. the amt. of INA macromols. in the droplets examd. here, which in turn allowed for the detn. of nucleation rates for single INA macromols. The main differences between the Swedish birch pollen and the Czech birch pollen were obvious in the temp. range between -17 and -24 °C. In this range, a second plateau region could be seen for Swedish birch pollen. As we assume INA macromols. to be the reason for the ice nucleation, we concluded that birch pollen is able to produce at least two different types of INA macromols. We were able to derive parameterizations for the heterogeneous nucleation rates for both INA macromol. types, using two different methods: a simple exponential fit and the Soccer ball model. With these parameterization methods we were able to describe the ice nucleation behavior of single INA macromols. from both the Czech and the Swedish birch pollen.
- 14Knopf, D. A.; Alpert, P. A.; Wang, B.; Aller, J. Y. Stimulation of Ice Nucleation by Marine Diatoms. Nat. Geosci. 2011, 4 (2), 88– 90, DOI: 10.1038/ngeo103714https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXht1Wgt78%253D&md5=be00c72f42d6c1302c333bc0d13d07b9Stimulation of ice nucleation by marine diatomsKnopf, D. A.; Alpert, P. A.; Wang, B.; Aller, J. Y.Nature Geoscience (2011), 4 (2), 88-90CODEN: NGAEBU; ISSN:1752-0894. (Nature Publishing Group)Atm. aerosol particles serve as nuclei for ice-crystal formation. As such, these particles are crit. to the generation of cirrus clouds, which form from gas and liq. water. Atm. aerosols also initiate ice formation in warmer, mixed-phase clouds, where ice crystals coexist with aq. droplets. Biogenic aerosol particles of terrestrial origin, including bacteria and pollen, can act as ice nuclei. Whether biogenic particles of marine origin also act as ice nuclei has remained uncertain. We exposed the cosmopolitan planktonic diatom species Thalassiosira pseudonana to water vapor and supercooled aq. sodium chloride under typical tropospheric conditions conducive to cirrus-cloud formation. Ice nucleation was detd. using a controlled vapor cooling-stage microscope system. Under all conditions, diatoms initiated ice formation. The presence of diatoms in water increased the temp. for ice formation up to 13 K, and in aq. sodium chloride, ice formed at temps. up to 30 K higher than when diatoms were not present. In addn., diatoms initiated ice formation from water vapor at relative humidities as low as 65%. The rate of ice nucleation was rapid and independent of surface area. We suggest that marine biogenic particles such as diatoms help explain high values and seasonal variations in ice-nuclei concns. in subpolar regions.
- 15Wilbourn, E. K.; Thornton, D. C. O.; Ott, C.; Graff, J.; Quinn, P. K.; Bates, T. S.; Betha, R.; Russell, L. M.; Behrenfeld, M. J.; Brooks, S. D. Ice Nucleation by Marine Aerosols Over the North Atlantic Ocean in Late Spring. J. Geophys Res.: Atmos. 2020, 125 (4), e2019JD030913 DOI: 10.1029/2019JD030913There is no corresponding record for this reference.
- 16Wilson, T. W.; Ladino, L. A.; Alpert, P. A.; Breckels, M. N.; Brooks, I. M.; Browse, J.; Burrows, S. M.; Carslaw, K. S.; Huffman, J. A.; Judd, C.; Kilthau, W. P.; Mason, R. H.; McFiggans, G.; Miller, L. A.; Najera, J. J.; Polishchuk, E.; Rae, S.; Schiller, C. L.; Si, M.; Temprado, J. V.; Whale, T. F.; Wong, J. P. S.; Wurl, O.; Yakobi-Hancock, J. D.; Abbatt, J. P. D.; Aller, J. Y.; Bertram, A. K.; Knopf, D. A.; Murray, B. J. A Marine Biogenic Source of Atmospheric Ice-Nucleating Particles. Nature 2015, 525 (7568), 234– 238, DOI: 10.1038/nature1498616https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXhsVyrtb%252FK&md5=2712b8caacd91d6435cc8b1e99cf2504A marine biogenic source of atmospheric ice-nucleating particlesWilson, Theodore W.; Ladino, Luis A.; Alpert, Peter A.; Breckels, Mark N.; Brooks, Ian M.; Browse, Jo; Burrows, Susannah M.; Carslaw, Kenneth S.; Huffman, J. Alex; Judd, Christopher; Kilthau, Wendy P.; Mason, Ryan H.; McFiggans, Gordon; Miller, Lisa A.; Najera, Juan J.; Polishchuk, Elena; Rae, Stuart; Schiller, Corinne L.; Si, Meng; Temprado, Jesus Vergara; Whale, Thomas F.; Wong, Jenny P. S.; Wurl, Oliver; Yakobi-Hancock, Jacqueline D.; Abbatt, Jonathan P. D.; Aller, Josephine Y.; Bertram, Allan K.; Knopf, Daniel A.; Murray, Benjamin J.Nature (London, United Kingdom) (2015), 525 (7568), 234-238CODEN: NATUAS; ISSN:0028-0836. (Nature Publishing Group)The amt. of ice present in clouds can affect cloud lifetime, pptn. and radiative properties. The formation of ice in clouds is facilitated by the presence of airborne ice-nucleating particles. Sea spray is one of the major global sources of atm. particles, but it is unclear to what extent these particles are capable of nucleating ice. Sea-spray aerosol contains large amts. of org. material that is ejected into the atm. during bubble bursting at the organically enriched sea-air interface or sea surface microlayer. Here we show that org. material in the sea surface microlayer nucleates ice under conditions relevant for mixed-phase cloud and high-altitude ice cloud formation. The ice-nucleating material is probably biogenic and less than approx. 0.2 μm in size. We find that exudates sepd. from cells of the marine diatom Thalassiosira pseudonana nucleate ice, and propose that org. material assocd. with phytoplankton cell exudates is a likely candidate for the obsd. ice-nucleating ability of the microlayer samples. Global model simulations of marine org. aerosol, in combination with our measurements, suggest that marine org. material may be an important source of ice-nucleating particles in remote marine environments such as the Southern Ocean, North Pacific Ocean and North Atlantic Ocean.
- 17Tesson, S. V.; Šantl-Temkiv, T. Ice nucleation activity and aeolian dispersal success in airborne and aquatic microalgae. Front. Microbiol. 2018, 9, 2681, DOI: 10.3389/fmicb.2018.0268117https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BB3crlsVOjsA%253D%253D&md5=f724891fabb1f0031495291e16b77075Ice Nucleation Activity and Aeolian Dispersal Success in Airborne and Aquatic MicroalgaeTesson Sylvie V M; Santl-Temkiv Tina; Santl-Temkiv Tina; Santl-Temkiv TinaFrontiers in microbiology (2018), 9 (), 2681 ISSN:1664-302X.Microalgae are common members of the atmospheric microbial assemblages. Diverse airborne microorganisms are known to produce ice nucleation active (INA) compounds, which catalyze cloud and rain formation, and thus alter cloud properties and their own deposition patterns. While the role of INA bacteria and fungi in atmospheric processes receives considerable attention, the numerical abundance and the capacity for ice nucleation in atmospheric microalgae are understudied. We isolated 81 strains of airborne microalgae from snow samples and determined their taxonomy by sequencing their ITS markers, 18S rRNA genes or 23S rRNA genes. We studied ice nucleation activity of airborne isolates, using droplet freezing assays, and their ability to withstand freezing. For comparison, we investigated 32 strains of microalgae from a culture collection, which were isolated from polar and temperate aqueous habitats. We show that ∼17% of airborne isolates, which belonged to taxa Trebouxiphyceae, Chlorophyceae and Stramenopiles, were INA. A large fraction of INA strains (over 40%) had ice nucleation activity at temperatures ≥-6°C. We found that 50% of aquatic microalgae were INA, but the majority were active at temperatures <-12°C. Most INA compounds produced by microalgae were proteinaceous and associated with the cells. While there were no deleterious effects of freezing on the viability of airborne microalgae, some of the aquatic strains were killed by freezing. In addition, the effect of desiccation was investigated for the aquatic strains and was found to constitute a limiting factor for their atmospheric dispersal. In conclusion, airborne microalgae possess adaptations to atmospheric dispersal, in contrast to microalgae isolated from aquatic habitats. We found that widespread taxa of both airborne and aquatic microalgae were INA at warm, sub-zero temperatures (>-15°C) and may thus participate in cloud and precipitation formation.
- 18Failor, K. C.; Schmale, D. G.; Vinatzer, B. A.; Monteil, C. L. Ice Nucleation Active Bacteria in Precipitation Are Genetically Diverse and Nucleate Ice by Employing Different Mechanisms. ISME J. 2017, 11 (12), 2740– 2753, DOI: 10.1038/ismej.2017.12418https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC1cfitV2isg%253D%253D&md5=cdde9817415ab4cdf085132adf4cfbeeIce nucleation active bacteria in precipitation are genetically diverse and nucleate ice by employing different mechanismsFailor K C; Schmale D G 3rd; Vinatzer B A; Monteil C L; Monteil C L; Monteil C LThe ISME journal (2017), 11 (12), 2740-2753 ISSN:.A growing body of circumstantial evidence suggests that ice nucleation active (Ice(+)) bacteria contribute to the initiation of precipitation by heterologous freezing of super-cooled water in clouds. However, little is known about the concentration of Ice(+) bacteria in precipitation, their genetic and phenotypic diversity, and their relationship to air mass trajectories and precipitation chemistry. In this study, 23 precipitation events were collected over 15 months in Virginia, USA. Air mass trajectories and water chemistry were determined and 33 134 isolates were screened for ice nucleation activity (INA) at -8 °C. Of 1144 isolates that tested positive during initial screening, 593 had confirmed INA at -8 °C in repeated tests. Concentrations of Ice(+) strains in precipitation were found to range from 0 to 13 219 colony forming units per liter, with a mean of 384±147. Most Ice(+) bacteria were identified as members of known and unknown Ice(+) species in the Pseudomonadaceae, Enterobacteriaceae and Xanthomonadaceae families, which nucleate ice employing the well-characterized membrane-bound INA protein. Two Ice(+) strains, however, were identified as Lysinibacillus, a Gram-positive genus not previously known to include Ice(+) bacteria. INA of the Lysinibacillus strains is due to a nanometer-sized molecule that is heat resistant, lysozyme and proteinase resistant, and secreted. Ice(+) bacteria and the INA mechanisms they employ are thus more diverse than expected. We discuss to what extent the concentration of culturable Ice(+) bacteria in precipitation and the identification of a new heat-resistant biological INA mechanism support a role for Ice(+) bacteria in the initiation of precipitation.
- 19Ladino, L. A.; Yakobi-Hancock, J. D.; Kilthau, W. P.; Mason, R. H.; Si, M.; Li, J.; Miller, L. A.; Schiller, C. L.; Huffman, J. A.; Aller, J. Y.; Knopf, D. A.; Bertram, A. K.; Abbatt, J. P. D. Addressing the Ice Nucleating Abilities of Marine Aerosol: A Combination of Deposition Mode Laboratory and Field Measurements. Atmos. Environ. 2016, 132, 1– 10, DOI: 10.1016/j.atmosenv.2016.02.02819https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XjtlCgu7c%253D&md5=02b56d9f5bbe2687ee3fbba03e663c14Addressing the ice nucleating abilities of marine aerosol: A combination of deposition mode laboratory and field measurementsLadino, L. A.; Yakobi-Hancock, J. D.; Kilthau, W. P.; Mason, R. H.; Si, M.; Li, J.; Miller, L. A.; Schiller, C. L.; Huffman, J. A.; Aller, J. Y.; Knopf, D. A.; Bertram, A. K.; Abbatt, J. P. D.Atmospheric Environment (2016), 132 (), 1-10CODEN: AENVEQ; ISSN:1352-2310. (Elsevier Ltd.)This study addresses, through two types of expts., the potential for the oceans to act as a source of atm. ice-nucleating particles (INPs). The INP concn. via deposition mode nucleation was measured in situ at a coastal site in British Columbia in August 2013. The INP concn. at conditions relevant to cirrus clouds (i.e., -40 °C and relative humidity with respect to ice, RHice = 139%) ranged from 0.2 L-1 to 3.3 L-1. Correlations of the INP concns. with levels of anthropogenic tracers (i.e., CO, SO2, NOx, and black carbon) and nos. of fluorescent particles do not indicate a significant influence from anthropogenic sources or submicron bioaerosols, resp. Addnl., the INPs measured in the deposition mode showed a poor correlation with the concn. of particles with sizes larger than 500 nm, which is in contrast with observations made in the immersion freezing mode. To investigate the nature of particles that could have acted as deposition INP, lab. expts. with potential marine aerosol particles were conducted under the ice-nucleating conditions used in the field. At -40 °C, no deposition activity was obsd. with salt aerosol particles (sodium chloride and two forms of com. sea salt: Sigma-Aldrich and Instant Ocean), particles composed of a com. source of natural org. matter (Suwannee River humic material), or particle mixts. of sea salt and humic material. In contrast, exudates from three phytoplankton (Thalassiosira pseudonana, Nanochloris atomus, and Emiliania huxleyi) and one marine bacterium (Vibrio harveyi) exhibited INP activity at low RHice values, down to below 110%. This suggests that the INPs measured at the field site were of marine biol. origins, although we cannot rule out other sources, including mineral dust.
- 20Maki, L. R.; Galyan, E. L.; Chang-Chien, M. M.; Caldwell, D. R. Ice Nucleation Induced by Pseudomonas Syringae. Appl. Microbiol. 1974, 28 (3), 456– 459, DOI: 10.1128/am.28.3.456-459.197420https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADyaE2M%252FivFGqtA%253D%253D&md5=ae0521124cc7fbba3e20bbf344a43d0fIce nucleation induced by pseudomonas syringaeMaki L R; Galyan E L; Chang-Chien M M; Caldwell D RApplied microbiology (1974), 28 (3), 456-9 ISSN:0003-6919.Broth cultures of suspensions of Pseudomonas syringae isolated from decaying alder leaves (Alnus tenuifolia) were found to freeze at very warm (-1.8 to -3.8 C) temperatures. The initiation of freezing appears associated with the intact cell and not with extracellular material. Chemical treatments and physical destruction of the cell destroy activity. Bacteria must be in concentrations of approximately 10(6)/ml before freezing at warm temperatures occurs.
- 21Šantl-Temkiv, T.; Sahyoun, M.; Finster, K.; Hartmann, S.; Augustin-Bauditz, S.; Stratmann, F.; Wex, H.; Clauss, T.; Nielsen, N. W.; Sørensen, J. H.; Korsholm, U. S.; Wick, L. Y.; Karlson, U. G. Characterization of airborne ice-nucleation-active bacteria and bacterial fragments. Atmos. Environ. 2015, 109, 105– 117, DOI: 10.1016/j.atmosenv.2015.02.06021https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXjsFWru7o%253D&md5=8a7d5ff5a4f29ea8bc4a21a19b21f91cCharacterization of airborne ice-nucleation-active bacteria and bacterial fragmentsSantl-Temkiv, Tina; Sahyoun, Maher; Finster, Kai; Hartmann, Susan; Augustin-Bauditz, Stefanie; Stratmann, Frank; Wex, Heike; Clauss, Tina; Nielsen, Niels Woetmann; Soerensen, Jens Havskov; Korsholm, Ulrik Smith; Wick, Lukas Y.; Karlson, Ulrich GosewinkelAtmospheric Environment (2015), 109 (), 105-117CODEN: AENVEQ; ISSN:1352-2310. (Elsevier Ltd.)Some bacteria have the unique capacity of synthesizing ice-nucleation-active (INA) proteins and exposing them at their outer membrane surface. As INA bacteria enter the atm., they may impact the formation of clouds and pptn. We studied members of airborne bacterial communities for their capacity to catalyze ice formation and we report on the excretion of INA proteins by airborne Pseudomonas sp. We also obsd. for the first time that INA biol. fragments <220 nm were present in pptn. samples (199 and 482 INA fragments per L of pptn.), which confirms the presence of submicron INA biol. fragments in the atm. During 14 pptn. events, strains affiliated with the genus Pseudomonas, which are known to carry ina genes, were dominant. A screening for INA properties revealed that ∼12% of the cultivable bacteria caused ice formation at ≤-7 °C. They had likely been emitted to the atm. from terrestrial surfaces, e.g. by convective transport. We tested the ability of isolated INA strains to produce outer membrane vesicles and found that two isolates could do so. However, only very few INA vesicles were released per INA cell. Thus, the source of the submicron INA proteinaceous particles that we detected in the atm. remains to be elucidated.
- 22Creamean, J. M.; Ceniceros, J. E.; Newman, L.; Pace, A. D.; Hill, T. C. J.; Demott, P. J.; Rhodes, M. E. Evaluating the Potential for Haloarchaea to Serve as Ice Nucleating Particles. Biogeosciences 2021, 18 (12), 3751– 3762, DOI: 10.5194/bg-18-3751-202122https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXis1ynsrjO&md5=e379fb956036c55e014dd5ccd2a8c354Evaluating the potential for Haloarchaea to serve as ice nucleating particlesCreamean, Jessie M.; Ceniceros, Julio E.; Newman, Lilyanna; Pace, Allyson D.; Hill, Thomas C. J.; DeMott, Paul J.; Rhodes, Matthew E.Biogeosciences (2021), 18 (12), 3751-3762CODEN: BIOGGR; ISSN:1726-4189. (Copernicus Publications)Aerosols play a crucial role in cloud formation. Biol. derived materials from bacteria, fungi, pollen, lichen, viruses, algae, and diatoms can serve as ice nucleating particles (INPs), some of which initiate glaciation in clouds at relatively warm freezing temps. However, detg. the magnitude of the interactions between clouds and biol. derived INPs remains a significant challenge due to the diversity and complexity of bioaerosols and limited observations of such aerosols facilitating cloud ice formation. Addnl., microorganisms from the domain Archaea have, to date, not been evaluated as INPs. Here, we present the first results reporting the ice nucleation activity of four species in the class Haloarchaea. Intact cells of Halococcus morrhuae and Haloferax sulfurifontis demonstrated the ability to induce immersion freezing at temps. up to -18 °C, while lysed cells of Haloquadratum walsbyi and Natronomonas pharaonis were unable to serve as immersion INPs. Exposure to heat and peroxide digestion indicated that the INPs of intact cells were driven by org. (H. morrhuae and H. sulfurifontis) and possibly also heat labile materials (H. sulfurifontis only). While halophiles are prominent in hypersaline environments such as the Great Salt Lake and the Dead Sea, other members of the Archaea, such as methanogens and thermophiles, are prevalent in anoxic systems in seawater, sea ice, marine sediments, glacial ice, permafrost, and other cold niches. Archaeal extremophiles are both diverse and highly abundant. Thus, it is important to assess their ability to serve as INPs as it may lead to an improved understanding of biol. impacts on clouds.
- 23Hill, T. C. J.; DeMott, P. J.; Tobo, Y.; Fröhlich-Nowoisky, J.; Moffett, B. F.; Franc, G. D.; Kreidenweis, S. M. Sources of Organic Ice Nucleating Particles in Soils. Atmos. Chem. Phys. 2016, 16 (11), 7195– 7211, DOI: 10.5194/acp-16-7195-201623https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhslKqt77I&md5=3196772bd5761b3adbd4da0d67f32ae4Sources of organic ice nucleating particles in soilsHill, Tom C. J.; DeMott, Paul J.; Tobo, Yutaka; Frohlich-Nowoisky, Janine; Moffett, Bruce F.; Franc, Gary D.; Kreidenweis, Sonia M.Atmospheric Chemistry and Physics (2016), 16 (11), 7195-7211CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Soil org. matter (SOM) may be a significant source of atm. ice nucleating particles (INPs), esp. of those active >-15 °C. However, due to both a lack of investigations and the complexity of the SOM itself, the identities of these INPs remain unknown. To more comprehensively characterize org. INPs we tested locally representative soils in Wyoming and Colorado for total org. INPs, INPs in the heat-labile fraction, ice nucleating (IN) bacteria, IN fungi, IN fulvic and humic acids, IN plant tissue, and ice nucleation by monolayers of aliph. alcs. All soils contained ≈106 to ≈5×107 INPs g-1 dry soil active at -10 °C. Removal of SOM with H2O2 removed ≥99% of INPs active >-18 °C (the limit of testing), while heating of soil suspensions to 105 °C showed that labile INPs increasingly predominated >-12 °C and comprised ≥90%of INPs active >-9 °C. Papain protease, which inactivates IN proteins produced by the fungus Mortierella alpina, common in the region's soils, lowered INPs active at ≥-11 °C by _75% in two arable soils and in sagebrush shrubland soil. By contrast, lysozyme, which digests bacterial cell walls, only reduced INPs active at ≥-7.5 or ≥-6 °C, depending on the soil. The known IN bacteria were not detected in any soil, using PCR for the ina gene that codes for the active protein. We directly isolated and photographed two INPs from soil, using repeated cycles of freeze testing and subdivision of droplets of dil. soil suspensions; they were complex and apparently org. entities. Ice nucleation activity was not affected by digestion of Proteinase K-susceptible proteins or the removal of entities composed of fulvic and humic acids, sterols, or aliph. alc. monolayers. Org. INPs active colder than -10 to -12 °C were resistant to all investigations other than heat, oxidn. with H2O2, and, for some, digestion with papain. They may originate from decompg. plant material, microbial biomass, and/or the humin component of the SOM. In the case of the latter then they are most likely to be a carbohydrate. Reflecting the diversity of the SOM itself, soil INPs have a range of sources which occur with differing relative abundances.
- 24Pouleur, S.; Richard, C.; Martin, J.-G.; Antoun, H. Ice Nucleation Activity in Fusarium acuminatum and Fusarium avenaceum. Appl. Environ. Microbiol. 1992, 58 (9), 2960– 2964, DOI: 10.1128/aem.58.9.2960-2964.199224https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC3crot1Wksw%253D%253D&md5=2a088d316c12f4b6f53e99b9588f55c0Ice Nucleation Activity in Fusarium acuminatum and Fusarium avenaceumPouleur S; Richard C; Martin J G; Antoun HApplied and environmental microbiology (1992), 58 (9), 2960-4 ISSN:0099-2240.Twenty fungal genera, including 14 Fusarium species, were examined for ice nucleation activity at -5.0 degrees C, and this activity was found only in Fusarium acuminatum and Fusarium avenaceum. This characteristic is unique to these two species. Ice nucleation activity of F. avenaceum was compared with ice nucleation activity of a Pseudomonas sp. strain. Cumulative nucleus spectra are similar for both microorganisms, while the maximum temperatures of ice nucleation were -2.5 degrees C for F. avenaceum and -1.0 degrees C for the bacteria. Ice nucleation activity of F. avenaceum was stable at pH levels from 1 to 13 and tolerated temperature treatments up to 60 degrees C, suggesting that these ice nuclei are more similar to lichen ice nuclei than to bacterial ones. Ice nuclei of F. avenaceum, unlike bacterial ice nuclei, pass through a 0.22-mum-pore-size filter. Fusarial nuclei share some characteristics with the so-called leaf-derived nuclei with which they might be identified: they are cell free and stable up to 60 degrees C, and they are found in the same kinds of environment. Highly stable ice nuclei produced by fast-growing microorganisms have potential applications in biotechnology. This is the first report of ice nucleation activity in free-living fungi.
- 25Fröhlich-Nowoisky, J.; Hill, T. C.; Pummer, B. G.; Yordanova, P.; Franc, G. D.; Pöschl, U. Ice nucleation activity in the widespread soil fungus Mortierella alpina. Biogeosciences 2015, 12 (4), 1057– 1071, DOI: 10.5194/bg-12-1057-2015There is no corresponding record for this reference.
- 26Cascajo-Castresana, M.; David, R. O.; Iriarte-Alonso, M. A.; Bittner, A. M.; Marcolli, C. Protein Aggregates Nucleate Ice: The Example of Apoferritin. Atmos. Chem. Phys. 2020, 20 (6), 3291– 3315, DOI: 10.5194/acp-20-3291-202026https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXps1aktbg%253D&md5=19298ee52a75e27c35867e5d39f05b91Protein aggregates nucleate ice: the example of apoferritinCascajo-Castresana, Maria; David, Robert O.; Iriarte-Alonso, Maiara A.; Bittner, Alexander M.; Marcolli, ClaudiaAtmospheric Chemistry and Physics (2020), 20 (6), 3291-3315CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Biol. material has gained increasing attention recently as a source of ice-nucleating particles that may account for cloud glaciation at moderate supercooling. While the ice-nucleation (IN) ability of some bacteria can be related to membrane-bound proteins with epitaxial fit to ice, little is known about the IN-active entities present in biol. material in general. To elucidate the potential of proteins and viruses to contribute to the IN activity of biol. material, we performed bulk freezing expts. with the newly developed drop freezing assay DRoplet Ice Nuclei Counter Zurich (DRINCZ), which allows the simultaneous cooling of 96 sample aliquots in a chilled ethanol bath. We performed a screening of common proteins, namely the iron storage protein ferritin and its iron-free counterpart apoferritin, the milk protein casein, the egg protein ovalbumin, two hydrophobins, and a yeast ice-binding protein, all of which revealed IN activity with active site densities > 0.1 mg-1 at -10 °C. The tobacco mosaic virus, a plant virus based on helically assembled proteins, also proved to be IN active with active site densities increasing from 100 mg-1 at -14 °C to 10 000 mg-1 at -20 °C. Among the screened proteins, the IN activity of horse spleen ferritin and apoferritin, which form cages of 24 co-assembled protein subunits, proved to be outstanding with active site densities > 10 mg-1 at -5 °C. Investigation of the pH dependence and heat resistance of the apoferritin sample confirmed the proteinaceous nature of its IN-active entities but excluded the correctly folded cage monomer as the IN-active species. A diln. series of apoferritin in water revealed two distinct freezing ranges, an upper one from -4 to -11 °C and a lower one from -11 to -21 °C. Dynamic light scattering measurements related the upper freezing range to ice-nucleating sites residing on aggregates and the lower freezing range to sites located on misfolded cage monomers or oligomers. The sites proved to persist during several freeze-thaw cycles performed with the same sample aliquots. Based on these results, IN activity seems to be a common feature of diverse proteins, irresp. of their function, but arising only rarely, most probably through defective folding or aggregation to structures that are IN active.
- 27Adams, M. P.; Atanasova, N. S.; Sofieva, S.; Ravantti, J.; Heikkinen, A.; Brasseur, Z.; Duplissy, J.; Bamford, D. H.; Murray, B. J. Ice Nucleation by Viruses and Their Potential for Cloud Glaciation. Biogeosciences 2021, 18 (14), 4431– 4444, DOI: 10.5194/bg-18-4431-202127https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXis1yns77L&md5=1b39e64a52811f9a15358518ac5b1786Ice nucleation by viruses and their potential for cloud glaciationAdams, Michael P.; Atanasova, Nina S.; Sofieva, Svetlana; Ravantti, Janne; Heikkinen, Aino; Brasseur, Zoe; Duplissy, Jonathan; Bamford, Dennis H.; Murray, Benjamin J.Biogeosciences (2021), 18 (14), 4431-4444CODEN: BIOGGR; ISSN:1726-4189. (Copernicus Publications)In order to effectively predict the formation of ice in clouds we need to know which subsets of aerosol particles are effective at nucleating ice, how they are distributed and where they are from. A large proportion of ice-nucleating particles (INPs) in many locations are likely of biol. origin, and some INPs are extremely small, being just tens of nanometers in size. The identity and sources of such INPs are not well characterized. Here, we show that several different types of virus particles can nucleate ice, with up to about 1 in 20 million virus particles able to nucleate ice at -20 °C. In terms of the impact on cloud glaciation, the ice-nucleating ability (the fraction which are ice nucleation active as a function of temp.) taken together with typical virus particle concns. in the atm. leads to the conclusion that virus particles make a minor contribution to the atm. ice-nucleating particle population in the terrestrial-influenced atm. However, they cannot be ruled out as being important in the remote marine atm. It is striking that virus particles have an ice-nucleating activity, and further work should be done to explore other types of viruses for both their ice-nucleating potential and to understand the mechanism by which viruses nucleate ice.
- 28Alpert, P. A.; Aller, J. Y.; Knopf, D. A. Ice Nucleation from Aqueous NaCl Droplets with and without Marine Diatoms. Atmos. Chem. Phys. 2011, 11 (12), 5539– 5555, DOI: 10.5194/acp-11-5539-201128https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXht1WjtrrO&md5=b1267c0528d6017d98040fbee83928e4Ice nucleation from aqueous NaCl droplets with and without marine diatomsAlpert, P. A.; Aller, J. Y.; Knopf, D. A.Atmospheric Chemistry and Physics (2011), 11 (12), 5539-5555CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)Ice formation in the atm. by homogeneous and heterogeneous nucleation is one of the least understood processes in cloud microphysics and climate. Here we describe our investigation of the marine environment as a potential source of atm. IN by exptl. observing homogeneous ice nucleation from aq. NaCl droplets and comparing against heterogeneous ice nucleation from aq. NaCl droplets contg. intact and fragmented diatoms. Homogeneous and heterogeneous ice nucleation are studied as a function of temp. and water activity, aw. Addnl. analyses are presented on the dependence of diatom surface area and aq. vol. on heterogeneous freezing temps., ice nucleation rates, ωhet, ice nucleation rate coeffs., Jhet, and differential and cumulative ice nuclei spectra, k(T) and K(T), resp. Homogeneous freezing temps. and corresponding nucleation rate coeffs. are in agreement with the water activity based homogeneous ice nucleation theory within exptl. and predictive uncertainties. Our results confirm, as predicted by classical nucleation theory, that a stochastic interpretation can be used to describe the homogeneous ice nucleation process. Heterogeneous ice nucleation initiated by intact and fragmented diatoms can be adequately represented by a modified water activity based ice nucleation theory. A horizontal shift in water activity, Δaw,het = 0.2303, of the ice melting curve can describe median heterogeneous freezing temps. Individual freezing temps. showed no dependence on available diatom surface area and aq. vol. Detd. at median diatom freezing temps. for aw from 0.8 to 0.99, ωhet≃0.11+0.06-0.05 s-1, Jhet≃1.0+1.16-0.61 × 104 cm-2 s-1, and K≃6.2+3.5-4.1 × 104 cm-2. The exptl. derived ice nucleation rates and nuclei spectra allow us to est. ice particle prodn. which we subsequently use for a comparison with obsd. ice crystal concns. typically found in cirrus and polar marine mixed-phase clouds. Differences in application of time-dependent and time-independent analyses to predict ice particle prodn. are discussed.
- 29Ickes, L.; Porter, G. C. E.; Wagner, R.; Adams, M. P.; Bierbauer, S.; Bertram, A. K.; Bilde, M.; Christiansen, S.; Ekman, A. M. L.; Gorokhova, E.; Höhler, K.; Kiselev, A. A.; Leck, C.; Möhler, O.; Murray, B. J.; Schiebel, T.; Ullrich, R.; Salter, M. E. The Ice-Nucleating Activity of Arctic Sea Surface Microlayer Samples and Marine Algal Cultures. Atmos. Chem. Phys. 2020, 20 (18), 11089– 11117, DOI: 10.5194/acp-20-11089-202029https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXitVyltL3P&md5=c5c9b8c7e0f0e823d26c01029b4efaa2The ice-nucleating activity of Arctic sea surface microlayer samples and marine algal culturesIckes, Luisa; Porter, Grace C. E.; Wagner, Robert; Adams, Michael P.; Bierbauer, Sascha; Bertram, Allan K.; Bilde, Merete; Christiansen, Sigurd; Ekman, Annica M. L.; Gorokhova, Elena; Hoehler, Kristina; Kiselev, Alexei A.; Leck, Caroline; Moehler, Ottmar; Murray, Benjamin J.; Schiebel, Thea; Ullrich, Romy; Salter, Matthew E.Atmospheric Chemistry and Physics (2020), 20 (18), 11089-11117CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)In recent years, sea spray as well as the biol. material it contains has received increased attention as a source of ice-nucleating particles (INPs). Such INPs may play a role in remote marine regions, where other sources of INPs are scarce or absent. In the Arctic, these INPs can influence water-ice partitioning in low-level clouds and thereby the cloud lifetime, with consequences for the surface energy budget, sea ice formation and melt, and climate. Marine aerosol is of a diverse nature, so identifying sources of INPs is challenging. One fraction of marine bioaerosol (phytoplankton and their exudates) has been a particular focus of marine INP research. Firstly, we compare the ice-nucleating ability of two common phytoplankton species with Arctic seawater microlayer samples using the same instrumentation to see if these phytoplankton species produce ice-nucleating material with sufficient activity to account for the ice nucleation obsd. in Arctic microlayer samples. We present the first measurements of the ice-nucleating ability of two predominant phytoplankton species: Melosira arctica, a common Arctic diatom species, and Skeletonema marinoi, a ubiquitous diatom species across oceans worldwide. To det. the potential effect of nutrient conditions and characteristics of the algal culture, such as the amt. of org. carbon assocd. with algal cells, on the ice nucleation activity, Skeletonema marinoi was grown under different nutrient regimes.
- 30Bogler, S.; Borduas-Dedekind, N. Lignin’s Ability to Nucleate Ice via Immersion Freezing and Its Stability towards Physicochemical Treatments and Atmospheric Processing. Atmos. Chem. Phys. 2020, 20 (23), 14509– 14522, DOI: 10.5194/acp-20-14509-202030https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXis1antbzL&md5=0178f8463d4f87656ea1ff9aee2b9f68Lignin's ability to nucleate ice via immersion freezing and its stability towards physicochemical treatments and atmospheric processingBogler, Sophie; Borduas-Dedekind, NadineAtmospheric Chemistry and Physics (2020), 20 (23), 14509-14522CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Aerosol-cloud interactions dominate the uncertainties in current predictions of the atm.'s radiative balance. Specifically, the ice phase remains difficult to predict in mixed-phase clouds, where liq. water and ice co-exist. The formation of ice in these clouds originates from heterogeneous ice nucleation processes, of which immersion freezing is a dominant pathway. Among atm. surfaces capable of forming a template for ice, mineral dust, biol. material and more recently org. matter are known to initiate freezing. To further our understanding of the role of org. matter in ice nucleation, we chose to investigate the ice nucleation (IN) ability of a specific subcomponent of atm. org. matter, the biopolymer lignin. Ice nucleation expts. were conducted in our custom-built freezing ice nuclei counter (FINC) to measure freezing temps. in the immersion freezing mode. We find that lignin acts as an ice-active macromol. at temps. relevant for mixed-phase cloud processes (e.g. 50% activated fraction up to -18.8°C at 200 mg C L-1). Within a diln. series of lignin solns., we obsd. a non-linear effect in freezing temps.; the no. of IN sites per mg of carbon increased with decreasing lignin concn. We attribute this change to a concn.-dependant aggregation of lignin in soln. We further investigated the effect of physicochem. treatments on lignin's IN activity, including expts. with sonication, heating and reaction with hydrogen peroxide. Only harsh conditions such as heating to 260°C and addn. of a mixt. with a ratio of 1 : 750 of grams of lignin to millilitres of hydrogen peroxide were able to decrease lignin's IN activity to the instrument's background level. Next, photochem. and ozone bubbling expts. were conducted to test the effect of atm. processing on lignin's IN activity. We showed that this activity was not susceptible to changes under atmospherically relevant conditions, despite chem. changes obsd. by UV-Vis absorbance. Our results present lignin as a recalcitrant IN-active subcomponent of org. matter within, for example, biomass burning aerosols and brown carbon. They further contribute to the understanding of how sol. org. material in the atm. can nucleate ice.
- 31Hiranuma, N.; Möhler, O.; Yamashita, K.; Tajiri, T.; Saito, A.; Kiselev, A.; Hoffmann, N.; Hoose, C.; Jantsch, E.; Koop, T.; Murakami, M. Ice Nucleation by Cellulose and Its Potential Contribution to Ice Formation in Clouds. Nat. Geosci. 2015, 8 (4), 273– 277, DOI: 10.1038/ngeo237431https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXjs1GqsL8%253D&md5=4b9b7fcd57b1a6c80c53f584a3838c1dIce nucleation by cellulose and its potential contribution to ice formation in cloudsHiranuma, N.; Moehler, O.; Yamashita, K.; Tajiri, T.; Saito, A.; Kiselev, A.; Hoffmann, N.; Hoose, C.; Jantsch, E.; Koop, T.; Murakami, M.Nature Geoscience (2015), 8 (4), 273-277CODEN: NGAEBU; ISSN:1752-0894. (Nature Publishing Group)Ice particles in the atm. influence clouds, pptn. and climate, and often form with help from aerosols that serve as ice-nucleating particles. Biol. particles, including non-proteinaceous ones, contribute to the diverse spectrum of ice-nucleating particles. However, little is known about their atm. abundance and ice nucleation efficiency, and their role in clouds and the climate system is poorly constrained. One biol. particle type, cellulose, has been shown to exist in an airborne form that is prevalent throughout the year even at remote and elevated locations. Here we report expts. in a cloud simulation chamber to demonstrate that microcryst. cellulose particles can act as efficient ice-nucleating particles in simulated supercooled clouds. In six immersion mode freezing expts., we measured the ice nucleation active surface-site densities of aerosolized cellulose across a range of temps. Using these active surface-site densities, we developed parameters describing the ice nucleation ability of these particles and applied them to obsd. atm. cellulose and plant debris concns. in a global aerosol model. We find that ice nucleation by cellulose becomes significant (>0.1 l-1) below about -21 °C, temps. relevant to mixed-phase clouds. We conclude that the ability of cellulose to act as ice-nucleating particles requires a revised quantification of their role in cloud formation and pptn.
- 32Hiranuma, N.; Adachi, K.; Bell, D. M.; Belosi, F.; Beydoun, H.; Bhaduri, B.; Bingemer, H.; Budke, C.; Clemen, H.-C.; Conen, F.; Cory, K. M.; Curtius, J.; DeMott, P. J.; Eppers, O.; Grawe, S.; Hartmann, S.; Hoffmann, N.; Höhler, K.; Jantsch, E.; Kiselev, A.; Koop, T.; Kulkarni, G.; Mayer, A.; Murakami, M.; Murray, B. J.; Nicosia, A.; Petters, M. D.; Piazza, M.; Polen, M.; Reicher, N.; Rudich, Y.; Saito, A.; Santachiara, G.; Schiebel, T.; Schill, G. P.; Schneider, J.; Segev, L.; Stopelli, E.; Sullivan, R. C.; Suski, K.; Szakáll, M.; Tajiri, T.; Taylor, H.; Tobo, Y.; Ullrich, R.; Weber, D.; Wex, H.; Whale, T. F.; Whiteside, C. L.; Yamashita, K.; Zelenyuk, A.; Möhler, O. A Comprehensive Characterization of Ice Nucleation by Three Different Types of Cellulose Particles Immersed in Water. Atmos. Chem. Phys. 2019, 19 (7), 4823– 4849, DOI: 10.5194/acp-19-4823-201932https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXps1aks7k%253D&md5=28b62af8c11cec554e97e21e1a9aea5cA comprehensive characterization of ice nucleation by three different types of cellulose particles immersed in waterHiranuma, Naruki; Adachi, Kouji; Bell, David M.; Belosi, Franco; Beydoun, Hassan; Bhaduri, Bhaskar; Bingemer, Heinz; Budke, Carsten; Clemen, Hans-Christian; Conen, Franz; Cory, Kimberly M.; Curtius, Joachim; Demott, Paul J.; Eppers, Oliver; Grawe, Sarah; Hartmann, Susan; Hoffmann, Nadine; Hohler, Kristina; Jantsch, Evelyn; Kiselev, Alexei; Koop, Thomas; Kulkarni, Gourihar; Mayer, Amelie; Murakami, Masataka; Murray, Benjamin J.; Nicosia, Alessia; Petters, Markus D.; Piazza, Matteo; Polen, Michael; Reicher, Naama; Rudich, Yinon; Saito, Atsushi; Santachiara, Gianni; Schiebel, Thea; Schill, Gregg P.; Schneider, Johannes; Segev, Lior; Stopelli, Emiliano; Sullivan, Ryan C.; Suski, Kaitlyn; Szakall, Miklos; Tajiri, Takuya; Taylor, Hans; Tobo, Yutaka; Ullrich, Romy; Weber, Daniel; Wex, Heike; Whale, Thomas F.; Whiteside, Craig L.; Yamashita, Katsuya; Zelenyuk, Alla; Mohler, OttmarAtmospheric Chemistry and Physics (2019), 19 (7), 4823-4849CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)We present the lab. results of immersion freezing efficiencies of cellulose particles at supercooled temp. (T) conditions. Three types of chem. homogeneous cellulose samples are used as surrogates that represent supermicron and submicron ice-nucleating plant structural polymers. These samples include microcryst. cellulose (MCC), fibrous cellulose (FC) and nanocryst. cellulose (NCC). Our immersion freezing dataset includes data from various ice nucleation measurement techniques available at 17 different institutions, including nine dry dispersion and 11 aq. suspension techniques. With a total of 20 methods, we performed systematic accuracy and precision anal. of measurements from all 20 measurement techniques by evaluating T -binned (1 °C) data over a wide range (-36 °C < T < -4 °C). Specifically, we intercompared the geometric surface area-based ice nucleation active surface site (INAS) d. data derived from our measurements as a function of T, ns,geo(T). Addnl., we also compared the ns,geo(T) values and the freezing spectral slope parameter (1log(ns,geo)/ Δ T) from our measurements to previous literature results. Results show all three cellulose materials are reasonably ice active. The freezing efficiencies of NCC samples agree reasonably well, whereas the diversity for the other two samples spans ≈ 10 °C. Despite given uncertainties within each instrument technique, the overall trend of the ns,geo(T) spectrum traced by the T -binned av. of measurements suggests that predominantly supermicron-sized cellulose particles (MCC and FC) generally act as more efficient ice-nucleating particles (INPs) than NCC with about 1 order of magnitude higher ns,geo(T).
- 33Alsante, A. N.; Thornton, D. C. O.; Brooks, S. D. Ice Nucleation Catalyzed by the Photosynthesis Enzyme RuBisCO and Other Abundant Biomolecules. Commun. Earth Environ. 2023, 4 (1), 51, DOI: 10.1038/s43247-023-00707-7There is no corresponding record for this reference.
- 34Wolf, M. J.; Coe, A.; Dove, L. A.; Zawadowicz, M. A.; Dooley, K.; Biller, S. J.; Zhang, Y.; Chisholm, S. W.; Cziczo, D. J. Investigating the Heterogeneous Ice Nucleation of Sea Spray Aerosols Using Prochlorococcus as a Model Source of Marine Organic Matter. Environ. Sci. Technol. 2019, 53 (3), 1139– 1149, DOI: 10.1021/acs.est.8b0515034https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXis1SktrrO&md5=dcb8b0d4eef55066f8f1929f628cd69fInvestigating the Heterogeneous Ice Nucleation of Sea Spray Aerosols Using Prochlorococcus as a Model Source of Marine Organic MatterWolf, Martin J.; Coe, Allison; Dove, Lilian A.; Zawadowicz, Maria A.; Dooley, Keven; Biller, Steven J.; Zhang, Yue; Chisholm, Sallie W.; Cziczo, Daniel J.Environmental Science & Technology (2019), 53 (3), 1139-1149CODEN: ESTHAG; ISSN:0013-936X. (American Chemical Society)Sea spray is the largest aerosol source on Earth. Bubble bursting mechanisms at the ocean surface create smaller film burst and larger jet drop particles. This study quantified the effects of particle chem. on the depositional ice nucleation efficiency of lab.-generated sea spray aerosols under the cirrus-relevant conditions. Cultures of Prochlorococcus, the most abundant phytoplankton species in the global ocean, were used as a model source of org. sea spray aerosols. We show that smaller particles generated from lyzed Prochlorococcus cultures are organically enriched and nucleate more effectively than larger particles generated from the same cultures. We then quantified the ice nucleation efficiency of single component org. mols. that mimic Prochlorococcus proteins, lipids, and saccharides. Amylopectin, agarose, and aspartic acid exhibited similar crit. ice saturations, fractional activations, and ice nucleation active site no. densities to particles generated from Prochlorococcus cultures. These findings indicate that saccharides and proteins with numerous and well-ordered hydrophilic functional groups may det. the ice nucleation abilities of org. sea spray aerosols.
- 35Pummer, B. G.; Budke, C.; Augustin-Bauditz, S.; Niedermeier, D.; Felgitsch, L.; Kampf, C. J.; Huber, R. G.; Liedl, K. R.; Loerting, T.; Moschen, T.; Schauperl, M.; Tollinger, M.; Morris, C. E.; Wex, H.; Grothe, H.; Pöschl, U.; Koop, T.; Fröhlich-Nowoisky, J. Ice Nucleation by Water-Soluble Macromolecules. Atmos. Chem. Phys. 2015, 15 (8), 4077– 4091, DOI: 10.5194/acp-15-4077-201535https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXns1ahsL4%253D&md5=b851059d5ff5097c39d6cdc4a27914aaIce nucleation by water-soluble macromoleculesPummer, B. G.; Budke, C.; Augustin-Bauditz, S.; Niedermeier, D.; Felgitsch, L.; Kampf, C. J.; Huber, R. G.; Liedl, K. R.; Loerting, T.; Moschen, T.; Schauperl, M.; Tollinger, M.; Morris, C. E.; Wex, H.; Grothe, H.; Poeschl, U.; Koop, T.; Froehlich-Nowoisky, J.Atmospheric Chemistry and Physics (2015), 15 (8), 4077-4091CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Cloud glaciation is critically important for the global radiation budget (albedo) and for initiation of pptn. But the freezing of pure water droplets requires cooling to temps. as low as 235 K. Freezing at higher temps. requires the presence of an ice nucleator, which serves as a template for arranging water mols. in an ice-like manner. It is often assumed that these ice nucleators have to be insol. particles. We point out that also free macromols. which are dissolved in water can efficiently induce ice nucleation: the size of such ice nucleating macromols. (INMs) is in the range of nanometers, corresponding to the size of the crit. ice embryo. As the latter is temp.-dependent, we see a correlation between the size of INMs and the ice nucleation temp. as predicted by classical nucleation theory. Different types of INMs have been found in a wide range of biol. species and comprise a variety of chem. structures including proteins, saccharides, and lipids. Our investigation of the fungal species Acremonium implicatum, Isaria farinosa, and Mortierella alpina shows that their ice nucleation activity is caused by proteinaceous water-sol. INMs. We combine these new results and literature data on INMs from fungi, bacteria, and pollen with theor. calcns. to develop a chem. interpretation of ice nucleation and water-sol. INMs. This has atm. implications since many of these INMs can be released by fragmentation of the carrier cell and subsequently may be distributed independently. Up to now, this process has not been accounted for in atm. models.
- 36Wex, H.; Augustin-Bauditz, S.; Boose, Y.; Budke, C.; Curtius, J.; Diehl, K.; Dreyer, A.; Frank, F.; Hartmann, S.; Hiranuma, N.; Jantsch, E.; Kanji, Z. A.; Kiselev, A.; Koop, T.; Möhler, O.; Niedermeier, D.; Nillius, B.; Rösch, M.; Rose, D.; Schmidt, C.; Steinke, I.; Stratmann, F. Intercomparing Different Devices for the Investigation of Ice Nucleating Particles Using Snomax® as Test Substance. Atmos. Chem. Phys. 2015, 15 (3), 1463– 1485, DOI: 10.5194/acp-15-1463-201536https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXivFOgsr4%253D&md5=40d4551c82cf2eb8f98389a4bcd243e3Intercomparing different devices for the investigation of ice nucleating particles using Snomax as test substanceWex, H.; Augustin-Bauditz, S.; Boose, Y.; Budke, C.; Curtius, J.; Diehl, K.; Dreyer, A.; Frank, F.; Hartmann, S.; Hiranuma, N.; Jantsch, E.; Kanji, Z. A.; Kiselev, A.; Koop, T.; Moehler, O.; Niedermeier, D.; Nillius, B.; Roesch, M.; Rose, D.; Schmidt, C.; Steinke, I.; Stratmann, F.Atmospheric Chemistry and Physics (2015), 15 (3), 1463-1485, 23 pp.CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Seven different instruments and measurement methods were used to examine the immersion freezing of bacterial ice nuclei from Snomax (hereafter Snomax), a product contg. ice-active protein complexes from nonviable Pseudomonas syringae bacteria. The exptl. conditions were kept as similar as possible for the different measurements. Of the participating instruments, some examd. droplets which had been made from suspensions directly, and the others examd. droplets activated on previously generated Snomax particles, with particle diams. of mostly a few hundred nanometers and up to a few micrometers in some cases. Data were obtained in the temp. range from -2 to -38 °C, and it was found that all ice-active protein complexes were already activated above -12 °C. Droplets with different Snomax mass concns. covering 10 orders of magnitude were examd. Some instruments had very short ice nucleation times down to below 1 s, while others had comparably slow cooling rates around 1 Kmin-1. Displaying data from the different instruments in terms of nos. of ice-active protein complexes per dry mass of Snomax, nm, showed that within their uncertainty, the data agree well with each other as well as to previously reported literature results. Two parameterizations were taken from literature for a direct comparison to our results, and these were a time-dependent approach based on a contact angle distribution (Niedermeier et al., 2014) and a modification of the parameterization presented in Hartmann et al. (2013) representing a time-independent approach. The agreement between these and the measured data were good; i.e., they agreed within a temp. range of 0.6K or equivalently a range in nm of a factor of 2. From the results presented herein, we propose that Snomax, at least when carefully shared and prepd., is a suitable material to test and compare different instruments for their accuracy of measuring immersion freezing.
- 37Hartmann, S.; Ling, M.; Dreyer, L. S. A.; Zipori, A.; Finster, K.; Grawe, S.; Jensen, L. Z.; Borck, S.; Reicher, N.; Drace, T.; Niedermeier, D.; Jones, N. C.; Hoffmann, S. V.; Wex, H.; Rudich, Y.; Boesen, T.; Šantl-Temkiv, T. Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity. Front. Microbiol. 2022, 13, 872306, DOI: 10.3389/fmicb.2022.87230637https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BB2Mfjtlyjtg%253D%253D&md5=80ab0ba31518c87430496235534fd938Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their ActivityHartmann Susan; Grawe Sarah; Niedermeier Dennis; Wex Heike; Ling Meilee; Finster Kai; Jensen Lasse Z; Borck Stella; Santl-Temkiv Tina; Ling Meilee; Finster Kai; Jensen Lasse Z; Borck Stella; Santl-Temkiv Tina; Ling Meilee; Dreyer Lasse S A; Jensen Lasse Z; Borck Stella; Drace Taner; Boesen Thomas; Zipori Assaf; Reicher Naama; Rudich Yinon; Jones Nykola C; Hoffmann Soren V; Boesen ThomasFrontiers in microbiology (2022), 13 (), 872306 ISSN:1664-302X.Microbially-produced ice nucleating proteins (INpro) are unique molecular structures with the highest known catalytic efficiency for ice formation. Airborne microorganisms utilize these proteins to enhance their survival by reducing their atmospheric residence times. INpro also have critical environmental effects including impacts on the atmospheric water cycle, through their role in cloud and precipitation formation, as well as frost damage on crops. INpro are ubiquitously present in the atmosphere where they are emitted from diverse terrestrial and marine environments. Even though bacterial genes encoding INpro have been discovered and sequenced decades ago, the details of how the INpro molecular structure and oligomerization foster their unique ice-nucleation activity remain elusive. Using machine-learning based software AlphaFold 2 and trRosetta, we obtained and analysed the first ab initio structural models of full length and truncated versions of bacterial INpro. The modeling revealed a novel beta-helix structure of the INpro central repeat domain responsible for ice nucleation activity. This domain consists of repeated stacks of two beta strands connected by two sharp turns. One beta-strand is decorated with a TxT amino acid sequence motif and the other strand has an SxL[T/I] motif. The core formed between the stacked beta helix-pairs is unusually polar and very distinct from previous INpro models. Using synchrotron radiation circular dichroism, we validated the β-strand content of the central repeat domain in the model. Combining the structural model with functional studies of purified recombinant INpro, electron microscopy and modeling, we further demonstrate that the formation of dimers and higher-order oligomers is key to INpro activity. Using computational docking of the new INpro model based on rigid-body algorithms we could reproduce a previously proposed homodimer structure of the INpro CRD with an interface along a highly conserved tyrosine ladder and show that the dimer model agrees with our functional data. The parallel dimer structure creates a surface where the TxT motif of one monomer aligns with the SxL[T/I] motif of the other monomer widening the surface that interacts with water molecules and therefore enhancing the ice nucleation activity. This work presents a major advance in understanding the molecular foundation for bacterial ice-nucleation activity.
- 38Lukas, M.; Schwidetzky, R.; Eufemio, R. J.; Bonn, M.; Meister, K. Toward Understanding Bacterial Ice Nucleation. J. Phys. Chem. B 2022, 126 (9), 1861– 1867, DOI: 10.1021/acs.jpcb.1c0934238https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XitFWjsb8%253D&md5=6629df0508ec4794b199fe434acd50bfToward Understanding Bacterial Ice NucleationLukas, Max; Schwidetzky, Ralph; Eufemio, Rosemary J.; Bonn, Mischa; Meister, KonradJournal of Physical Chemistry B (2022), 126 (9), 1861-1867CODEN: JPCBFK; ISSN:1520-5207. (American Chemical Society)A review. Bacterial ice nucleators (INs) are among the most effective ice nucleators known and relevant for freezing processes in agriculture, the atm., and the biosphere. Their ability to facilitate ice formation is due to specialized ice-nucleating proteins (INPs) anchored to the outer bacterial cell membrane and enabling the crystn. of water at temps. up to -2°. In this Perspective, the authors highlight the importance of functional aggregation of INPs for the exceptionally high ice nucleation activity of bacterial ice nucleators. The authors emphasize that the bacterial cell membrane, as well as environmental conditions, are crucial for a precise functional INP aggregation. Interdisciplinary approaches combining high-throughput droplet freezing assays with advanced physicochem. tools and protein biochem. are needed to link changes in protein structure or protein-water interactions with changes on the functional level.
- 39Valegård, K.; Hasse, D.; Andersson, I.; Gunn, L. H. Structure of Rubisco from Arabidopsis thaliana in Complex with 2-Carboxyarabinitol-1,5-Bisphosphate. Acta Crystallogr., Sect. D: Struct. Biol. 2018, 74 (1), 1– 9, DOI: 10.1107/S205979831701713239https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC1MvksF2quw%253D%253D&md5=6f330bf5a9353bf87b49a7db82c3bc9fStructure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bisphosphateValegard Karin; Hasse Dirk; Andersson Inger; Gunn Laura HActa crystallographica. Section D, Structural biology (2018), 74 (Pt 1), 1-9 ISSN:.The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Arabidopsis thaliana is reported at 1.5 ÅA resolution. In light of the importance of A. thaliana as a model organism for understanding higher plant biology, and the pivotal role of Rubisco in photosynthetic carbon assimilation, there has been a notable absence of an A. thaliana Rubisco crystal structure. A. thaliana Rubisco is an L8S8 hexadecamer comprising eight plastome-encoded catalytic large (L) subunits and eight nuclear-encoded small (S) subunits. A. thaliana produces four distinct small-subunit isoforms (RbcS1A, RbcS1B, RbcS2B and RbcS3B), and this crystal structure provides a snapshot of A. thaliana Rubisco containing the low-abundance RbcS3B small-subunit isoform. Crystals were obtained in the presence of the transition-state analogue 2-carboxy-D-arabinitol-1,5-bisphosphate. A. thaliana Rubisco shares the overall fold characteristic of higher plant Rubiscos, but exhibits an interesting disparity between sequence and structural relatedness to other Rubisco isoforms. These results provide the structural framework to understand A. thaliana Rubisco and the potential catalytic differences that could be conferred by alternative A. thaliana Rubisco small-subunit isoforms.
- 40Bar-On, Y. M.; Milo, R. The Global Mass and Average Rate of Rubisco. Proc. Natl. Acad. Sci. U. S. A. 2019, 116 (10), 4738– 4743, DOI: 10.1073/pnas.181665411640https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXktFeit7g%253D&md5=063c6eaf419c513d9b543716359efa10The global mass and average rate of rubiscoBar-On, Yinon M.; Milo, RonProceedings of the National Academy of Sciences of the United States of America (2019), 116 (10), 4738-4743CODEN: PNASA6; ISSN:0027-8424. (National Academy of Sciences)Photosynthetic carbon assimilation enables energy storage in the living world and produces most of the biomass in the biosphere. Rubisco (d-ribulose 1,5-bisphosphate carboxylase/oxygenase) is responsible for the vast majority of global carbon fixation and has been claimed to be the most abundant protein on Earth. Here we provide an updated and rigorous est. for the total mass of Rubisco on Earth, concluding it is 0.7 Gt, more than an order of magnitude higher than previously thought. We find that >90% of Rubisco enzymes are found in the 2 A~, 1014 m2 of leaves of terrestrial plants, and that Rubisco accounts for 3% of the total mass of leaves, which we est. at 30 Gt dry wt. We use our est. for the total mass of Rubisco to derive the effective time-averaged catalytic rate of Rubisco of 0.03 s1 on land and 0.6 s1 in the ocean. Compared with the maximal catalytic rate obsd. in vitro at 25°C, the effective rate in the wild is 100-fold slower on land and sevenfold slower in the ocean. The lower ambient temp., and Rubisco not working at night, can explain most of the difference from lab. conditions in the ocean but not on land, where quantification of many more factors on a global scale is needed. Our anal. helps sharpen the dramatic difference between lab. and wild environments and between the terrestrial and marine environments.
- 41Tabita, F. R.; Satagopan, S.; Hanson, T. E.; Kreel, N. E.; Scott, S. S. Distinct Form I, II, III, and IV Rubisco Proteins from the Three Kingdoms of Life Provide Clues about Rubisco Evolution and Structure/Function Relationships. J. Exp. Bot. 2007, 59 (7), 1515– 1524, DOI: 10.1093/jxb/erm361There is no corresponding record for this reference.
- 42Berman, H. M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T. N.; Weissig, H.; Shindyalov, I. N.; Bourne, P. E. The Protein Data Bank. Nucleic Acids Res. 2000, 28 (1), 235– 242, DOI: 10.1093/nar/28.1.23542https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3cXhvVKjt7w%253D&md5=227fb393f754be2be375ab727bfd05dcThe Protein Data BankBerman, Helen M.; Westbrook, John; Feng, Zukang; Gilliland, Gary; Bhat, T. N.; Weissig, Helge; Shindyalov, Ilya N.; Bourne, Philip E.Nucleic Acids Research (2000), 28 (1), 235-242CODEN: NARHAD; ISSN:0305-1048. (Oxford University Press)The Protein Data Bank (PDB; http://www.rcsb.org/pdb/)is the single worldwide archive of structural data of biol. macromols. This paper describes the goals of the PDB, the systems in place for data deposition and access, how to obtain further information, and near-term plans for the future development of the resource.
- 43Andersson, I. Large Structures at High Resolution: The 1.6 Å Crystal Structure of Spinach Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase Complexed with 2-Carboxyarabinitol Bisphosphate. J. Mol. Biol. 1996, 259 (1), 160– 174, DOI: 10.1006/jmbi.1996.031043https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADyaK283ktVKrtQ%253D%253D&md5=16132eef90ab69dde6a5aaf021aae450Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphateAndersson IJournal of molecular biology (1996), 259 (1), 160-74 ISSN:0022-2836.Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) from spinach is a hexadecamer (L8S8, Mr = 550,000) consisting of eight large (L, 475 residues) and eight small subunits (S, 123 residues). High-resolution data collection on crystals with large unit cells is not a trivial task due to the effect of radiation damage and the large number of overlapping reflections when conventional data collection methods are used. In order to minimise these effects, data on rubisco were collected with a giant Weissenberg camera at long crystal to image-plate distances at the synchrotron of the Photon Factory, Japan. Relative to conventional data sets, this experimental arrangement allowed a 20 to 30-fold reduction of the X-ray dose/exposure time for data collection. This paper describes the refined 1.6 A crystal structure of activated rubisco complexed with a transition state analogue, 2-carboxyarabinitol-bisphosphate. The crystallographic asymmetric unit contains an L4S4 unit, representing half of the molecule. The structure presented here is currently the highest resolution structure for any protein of comparable size. Refinement of the model was carried out by restrained least squares techniques without non-crystallographic symmetry averaging. The results show that all L and S subunits have identical three-dimensional structures, and their arrangement within the hexadecamer has no intrinsic asymmetry. A detailed analysis of the high-resolution maps identified 30 differences in the sequence of the small subunit, indicating a larger than usual heterogeneity for this nuclear encoded protein in spinach. No such differences were found in the sequence of the chloroplast encoded large subunit. The transition state analogue is in the cis conformation at the active site suggesting a key role for the carbamate of Lys201 in catalysis. Analysis of the active site around the catalytically essential magnesium ion further indicates that residues in the second liganding sphere of the metal play a role in fine-tuning the acid-base character and the position of the residues directly liganded to the metal.
- 44Ramírez-Silva, L.; Hernández-Alcántara, G.; Guerrero-Mendiola, C.; González-Andrade, M.; Rodríguez-Romero, A.; Rodríguez-Hernández, A.; Lugo-Munguía, A.; Gómez-Coronado, P. A.; Rodríguez-Méndez, C.; Vega-Segura, A. The K+-Dependent and-Independent Pyruvate Kinases Acquire the Active Conformation by Different Mechanisms. Int. J. Mol. Sci. 2022, 23 (3), 1347, DOI: 10.3390/ijms2303134744https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XktFWgsr4%253D&md5=5e32d323774dcee725fd51a51e591659The K+-Dependent and -Independent Pyruvate Kinases Acquire the Active Conformation by Different MechanismsRamirez-Silva, Leticia; Hernandez-Alcantara, Gloria; Guerrero-Mendiola, Carlos; Gonzalez-Andrade, Martin; Rodriguez-Romero, Adela; Rodriguez-Hernandez, Annia; Lugo-Munguia, Alan; Gomez-Coronado, Paul A.; Rodriguez-Mendez, Cristina; Vega-Segura, AliciaInternational Journal of Molecular Sciences (2022), 23 (3), 1347CODEN: IJMCFK; ISSN:1422-0067. (MDPI AG)Eukarya pyruvate kinases possess glutamate at position 117 (numbering of rabbit muscle enzyme), whereas bacteria have either glutamate or lysine. Those with E117 are K+-dependent, whereas those with K117 are K+-independent. In a phylogenetic tree, 80% of the sequences with E117 are occupied by T113/K114/T120 and 77% of those with K117 possess L113/Q114/(L,I,V)120. This work aims to understand these residues' contribution to the K+-independent pyruvate kinases using the K+-dependent rabbit muscle enzyme. Residues 117 and 120 are crucial in the differences between the K+-dependent and -independent mutants. K+-independent activity increased with L113 and Q114 to K117, but L120 induced structural differences that inactivated the enzyme. T120 appears to be key in folding the protein and closure of the lid of the active site to acquire its active conformation in the K+-dependent enzymes. E117K mutant was K+-independent and the enzyme acquired the active conformation by a different mechanism. In the K+-independent apoenzyme of Mycobacterium tuberculosis, K72 (K117) flips out of the active site; in the holoenzyme, K72 faces toward the active site bridging the substrates through water mols. The results provide evidence that two different mechanisms have evolved for the catalysis of this reaction.
- 45Stec, B.; Hehir, M. J.; Brennan, C.; Nolte, M.; Kantrowitz, E. R. Kinetic and X-ray Structural Studies of Three Mutant E. coli Alkaline Phosphatases: Insights into the Catalytic Mechanism without the Nucleophile Ser102. J. Mol. Biol. 1998, 277 (3), 647– 662, DOI: 10.1006/jmbi.1998.163545https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaK1cXjtFKlt7o%253D&md5=490c008bbf73d3cee60a1efde7e044fcKinetic and x-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102Stec, Boguslaw; Hehir, Michael J.; Brennan, Christopher; Nolte, Matthias; Kantrowitz, Evan R.Journal of Molecular Biology (1998), 277 (3), 647-662CODEN: JMOBAK; ISSN:0022-2836. (Academic Press Ltd.)Escherichia coli alk. phosphatase (EC 3.1.3.1) is a non-specific phosphomonoesterase that catalyzes the hydrolysis reaction via a phosphoseryl intermediate to produce inorg. phosphate and the corresponding alc. We investigated the nature of the primary nucleophile, fulfilled by the deprotonated Ser102, in the catalytic mechanism by mutating this residue to glycine, alanine and cysteine. The efficiencies of the S102G, S102A and S102C enzymes were 6 × 105-fold, 105-fold and 104-fold lower than the wild-type enzyme, resp., as measured by the kcat/Km ratio, still substantially higher than the non-catalyzed reaction. In order to investigate the structural details of the altered active site, the enzymes were crystd. and their structures detd. The enzymes crystd. in a new crystal form corresponding to the space group P6322. Each structure has phosphate at each active site and shows little departure from the wild-type model. For the S102G and S102A enzymes, the phosphate occupies the same position as in the wild-type enzyme, while in the S102C enzyme it is displaced by 2.5 Å. This kinetic and structural study suggests an explanation for differences in catalytic efficiency of the mutant enzymes and provides a means to study the nature and strength of different nucleophiles in the same environment. The anal. of these results provides insight into the mechanisms of other classes of phosphatases that do not utilize a serine nucleophile.
- 46Wang, X.; Wang, C.; Tang, J.; Dyda, F.; Zhang, X. C. The Crystal Structure of Bovine Bile Salt Activated Lipase: Insights into the Bile Salt Activation Mechanism. Structure 1997, 5 (9), 1209– 1218, DOI: 10.1016/S0969-2126(97)00271-246https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaK2sXmslOnt7s%253D&md5=2f54b31d683f266ba7aa1fbadbb08624The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanismWang, Xiaoqiang; Wang, Chi-Sun; Tang, Jordan; Dyda, Fred; Zhang, Xuejun C.Structure (London) (1997), 5 (9), 1209-1218CODEN: STRUE6; ISSN:0969-2126. (Current Biology)The intestinally located pancreatic enzyme, bile-salt activated lipase (I), possesses unique activities for digesting different kinds of lipids. It also differs from other lipases in a requirement of bile salts for activity. A structure-based explanation for these unique properties has not been reached so far due to the absence of a 3-dimensional structure. Here, the crystal structures of bovine I and its complex with taurocholate were detd. at 2.8 Å resoln. The overall structure of I belonged to the α/β hydrolase fold family. Two bile salt binding sites were found in each I mol. within the I-taurocholate complex structure. One of these sites was located close to a hairpin loop near the active site. Upon the binding of taurocholate, this loop became less mobile and assumed a different conformation. The other bile salt binding site was located remote from the active site. In both structures, I formed similar dimers with the active sites facing each other. Bile salts activated I by binding to a relatively short 10-residue loop near the active site, and stabilized the loop in an open conformation. Presumably, this conformational change leads to the formation of the substrate-binding site, as suggested from kinetic data. The I dimer obsd. in the crystal structure may also play a functional role under physiol. conditions.
- 47Frankaer, C. G.; Mossin, S.; Ståhl, K.; Harris, P. Towards Accurate Structural Characterization of Metal Centres in Protein Crystals: The Structures of Ni and Cu T6 Bovine Insulin Derivatives. Acta Crystallogr., Sect. D Biol. Crystallogr. 2014, 70 (1), 110– 122, DOI: 10.1107/S139900471302904047https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXlvFymsQ%253D%253D&md5=eef4a17dc83586ec0d2aa1a2a18cba40Towards accurate structural characterization of metal centres in protein crystals: the structures of Ni and Cu T6 bovine insulin derivativesFrankaer, Christian Grundahl; Mossin, Susanne; Stahl, Kenny; Harris, PernilleActa Crystallographica, Section D: Biological Crystallography (2014), 70 (1), 110-122CODEN: ABCRE6; ISSN:1399-0047. (International Union of Crystallography)Using synchrotron radiation (SR), the crystal structures of T6 bovine insulin complexed with Ni2+ and Cu2+ were solved to 1.50 and 1.45 Å resoln., resp. The level of detail around the metal centers in these structures was highly limited, and the coordination of water in Cu site II of the copper insulin deriv. was deteriorated as a consequence of radiation damage. To provide more detail, x-ray absorption spectroscopy (XAS) was used to improve the information level about metal coordination in each deriv. The nickel deriv. contains hexacoordinated Ni2+ with trigonal symmetry, whereas the copper deriv. contains tetragonally distorted hexacoordinated Cu2+ as a result of the Jahn-Teller effect, with a significantly longer coordination distance for one of the three water mols. in the coordination sphere. That the copper center is of type II was further confirmed by EPR. The coordination distances were refined from EXAFS with std. deviations within 0.01 Å. The insulin deriv. contg. Cu2+ is sensitive towards photoredn. when exposed to SR. During the redn. of Cu2+ to Cu+, the coordination geometry of copper changes towards lower coordination nos. Primary damage, i.e. photoredn., was followed directly by XANES as a function of radiation dose, while secondary damage as structural changes around the Cu atoms after exposure to different radiation doses was studied by crystallog. using a lab. diffractometer. Protection against photoredn. and subsequent radiation damage was carried out by solid embedment of Cu insulin in a saccharose matrix. At 100 K the photoredn. was suppressed by ∼15%, and it was suppressed by a further ∼30% on cooling the samples to 20 K.
- 48Fornea, A. P.; Brooks, S. D.; Dooley, J. B.; Saha, A. Heterogeneous Freezing of Ice on Atmospheric Aerosols Containing Ash, Soot, and Soil. J. Geophys. Res.: Atmos. 2009, 114 (13), D13201 DOI: 10.1029/2009JD011958There is no corresponding record for this reference.
- 49Budke, C.; Koop, T. BINARY: An Optical Freezing Array for Assessing Temperature and Time Dependence of Heterogeneous Ice Nucleation. Atmos. Meas. Tech. 2015, 8 (2), 689– 703, DOI: 10.5194/amt-8-689-2015There is no corresponding record for this reference.
- 50Alsante, A. N. Characterization of Marine Biogenic Atmospheric Ice Nucleating Particles. Doctoral Dissertation, Texas A&M University, College Station, TX, 2023.There is no corresponding record for this reference.
- 51Vali, G. Quantitative Evaluation of Experimental Results and the Heterogeneous Freezing Nucleation of Supercooled Droplets. J. Atmos. Sci. 1971, 28 (3), 402– 409, DOI: 10.1175/1520-0469(1971)028<0402:QEOERA>2.0.CO;2There is no corresponding record for this reference.
- 52Li, Y.; Lubchenko, V.; Vekilov, P. G. The Use of Dynamic Light Scattering and Brownian Microscopy to Characterize Protein Aggregation. Rev. Sci. Instrum. 2011, 82 (5), 053106, DOI: 10.1063/1.359258152https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXms1Sltbo%253D&md5=284050378c4ea13c15105138dec78c8aThe use of dynamic light scattering and Brownian microscopy to characterize protein aggregationLi, Ye; Lubchenko, Vassiliy; Vekilov, Peter G.Review of Scientific Instruments (2011), 82 (5), 053106/1-053106/8CODEN: RSINAK; ISSN:0034-6748. (American Institute of Physics)Dynamic light scattering (DLS) is often used to monitor aggregation in protein solns. Here, the authors explore the veracity of the aggregate sizes, size distribution widths, concns., and lifetime resulting from DLS. The authors use as an example a soln. of the protein lysozyme in which dense liq. clusters of radius about 100 nm reproducibly exist. The authors compare the results of DLS to those of Brownian microscopy. The authors show that because of the 6th power dependence of the scattered light intensity on the size of the scatterers, DLS overestimates the mean size of the clusters. The factor of overestimation depends on the shape of the size distribution and is ∼1.6 × in the studied soln. The related underestimate of the cluster concn. is ∼10 ×. The CONTIN algorithm, often employed to process DLS data, may, in some instances, produce non-phys. results. The authors put forth an alternative method to det. the aggregates' sizes, concns., and vol. fractions. The authors show that DLS yields a reliable width of the cluster size distribution only if the cluster concn. is above 109 cm-3 and their vol. fraction is above 10-6. DLS yields a lower bound of the cluster lifetime, which may be orders of magnitude lower than the real one. (c) 2011 American Institute of Physics.
- 53Stetefeld, J.; McKenna, S. A.; Patel, T. R. Dynamic Light Scattering: A Practical Guide and Applications in Biomedical Sciences. Biophys. Rev. 2016, 8, 409– 427, DOI: 10.1007/s12551-016-0218-653https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28Xhs1Gqs7bP&md5=468714b5413c92edb45e985fc32e8164Dynamic light scattering: a practical guide and applications in biomedical sciencesStetefeld, Jorg; McKenna, Sean A.; Patel, Trushar R.Biophysical Reviews (2016), 8 (4), 409-427CODEN: BRIECG; ISSN:1867-2450. (Springer)Dynamic light scattering (DLS), also known as photon correlation spectroscopy (PCS), is a very powerful tool for studying the diffusion behavior of macromols. in soln. The diffusion coeff., and hence the hydrodynamic radii calcd. from it, depends on the size and shape of macromols. In this review, we provide evidence of the usefulness of DLS to study the homogeneity of proteins, nucleic acids, and complexes of protein-protein or protein-nucleic acid prepns., as well as to study protein-small mol. interactions. Further, we provide examples of DLS's application both as a complementary method to anal. ultracentrifugation studies and as a screening tool to validate soln. scattering models using detd. hydrodynamic radii.
- 54Bhattacharjee, S. DLS and Zeta Potential─What They Are and What They Are Not?. J. Controlled Release 2016, 235, 337– 351, DOI: 10.1016/j.jconrel.2016.06.01754https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhtFOgt73O&md5=50555ae8bc84aff2dc92b1c2d24dcf80DLS and zeta potential - What they are and what they are not?Bhattacharjee, SouravJournal of Controlled Release (2016), 235 (), 337-351CODEN: JCREEC; ISSN:0168-3659. (Elsevier B.V.)A review. Adequate characterization of NPs (nanoparticles) is of paramount importance to develop well defined nanoformulations of therapeutic relevance. Detn. of particle size and surface charge of NPs are indispensable for proper characterization of NPs. DLS (dynamic light scattering) and ZP (zeta potential) measurements have gained popularity as simple, easy and reproducible tools to ascertain particle size and surface charge. Unfortunately, on practical grounds plenty of challenges exist regarding these two techniques including inadequate understanding of the operating principles and dealing with crit. issues like sample prepn. and interpretation of the data. As both DLS and ZP have emerged from the realms of phys. colloid chem. - it is difficult for researchers engaged in nanomedicine research to master these two techniques. Addnl., there is little literature available in drug delivery research which offers a simple, concise account on these techniques. This review tries to address this issue while providing the fundamental principles of these techniques, summarizing the core math. principles and offering practical guidelines on tackling commonly encountered problems while running DLS and ZP measurements. Finally, the review tries to analyze the relevance of these two techniques from translatory perspective.
- 55Worthy, S. E.; Kumar, A.; Xi, Y.; Yun, J.; Chen, J.; Xu, C.; Irish, V. E.; Amato, P.; Bertram, A. K. The effect of (NH4)2SO4 on the freezing properties of non-mineral dust ice-nucleating substances of atmospheric relevance. Atmos. Chem. Phys. 2021, 21 (19), 14631– 14648, DOI: 10.5194/acp-21-14631-202155https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXitlKjur7M&md5=0ff59829015b7508e61d1ee215605fd0The effect of (NH4)2SO4 on the freezing properties of non-mineral dust ice-nucleating substances of atmospheric relevanceWorthy, Soleil E.; Kumar, Anand; Xi, Yu; Yun, Jingwei; Chen, Jessie; Xu, Cuishan; Irish, Victoria E.; Amato, Pierre; Bertram, Allan K.Atmospheric Chemistry and Physics (2021), 21 (19), 14631-14648CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)A wide range of materials including mineral dust, soil dust, and bioaerosols have been shown to act as ice nuclei in the atm. During atm. transport, these materials can become coated with inorg. and org. solutes which may impact their ability to nucleate ice. While a no. of studies have investigated the impact of solutes at low concns. on ice nucleation by mineral dusts, very few studies have examd. their impact on non-mineral dust ice nuclei. We studied the effect of dil. (NH4)2SO4 solns. (0.05 M) on immersion freezing of a variety of non-mineral dust ice-nucleating substances (INSs) including bacteria, fungi, sea ice diatom exudates, sea surface microlayer substances, and humic substances using the droplet-freezing technique. We also studied the effect of (NH4)2SO4 solns. (0.05 M) on the immersion freezing of several types of mineral dust particles for comparison purposes. (NH4)2SO4 had no effect on the median freezing temp. (ΔT50) of 9 of the 10 non-mineral dust materials tested. There was a small but statistically significant decrease in ΔT50 (-0.43 ± 0.19°C) for the bacteria Xanthomonas campestris in the presence of (NH4)2SO4 compared to pure water. Conversely, (NH4)2SO4 increased the median freezing temp. of four different mineral dusts (potassium-rich feldspar, Arizona Test Dust, kaolinite, montmorillonite) by 3 to 9°C and increased the ice nucleation active site d. per g of material (nm(T)) by a factor of ∼ 10 to ∼ 30. This significant difference in the response of mineral dust and non-mineral dust ice-nucleating substances when exposed to (NH4)2SO4 suggests that they nucleate ice and/or interact with (NH4)2SO4 via different mechanisms. This difference suggests that the relative importance of mineral dust to non-mineral dust particles for ice nucleation in mixed-phase clouds could potentially increase as these particles become coated with (NH4)2SO4 in the atm. This difference also suggests that the addn. of (NH4)2SO4 (0.05 M) to atm. samples of unknown compn. could potentially be used as an indicator or assay for the presence of mineral dust ice nuclei, although addnl. studies are still needed as a function of INS concn. to confirm the same trends are obsd. for different INS concns. than those used here. A comparison with results in the literature does suggest that our results may be applicable to a range of mineral dust and non-mineral dust INS concns.
- 56Forman, H. J.; Zhang, H.; Rinna, A. Glutathione: Overview of Its Protective Roles, Measurement, and Biosynthesis. Mol. Aspects Med. 2009, 30 (1), 1– 12, DOI: 10.1016/j.mam.2008.08.00656https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD1MXltFelurY%253D&md5=c1b1aa2b03389bf1434af0762df78fe1Glutathione: Overview of its protective roles, measurement, and biosynthesisForman, Henry Jay; Zhang, Hongqiao; Rinna, AlessandraMolecular Aspects of Medicine (2009), 30 (1-2), 1-12CODEN: MAMED5; ISSN:0098-2997. (Elsevier B.V.)This review is the introduction to a special issue concerning, glutathione (GSH), the most abundant low mol. wt. thiol compd. synthesized in cells. GSH plays crit. roles in protecting cells from oxidative damage and the toxicity of xenobiotic electrophiles, and maintaining redox homeostasis. Here, the functions and GSH and the sources of oxidants and electrophiles, the elimination of oxidants by redn. and electrophiles by conjugation with GSH are briefly described. Methods of assessing GSH status in the cells are also described. GSH synthesis and its regulation are addressed along with therapeutic approaches for manipulating GSH content that have been proposed. The purpose here is to provide a brief overview of some of the important aspects of glutathione metab. as part of this special issue that will provide a more comprehensive review of the state of knowledge regarding this essential mol.
- 57Pummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H. Suspendable Macromolecules Are Responsible for Ice Nucleation Activity of Birch and Conifer Pollen. Atmos Chem. Phys. 2012, 12 (5), 2541– 2550, DOI: 10.5194/acp-12-2541-201257https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38Xpt12iurg%253D&md5=70cd2ea58dc1a2321693e52dde19b124Suspendable macromolecules are responsible for ice nucleation activity of birch and conifer pollenPummer, B. G.; Bauer, H.; Bernardi, J.; Bleicher, S.; Grothe, H.Atmospheric Chemistry and Physics (2012), 12 (5), 2541-2550CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)The ice nucleation of bioaerosols (bacteria, pollen, spores, etc.) is a topic of growing interest, since their impact on ice cloud formation and thus on radiative forcing, an important parameter in global climate, is not yet fully understood. Here we show that pollen of different species strongly differ in their ice nucleation behavior. The av. freezing temps. in lab. expts. range from 240 to 255 K. As the most efficient nuclei (silver birch, Scots pine and common juniper pollen) have a distribution area up to the Northern timberline, their ice nucleation activity might be a cryoprotective mechanism. Far more intriguingly, it has turned out that water, which has been in contact with pollen and then been sepd. from the bodies, nucleates as good as the pollen grains themselves. The ice nuclei have to be easily-suspendable macromols. located on the pollen. Once extd., they can be distributed further through the atm. than the heavy pollen grains and so presumably augment the impact of pollen on ice cloud formation even in the upper troposphere. Our expts. lead to the conclusion that pollen ice nuclei, in contrast to bacterial and fungal ice nucleating proteins, are non-proteinaceous compds.
- 58Eickhoff, L.; Dreischmeier, K.; Zipori, A.; Sirotinskaya, V.; Adar, C.; Reicher, N.; Braslavsky, I.; Rudich, Y.; Koop, T. Contrasting Behavior of Antifreeze Proteins: Ice Growth Inhibitors and Ice Nucleation Promoters. J. Phys. Chem. Lett. 2019, 10 (5), 966– 972, DOI: 10.1021/acs.jpclett.8b0371958https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXivVOgtLg%253D&md5=e02f7d07b2094deefd6766805a619f95Contrasting Behavior of Antifreeze Proteins: Ice Growth Inhibitors and Ice Nucleation PromotersEickhoff, Lukas; Dreischmeier, Katharina; Zipori, Assaf; Sirotinskaya, Vera; Adar, Chen; Reicher, Naama; Braslavsky, Ido; Rudich, Yinon; Koop, ThomasJournal of Physical Chemistry Letters (2019), 10 (5), 966-972CODEN: JPCLCD; ISSN:1948-7185. (American Chemical Society)Several types of natural mols. interact specifically with ice crystals. Small antifreeze proteins (AFPs) adsorb to particular facets of ice crystals, thus inhibiting their growth, whereas larger ice-nucleating proteins (INPs) can trigger the formation of new ice crystals at temps. much higher than the homogeneous ice nucleation temp. of pure water. It has been proposed that both types of proteins interact similarly with ice and that, in principle, they may be able to exhibit both functions. Here we investigated two naturally occurring antifreeze proteins, one from fish, type-III AFP, and one from beetles, TmAFP. We show that in addn. to ice growth inhibition, both can also trigger ice nucleation above the homogeneous freezing temp., providing unambiguous exptl. proof for their contrasting behavior. Our anal. suggests that the predominant difference between AFPs and INPs is their mol. size, which is a very good predictor of their ice nucleation temp.
- 59Govindarajan, A. G.; Lindow, S. E. Size of Bacterial Ice-Nucleation Sites Measured in Situ by Radiation Inactivation Analysis. Proc. Natl. Acad. Sci. U. S. A. 1988, 85 (5), 1334– 1338, DOI: 10.1073/pnas.85.5.133459https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaL1cXhs1ClsLk%253D&md5=4e45a4bda6b45a7fa1d505943c820ff1Size of bacterial ice-nucleation sites measured in situ by radiation inactivation analysisGovindarajan, Arepura G.; Lindow, Steven E.Proceedings of the National Academy of Sciences of the United States of America (1988), 85 (5), 1334-8CODEN: PNASA6; ISSN:0027-8424.Four bacterial species are known to catalyze ice formation at temps. just below 0°. To better understand the relation between the mol. structure of bacterial ice-nucleation site(s) and the quant. qual. features of the ice-nucleation-active phenotype, γ-radiation anal. was used to det. the in situ size of ice-nucleation sites in strains of Pseudomonas syringae and Erwinia herbicola and in Escherichia coli HB101 carrying the plasmid pICE1.1 (contg. a 4-kilobase DNA insert from P. syringae that confers ice-nucleation activity). Lyophilized cells of each bacterial strain were irradiated with a flux of γ-radiation from 0 to 10.2 Mrad (1 Mrad = 106 J/kg). Differential concns. of active ice nuclei decreased as a 1st-order function of radiation dose in all strains as temp. was decreased from -2° to -14° in 1° intervals. Sizes of ice nuclei were calcd. from the γ-radiation flux at which 37% of initial ice nuclei active within each 1° temp. interval remained. The min. mass of a functional ice nucleus, active only between -12° and -13°, was ∼150 kDa for all strains. The size of ice nuclei increased logarithmically with increasing temp. from -12° to -2°, where the estd. nucleant mass was 19,000 kDa. The ice nucleant in these 3 bacterial species may represent an oligomeric structure, composed at least in part of an ice gene product that can self-assoc. to assume many possible sizes.
- 60Vali, G.; DeMott, P. J.; Möhler, O.; Whale, T. F. Technical Note: A Proposal for Ice Nucleation Terminology. Atmos. Chem. Phys. 2015, 15 (18), 10263– 10270, DOI: 10.5194/acp-15-10263-201560https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2MXhsFKjtLzM&md5=ab033699b6722f56dad8ab77b8a55399Technical note: a proposal for ice nucleation terminologyVali, G.; DeMott, P. J.; Mohler, O.; Whale, T. F.Atmospheric Chemistry and Physics (2015), 15 (18), 10263-10270CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)Terminol. dealing with ice nucleation in the atm., in biol. systems, and in other areas has not kept pace with the growth of empirical evidence and the development of new ideas over recent decades. Ambiguities and misinterpretations could be seen in the literature. This paper offers a set of definitions for various terms in common use, adds some qualifications, and introduces some new ones. Input has been received on the interpretation of various terms from a fair no. of researchers; diverse views have been accommodated with some success. It is anticipated that the terminol. proposed here will be helpful both to those who adopt it and to those who wish to explain a different perspective.
- 61Marcolli, C.; Gedamke, S.; Peter, T.; Zobrist, B. Efficiency of Immersion Mode Ice Nucleation on Surrogates of Mineral Dust. Atmos. Chem. Phys. 2007, 7 (19), 5081– 5091, DOI: 10.5194/acp-7-5081-200761https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD2sXhtlOnsrvO&md5=5ee33d2e099533fd3799da8e96465b80Efficiency of immersion mode ice nucleation on surrogates of mineral dustMarcolli, C.; Gedamke, S.; Peter, T.; Zobrist, B.Atmospheric Chemistry and Physics (2007), 7 (19), 5081-5091CODEN: ACPTCE; ISSN:1680-7316. (Copernicus Publications)A differential scanning calorimeter (DSC) was used to explore heterogeneous ice nucleation of emulsified aq. suspensions of two Arizona test dust (ATD) samples with particle diams. of nominally 0-3 and 0-7 μm, resp. Aq. suspensions with ATD concns. of 0.01-20 wt% have been investigated. The DSC thermograms exhibit a homogeneous and a heterogeneous freezing peak whose intensity ratios vary with the ATD concn. in the aq. suspensions. Homogeneous freezing temps. are in good agreement with recent measurements by other techniques. Depending on ATD concn., heterogeneous ice nucleation occurred at temps. as high as 256 K or down to the onset of homogeneous ice nucleation (237 K). For ATD-induced ice formation Classical Nucleation Theory (CNT) offers a suitable framework to parameterize nucleation rates as a function of temp., exptl. detd. ATD size, and emulsion droplet vol. distributions. The latter two quantities serve to est. the total heterogeneous surface area present in a droplet, whereas the suitability of an individual heterogeneous site to trigger nucleation is described by the compatibility function (or contact angle) in CNT. The intensity ratio of homogeneous to heterogeneous freezing peaks is in good agreement with the assumption that the ATD particles are randomly distributed amongst the emulsion droplets. The obsd. dependence of the heterogeneous freezing temps. on ATD concns. cannot be described by assuming a const. contact angle for all ATD particles, but requires the ice nucleation efficiency of ATD particles to be (log)normally distributed amongst the particles. Best quant. agreement is reached when explicitly assuming that high-compatibility sites are rare and that therefore larger particles have on av. more and better active sites than smaller ones. This anal. suggests that a particle has to have a diam. of at least 0.1 μm to exhibit on av. one active site.
- 62Wang, W.; Nema, S.; Teagarden, D. Protein Aggregation─Pathways and Influencing Factors. Int. J. Pharm. 2010, 390 (2), 89– 99, DOI: 10.1016/j.ijpharm.2010.02.02562https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3cXksFShtL8%253D&md5=bfd8e132dcfbe9d2fcaed1dd013c87c3Protein aggregation-Pathways and influencing factorsWang, Wei; Nema, Sandeep; Teagarden, DirkInternational Journal of Pharmaceutics (2010), 390 (2), 89-99CODEN: IJPHDE; ISSN:0378-5173. (Elsevier B.V.)A review. Proteins generally will tend to aggregate under a variety of environmental conditions in comparison with small drug mols. The extent of aggregation is dependent on many factors that can be broadly classified as intrinsic (primary, secondary, tertiary or quaternary structure) or extrinsic (environment in which protein is present, processing conditions, etc). These protein aggregates may exhibit less desirable characteristics like reduced or no biol. activity, potential for immunogenicity or other side effects. Protein aggregation remains one of the major challenges in the development and commercialization of biotechnol. products. This article is intended to review and discuss the latest understandings in protein aggregation pathways and the possible extrinsic factors that affect or control the protein aggregation process.
- 63Metskas, L. A.; Ortega, D.; Oltrogge, L. M.; Blikstad, C.; Lovejoy, D. R.; Laughlin, T. G.; Savage, D. F.; Jensen, G. J. Rubisco Forms a Lattice inside Alpha-Carboxysomes. Nat. Commun. 2022, 13 (1), 4863, DOI: 10.1038/s41467-022-32584-763https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38Xit1Sltb%252FI&md5=e92fcf3bc8662a6d4d9e3a313d95bfd0Rubisco forms a lattice inside alpha-carboxysomesMetskas, Lauren Ann; Ortega, Davi; Oltrogge, Luke M.; Blikstad, Cecilia; Lovejoy, Derik R.; Laughlin, Thomas G.; Savage, David F.; Jensen, Grant J.Nature Communications (2022), 13 (1), 4863CODEN: NCAOBW; ISSN:2041-1723. (Nature Portfolio)Abstr.: Despite the importance of microcompartments in prokaryotic biol. and bioengineering, structural heterogeneity has prevented a complete understanding of their architecture, ultrastructure, and spatial organization. Here, we employ cryo-electron tomog. to image α-carboxysomes, a pseudo-icosahedral microcompartment responsible for carbon fixation. We have solved a high-resoln. subtomogram av. of the Rubisco cargo inside the carboxysome, and detd. the arrangement of the enzyme. We find that the H. neapolitanus Rubisco polymerizes in vivo, mediated by the small Rubisco subunit. These fibrils can further pack to form a lattice with six-fold pseudo-symmetry. This arrangement preserves freedom of motion and accessibility around the Rubisco active site and the binding sites for two other carboxysome proteins, CsoSCA (a carbonic anhydrase) and the disordered CsoS2, even at Rubisco concns. exceeding 800 μM. This characterization of Rubisco cargo inside the α-carboxysome provides insight into the balance between order and disorder in microcompartment organization.
- 64Guerrero-Mendiola, C.; Oria-Hernández, J.; Ramírez-Silva, L. Kinetics of the Thermal Inactivation and Aggregate Formation of Rabbit Muscle Pyruvate Kinase in the Presence of Trehalose. Arch. Biochem. Biophys. 2009, 490 (2), 129– 136, DOI: 10.1016/j.abb.2009.08.01264https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD1MXht1Ggt77E&md5=f7fc1331a659c91ff2338c0302150094Kinetics of the thermal inactivation and aggregate formation of rabbit muscle pyruvate kinase in the presence of trehaloseGuerrero-Mendiola, Carlos; Oria-Hernandez, Jesus; Ramirez-Silva, LeticiaArchives of Biochemistry and Biophysics (2009), 490 (2), 129-136CODEN: ABBIA4; ISSN:0003-9861. (Elsevier B.V.)In a previous study, the authors found that 30-40% DMSO induces the active conformation of rabbit muscle pyruvate kinase (PK). Because DMSO is known to perturb the structure and function of many proteins, the authors explored the effect of trehalose (I) on the kinetics of thermal inactivation and stability of PK; this is because I, in contrast to DMSO, is totally excluded from the hydration shell of proteins. The results showed that 600 mM I inhibited the activity of PK by ∼20% at 25°; however, I protected PK from thermal inactivation at 60°, increased the apparent Tm of unfolding by 7.2°, induced a more compact state, and stabilized its tetrameric structure. The inactivation process was irreversible due to the formation of protein aggregates. I diminished the rate of formation of intermediates with propensity to aggregate, but did not affect the extent of aggregation. Remarkably, I affected the aggregation process by inducing aggregates with amyloid-like characteristics.
- 65Jiménez, J. L.; Nettleton, E. J.; Bouchard, M.; Robinson, C. V.; Dobson, C. M.; Saibil, H. R. The Protofilament Structure of Insulin Amyloid Fibrils. Proc. Natl. Acad. Sci. U. S. A. 2002, 99 (14), 9196– 9201, DOI: 10.1073/pnas.14245939965https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD38XlsVGgsrc%253D&md5=7e8d178ee6fdb7966f63361cac817d88The protofilament structure of insulin amyloid fibrilsJimenez, Jose L.; Nettleton, Ewan J.; Bouchard, Mario; Robinson, Carol V.; Dobson, Christopher M.; Saibil, Helen R.Proceedings of the National Academy of Sciences of the United States of America (2002), 99 (14), 9196-9201CODEN: PNASA6; ISSN:0027-8424. (National Academy of Sciences)Under soln. conditions where the native state is destabilized, the largely helical polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-β structure. However, there is a lack of information relating the 4.8 Å β-strand repeat to the higher order assembly of amyloid fibrils. We have used cryo-electron microscopy (EM), combining single particle anal. and helical reconstruction, to characterize these fibrils and to study the three-dimensional (3D) arrangement of their component protofilaments. Low-resoln. 3D structures of fibrils contg. 2, 4, and 6 protofilaments reveal a characteristic, compact shape of the insulin protofilament. Considerations of protofilament packing indicate that the cross-β ribbon is composed of relatively flat β-sheets rather than being the highly twisted, β-coil structure previously suggested by anal. of globular protein folds. Comparison of the various fibril structures suggests that very small, local changes in β-sheet twist are important in establishing the long-range coiling of the protofilaments into fibrils of diverse morphol.
- 66Kallberg, Y.; Gustafsson, M.; Persson, B.; Thyberg, J.; Johansson, J. Prediction of Amyloid Fibril-Forming Proteins. J. Biol. Chem. 2001, 276 (16), 12945– 12950, DOI: 10.1074/jbc.M01040220066https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3MXjtFymsro%253D&md5=2a96d3ac44fdd2dd50e026ce51042b14Prediction of amyloid fibril-forming proteinsKallberg, Yvonne; Gustafsson, Magnus; Persson, Bengt; Thyberg, Johan; Johansson, JanJournal of Biological Chemistry (2001), 276 (16), 12945-12950CODEN: JBCHA3; ISSN:0021-9258. (American Society for Biochemistry and Molecular Biology)In Alzheimer's disease and spongiform encephalopathies proteins transform from their native states into fibrils. The authors find that several amyloid-forming proteins harbor an α-helix in a polypeptide segment that should form a β-strand according to secondary structure predictions. In 1324 nonredundant protein structures, 37 β-strands with ≥7 residues were predicted in segments where the exptl. detd. structures show helixes. These discordances include the prion protein (helix 2, positions 179-191), the Alzheimer amyloid β-peptide (Aβ, positions 16-23), and lung surfactant protein C (SP-C, positions 12-27). In addn., human coagulation factor XIII (positions 258-266), triacylglycerol lipase from Candida antarctica (positions 256-266), and D-alanyl-D-alanine transpeptidase from Streptomyces R61 (positions 92-106) contain a discordant helix. These proteins have not been reported to form fibrils but in this study were found to form fibrils in buffered saline at pH 7.4. By replacing valines in the discordant helical part of SP-C with leucines, an α-helix is found exptl. and by secondary structure predictions. This analog does not form fibrils under conditions where SP-C forms abundant fibrils. Likewise, when Aβ residues 14-23 are removed or changed to a nondiscordant sequence, fibrils are no longer formed. The authors propose that α-helix/β-strand-discordant stretches are assocd. with amyloid fibril formation.
- 67Zhou, X.-M.; Entwistle, A.; Zhang, H.; Jackson, A. P.; Mason, T. O.; Shimanovich, U.; Knowles, T. P. J.; Smith, A. T.; Sawyer, E. B.; Perrett, S. Self-Assembly of Amyloid Fibrils That Display Active Enzymes. ChemCatChem 2014, 6 (7), 1961– 1968, DOI: 10.1002/cctc.20140212567https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXptl2ksro%253D&md5=a4150f83efb8e92e82bdbd33aea526ecSelf-Assembly of Amyloid Fibrils That Display Active EnzymesZhou, Xiao-Ming; Entwistle, Aiman; Zhang, Hong; Jackson, Antony P.; Mason, Thomas O.; Shimanovich, Ulyana; Knowles, Tuomas P. J.; Smith, Andrew T.; Sawyer, Elizabeth B.; Perrett, SarahChemCatChem (2014), 6 (7), 1961-1968CODEN: CHEMK3; ISSN:1867-3880. (Wiley-VCH Verlag GmbH & Co. KGaA)Enzyme immobilization is an important strategy to enhance the stability and recoverability of enzymes and to facilitate the sepn. of enzymes from reaction products. However, enzyme purifn. followed by sep. chem. steps to allow immobilization on a solid support reduces the efficiency and yield of the active enzyme. Here we describe polypeptide constructs that self-assemble spontaneously into nanofibrils with fused active enzyme subunits displayed on the amyloid fibril surface. We measured the steady-state kinetic parameters for the appended enzymes in situ within fibrils and compare these with the identical protein constructs in soln. Finally, we demonstrated that the fibrils can be recycled and reused in functional assays both in conventional batch processes and in a continuous-flow microreactor.
- 68Garnham, C. P.; Campbell, R. L.; Walker, V. K.; Davies, P. L. Novel Dimeric β-Helical Model of an Ice Nucleation Protein with Bridged Active Sites. BMC Struct. Biol. 2011, 11 (1), 1– 12, DOI: 10.1186/1472-6807-11-36There is no corresponding record for this reference.
- 69Qiu, Y.; Hudait, A.; Molinero, V. How Size and Aggregation of Ice-Binding Proteins Control Their Ice Nucleation Efficiency. J. Am. Chem. Soc. 2019, 141 (18), 7439– 7452, DOI: 10.1021/jacs.9b0185469https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXntlehsb0%253D&md5=69f5e714689808c09543511275bd615aHow Size and Aggregation of Ice-Binding Proteins Control Their Ice Nucleation EfficiencyQiu, Yuqing; Hudait, Arpa; Molinero, ValeriaJournal of the American Chemical Society (2019), 141 (18), 7439-7452CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)Organisms that thrive at cold temps. produce ice-binding proteins to manage the nucleation and growth of ice. Bacterial ice-nucleating proteins (INP) are typically large and form aggregates in the cell membrane, while insect hyperactive antifreeze proteins (AFP) are sol. and generally small. Expts. indicate that larger ice-binding proteins and their aggregates nucleate ice at warmer temps. Nevertheless, a quant. understanding of how size and aggregation of ice-binding proteins det. the temp. Thet at which proteins nucleate ice is still lacking. Here, we address this question using mol. simulations and nucleation theory. The simulations indicate that the 2.5 nm long antifreeze protein TmAFP nucleates ice at 2 ± 1 °C above the homogeneous nucleation temp., in good agreement with recent expts. We predict that the addn. of ice-binding loops to TmAFP increases Thet, but not enough to compete in efficiency with the bacterial INP. We implement an accurate procedure to det. Thet of surfaces of finite size using classical nucleation theory, and, after validating the theory against Thet of the proteins in mol. simulations, we use it to predict Thet of the INP of Ps. syringae as a function of the length and no. of proteins in the aggregates. We conclude that assemblies with at most 34 INP already reach the Thet = -2 °C characteristic of this bacterium. Interestingly, we find that Thet is a strongly varying nonmonotonic function of the distance between proteins in the aggregates. This indicates that, to achieve max. freezing efficiency, bacteria must exert exquisite, subangstrom control of the distance between INP in their membrane.
- 70Hudait, A.; Odendahl, N.; Qiu, Y.; Paesani, F.; Molinero, V. Ice-Nucleating and Antifreeze Proteins Recognize Ice through a Diversity of Anchored Clathrate and Ice-like Motifs. J. Am. Chem. Soc. 2018, 140 (14), 4905– 4912, DOI: 10.1021/jacs.8b0124670https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXlt1Kku7g%253D&md5=ede99e9416d945280adcc57d6453911aIce-Nucleating and Antifreeze Proteins Recognize Ice through a Diversity of Anchored Clathrate and Ice-like MotifsHudait, Arpa; Odendahl, Nathan; Qiu, Yuqing; Paesani, Francesco; Molinero, ValeriaJournal of the American Chemical Society (2018), 140 (14), 4905-4912CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)Cold-adapted organisms produce antifreeze proteins (AFPs) and ice-nucleating proteins (INPs) to prevent and promote ice formation. The crystal structure of hyperactive bacterial (Marinomonas primoryensis) MpAFP, suggested that this protein binds ice through an anchored clathrate motif. It is not known whether other hyperactive AFPs and INPs use the same motif to recognize or nucleate ice. Here, we used mol. dynamics (MD) simulations to elucidate the ice-binding motifs of hyperactive insect AFPs and a model INP of Pseudomonas syringae (Ps). We found that insect AFPs recognized ice through anchored clathrate motifs distinct from that of MpAFP. By performing MD simulations of ice nucleation by PsINP, we identified 2 distinct ice-binding sites on opposite sides of the β-helix. The ice-nucleating sequences identified in the MD simulations agreed with those previously proposed for the closely related INP of Pseudomonas borealis based on the structure of the protein. The MD simulations indicated that these sites have comparable ice nucleating efficiency, but distinct binding motifs, controlled by the amino acid sequence: one is anchored clathrate and the other ice-like. We conclude that anchored clathrate and ice-like motifs can be equally effective for binding proteins to ice and promoting ice nucleation.
- 71Pandey, R.; Usui, K.; Livingstone, R. A.; Fischer, S. A.; Pfaendtner, J.; Backus, E. H. G.; Nagata, Y.; Fröhlich-Nowoisky, J.; Schmüser, L.; Mauri, S.; Scheel, J. F.; Knopf, D. A.; Pöschl, U.; Bonn, M.; Weidner, T. Ice-Nucleating Bacteria Control the Order and Dynamics of Interfacial Water. Sci. Adv. 2016, 2 (4), e1501630 DOI: 10.1126/sciadv.1501630There is no corresponding record for this reference.
- 72Roeters, S. J.; Golbek, T. W.; Bregnhøj, M.; Drace, T.; Alamdari, S.; Roseboom, W.; Kramer, G.; Šantl-Temkiv, T.; Finster, K.; Pfaendtner, J.; Woutersen, S.; Boesen, T.; Weidner, T. Ice-Nucleating Proteins Are Activated by Low Temperatures to Control the Structure of Interfacial Water. Nat. Commun. 2021, 12 (1), 1183, DOI: 10.1038/s41467-021-21349-372https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXltFyju7o%253D&md5=d6c85611953ef60940e328827610e4ccIce-nucleating proteins are activated by low temperatures to control the structure of interfacial waterRoeters, Steven J.; Golbek, Thaddeus W.; Bregnhoej, Mikkel; Drace, Taner; Alamdari, Sarah; Roseboom, Winfried; Kramer, Gertjan; Santl-Temkiv, Tina; Finster, Kai; Pfaendtner, Jim; Woutersen, Sander; Boesen, Thomas; Weidner, TobiasNature Communications (2021), 12 (1), 1183CODEN: NCAOBW; ISSN:2041-1723. (Nature Research)Abstr.: Ice-nucleation active (INA) bacteria can promote the growth of ice more effectively than any other known material. Using specialized ice-nucleating proteins (INPs), they obtain nutrients from plants by inducing frost damage and, when airborne in the atm., they drive ice nucleation within clouds, which may affect global pptn. patterns. Despite their evident environmental importance, the mol. mechanisms behind INP-induced freezing have remained largely elusive. We investigate the structural basis for the interactions between water and the ice-nucleating protein InaZ from the INA bacterium Pseudomonas syringae. Using vibrational sum-frequency generation (SFG) and two-dimensional IR spectroscopy, we demonstrate that the ice-active repeats of InaZ adopt a β-helical structure in soln. and at water surfaces. In this configuration, interaction between INPs and water mols. imposes structural ordering on the adjacent water network. The obsd. order of water increases as the interface is cooled to temps. close to the m.p. of water. Exptl. SFG data combined with mol.-dynamics simulations and spectral calcns. show that InaZ reorients at lower temps. This reorientation can enhance water interactions, and thereby the effectiveness of ice nucleation.
- 73Aller, J. Y.; Radway, J. C.; Kilthau, W. P.; Bothe, D. W.; Wilson, T. W.; Vaillancourt, R. D.; Quinn, P. K.; Coffman, D. J.; Murray, B. J.; Knopf, D. A. Size-Resolved Characterization of the Polysaccharidic and Proteinaceous Components of Sea Spray Aerosol. Atmos. Environ. 2017, 154, 331– 347, DOI: 10.1016/j.atmosenv.2017.01.05373https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2sXislKjsrY%253D&md5=38679c7dc06d69fc4cc6413e090d3d97Size-resolved characterization of the polysaccharidic and proteinaceous components of sea spray aerosolAller, Josephine Y.; Radway, JoAnn C.; Kilthau, Wendy P.; Bothe, Dylan W.; Wilson, Theodore W.; Vaillancourt, Robert D.; Quinn, Patricia K.; Coffman, Derek J.; Murray, Benjamin J.; Knopf, Daniel A.Atmospheric Environment (2017), 154 (), 331-347CODEN: AENVEQ; ISSN:1352-2310. (Elsevier Ltd.)Dissolved org. polymers released by phytoplankton and bacteria abiol. self-assemble in surface ocean waters into nano-to micro-sized gels contg. polysaccharides, proteins, lipids and other components. These gels conc. in the sea surface microlayer (SML), where they can potentially contribute to sea spray aerosol (SSA). Sea spray is a major source of atm. aerosol mass over much of the earth's surface, and knowledge of its properties (including the amt. and nature of the org. content), size distributions and fluxes are fundamental for detg. its role in atm. chem. and climate. Using a cascade impactor, we collected size-fractionated aerosol particles from ambient air and from freshly generated Sea Sweep SSA in the western North Atlantic Ocean together with biol. and chem. characterization of subsurface and SML waters. Spectrophotometric methods were applied to quantify the polysaccharide-contg. transparent exopolymer (TEP) and protein-contg. Coomassie stainable material (CSM) in these particles and waters. This study demonstrates that both TEP and CSM in surface ocean waters are aerosolized with sea spray with the greatest total TEP assocd. with particles <180 nm in diam. and >5 000 nm. The higher concns. of TEP and CSM in particles >5 000 nm most likely reflects collection of microorganism cells and/or fragments. The greater concn. of CSM in larger size particles may also reflect greater stability of proteinaceous gels compared to polysaccharide-rich gels in surface waters and the SML. Both TEP and CSM were measured in the ambient marine air sample with concns. of 2.1 ± 0.16μg xanthan gum equiv. (XG eq.) m-3 and 14 ± 1.0μg bovine serum albumin equiv. (BSA eq.) m-3. TEP in Sea Sweep SSA averaged 4.7 ± 3.1μg XG eq. m-3 and CSM 8.6 ± 7.3μg BSA eq. m-3. This work shows the transport of marine biogenic material across the air-sea interface through primary particle emission and the first demonstration of particle size discriminated TEP and CSM characterization of SSA and ambient aerosol under field conditions.
- 74Alsante, A. N.; Thornton, D. C. O.; Brooks, S. D. Ocean Aerobiology. Front. Microbiol. 2021, 12, 764178 DOI: 10.3389/fmicb.2021.76417874https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BB2cfjtVSmtQ%253D%253D&md5=dabf1d381f8d0f3b7f021cccf8f3b194Ocean AerobiologyAlsante Alyssa N; Thornton Daniel C O; Brooks Sarah DFrontiers in microbiology (2021), 12 (), 764178 ISSN:1664-302X.Ocean aerobiology is defined here as the study of biological particles of marine origin, including living organisms, present in the atmosphere and their role in ecological, biogeochemical, and climate processes. Hundreds of trillions of microorganisms are exchanged between ocean and atmosphere daily. Within a few days, tropospheric transport potentially disperses microorganisms over continents and between oceans. There is a need to better identify and quantify marine aerobiota, characterize the time spans and distances of marine microorganisms' atmospheric transport, and determine whether microorganisms acclimate to atmospheric conditions and remain viable, or even grow. Exploring the atmosphere as a microbial habitat is fundamental for understanding the consequences of dispersal and will expand our knowledge of biodiversity, biogeography, and ecosystem connectivity across different marine environments. Marine organic matter is chemically transformed in the atmosphere, including remineralization back to CO2. The magnitude of these transformations is insignificant in the context of the annual marine carbon cycle, but may be a significant sink for marine recalcitrant organic matter over long (∼10(4) years) timescales. In addition, organic matter in sea spray aerosol plays a significant role in the Earth's radiative budget by scattering solar radiation, and indirectly by affecting cloud properties. Marine organic matter is generally a poor source of cloud condensation nuclei (CCN), but a significant source of ice nucleating particles (INPs), affecting the formation of mixed-phase and ice clouds. This review will show that marine biogenic aerosol plays an impactful, but poorly constrained, role in marine ecosystems, biogeochemical processes, and the Earth's climate system. Further work is needed to characterize the connectivity and feedbacks between the atmosphere and ocean ecosystems in order to integrate this complexity into Earth System models, facilitating future climate and biogeochemical predictions.
- 75Choi, J. H.; Jang, E.; Yoon, Y. J.; Park, J. Y.; Kim, T.-W.; Becagli, S.; Caiazzo, L.; Cappelletti, D.; Krejci, R.; Eleftheriadis, K.; Park, K.-T.; Jang, K. S. Influence of Biogenic Organics on the Chemical Composition of Arctic Aerosols. Global Biogeochem. Cycles 2019, 33 (10), 1238– 1250, DOI: 10.1029/2019GB00622675https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXhvFKrsbnK&md5=c1ad390ba5cd44c45d01c06f75345e3aInfluence of Biogenic Organics on the Chemical Composition of Arctic AerosolsChoi, J. H.; Jang, E.; Yoon, Y. J.; Park, J. Y.; Kim, T.-W.; Becagli, S.; Caiazzo, L.; Cappelletti, D.; Krejci, R.; Eleftheriadis, K.; Park, K.-T.; Jang, K. S.Global Biogeochemical Cycles (2019), 33 (10), 1238-1250CODEN: GBCYEP; ISSN:1944-9224. (Wiley-Blackwell)We use an ultrahigh-resoln. 15-T Fourier transform ion cyclotron resonance mass spectrometer to elucidate the compositional changes in Arctic org. aerosols collected at Ny-Ålesund, Svalbard, in May 2015. The Fourier transform ion cyclotron resonance mass spectrometer anal. of airborne org. matter provided information on the mol. compns. of aerosol particles collected during the Arctic spring period. The air mass transport history, combined with satellite-derived geog. information and chlorophyll concn. data, revealed that the mol. compns. of org. aerosols drastically differed depending on the origin of the potential source region. The protein and lignin compd. populations contributed more than 70% of the total intensity of assigned mols. when the air masses mainly passed over the ocean region. Interestingly, the intensity of microbe-derived orgs. (protein and carbohydrate compds.) was pos. correlated with the air mass exposure to phytoplankton biomass proxied as chlorophyll. Furthermore, the intensities of lignin and unsatd. hydrocarbon compds., typically derived from terrestrial vegetation, increased with an increase in the advection time of the air mass over the ocean domain. These results suggest that the accumulation of dissolved biogenic orgs. in the Arctic Ocean possibly derived from both phytoplankton and terrestrial vegetation could significantly influence the chem. properties of Arctic org. aerosols during a productive spring period. The interpretation of mol. changes in org. aerosols using an ultrahigh-resoln. mass spectrometer could provide deep insight for understanding org. aerosols in the atm. over the Arctic and the relationship of org. aerosols with biogeochem. processes in terms of aerosol formation and environmental changes.
- 76O’Sullivan, D.; Murray, B. J.; Ross, J. F.; Webb, M. E. The Adsorption of Fungal Ice-Nucleating Proteins on Mineral Dusts: A Reservoir of Atmospheric Ice-Nucleating Particles. Atmos. Chem. Phys. 2016, 16 (12), 7879– 7887, DOI: 10.5194/acp-16-7879-201676https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28Xhs1Oqu7jJ&md5=ccbaf214158cfd675a663064c979c46bThe adsorption of fungal ice-nucleating proteins on mineral dusts: a terrestrial reservoir of atmospheric ice-nucleating particlesO'Sullivan, Daniel; Murray, Benjamin J.; Ross, James F.; Webb, Michael E.Atmospheric Chemistry and Physics (2016), 16 (12), 7879-7887CODEN: ACPTCE; ISSN:1680-7324. (Copernicus Publications)The occurrence of ice-nucleating particles (INPs) in our atm. has a profound impact on the properties and lifetime of supercooled clouds. To date, the identities, sources and abundances of particles capable of nucleating ice at relatively low supercoolings (T >-15 °C) remain enigmatic. While biomols. such as proteins and carbohydrates have been implicated as important high-temp. INPs, the lack of knowledge on the environmental fates of these species makes it difficult to assess their potential atm. impacts. Here we show that such nanoscale ice-nucleating proteins from a common soil-borne fungus (Fusarium avenaceum) preferentially bind to and confer their ice-nucleating properties to kaolinite. The ice-nucleating activity of the proteinaceous INPs is unaffected by adsorption to the clay, and once bound the proteins do not readily desorb, retaining much of the activity even after multiple washings with pure water. The atm. implications of the finding that biol. residues can confer their ice-nucleating ability to dust particles are discussed.
- 77Roulston, T. H.; Cane, J. H.; Buchmann, S. L. What Governs Protein Content of Pollen: Preferences, Pollen-Pistil Interactions, or Phylogeny?. Ecol. Monogr. 2000, 70 (4), 617– 643, DOI: 10.1890/0012-9615(2000)070[0617:WGPCOP]2.0.CO;2There is no corresponding record for this reference.
- 78Hendrickson, B. N.; Alsante, A. N.; Brooks, S. D. Live Oak Pollen as a Source of Atmospheric Particles. Aerobiologia 2023, 39 (1), 51– 67, DOI: 10.1007/s10453-022-09773-4There is no corresponding record for this reference.
- 79Orellana, M. V.; Matrai, P. A.; Leck, C.; Rauschenberg, C. D.; Lee, A. M.; Coz, E. Marine Microgels as a Source of Cloud Condensation Nuclei in the High Arctic. Proc. Natl. Acad. Sci. U. S. A. 2011, 108 (33), 13612– 13617, DOI: 10.1073/pnas.110245710879https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXhtV2ms7jN&md5=c0c445fdccb5f9cf22ab0b0c6c3dcc19Marine microgels as a source of cloud condensation nuclei in the high ArcticOrellana, Monica V.; Matrai, Patricia A.; Leck, Caroline; Rauschenberg, Carlton D.; Lee, Allison M.; Coz, EstherProceedings of the National Academy of Sciences of the United States of America (2011), 108 (33), 13612-13617, S13612/1-S13612/4CODEN: PNASA6; ISSN:0027-8424. (National Academy of Sciences)Marine microgels play an important role in regulating ocean basin-scale biogeochem. dynamics. In this paper, we demonstrate that, in the high Arctic, marine gels with unique physicochem. characteristics originate in the org. material produced by ice algae and/or phytoplankton in the surface water. The polymers in this dissolved org. pool assembled faster and with higher microgel yields than at other latitudes. The reversible phase transitions shown by these Arctic marine gels, as a function of pH, dimethylsulfide, and dimethylsulfoniopropionate concns., stimulate the gels to attain sizes below 1 μm in diam. These marine gels were identified with an antibody probe specific toward material from the surface waters, sized, and quantified in airborne aerosol, fog, and cloud water, strongly suggesting that they dominate the available cloud condensation nuclei no. population in the high Arctic (north of 80° N) during the summer season. Knowledge about emergent properties of marine gels provides important new insights into the processes controlling cloud formation and radiative forcing, and links the biol. at the ocean surface with cloud properties and climate over the central Arctic Ocean and, probably, all oceans.
- 80Jassey, V. E. J.; Walcker, R.; Kardol, P.; Geisen, S.; Heger, T.; Lamentowicz, M.; Hamard, S.; Lara, E. Contribution of Soil Algae to the Global Carbon Cycle. New Phytol. 2022, 234 (1), 64– 76, DOI: 10.1111/nph.1795080https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XhtFektb%252FL&md5=5ee47536aa139ab6c9000c9e0bd92593Contribution of soil algae to the global carbon cycleJassey, Vincent E. J.; Walcker, Romain; Kardol, Paul; Geisen, Stefan; Heger, Thierry; Lamentowicz, Mariusz; Hamard, Samuel; Lara, EnriqueNew Phytologist (2022), 234 (1), 64-76CODEN: NEPHAV; ISSN:0028-646X. (Wiley-Blackwell)A review. Soil photoautotrophic prokaryotes and micro-eukaryotes - known as soil algae - are, together with heterotrophic microorganisms, a constitutive part of the microbiome in surface soils. Similar to plants, they fix atm. carbon (C) through photosynthesis for their own growth, yet their contribution to global and regional biogeochem. C cycling still remains quant. elusive. Here, we compiled an extensive dataset on soil algae to generate a better understanding of their distribution across biomes and predict their productivity at a global scale by means of machine learning modeling. We found that, on av., (5.5 ± 3.4) x 106 algae inhabit each gram of surface soil. Soil algal abundance esp. peaked in acidic, moist and vegetated soils. We est. that, globally, soil algae take up around 3.6 Pg C per yr, which corresponds to c. 6% of the net primary prodn. of terrestrial vegetation. We demonstrate that the C fixed by soil algae is crucial to the global C cycle and should be integrated into land-based efforts to mitigate C emissions.
- 81Rastelli, E.; Corinaldesi, C.; Dell’anno, A.; Lo Martire, M.; Greco, S.; Cristina Facchini, M.; Rinaldi, M.; O’Dowd, C.; Ceburnis, D.; Danovaro, R. Transfer of Labile Organic Matter and Microbes from the Ocean Surface to the Marine Aerosol: An Experimental Approach. Sci. Rep. 2017, 7 (1), 1– 10, DOI: 10.1038/s41598-017-10563-z81https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXhtlyhtrrK&md5=9cf1be99ffe93fc0dccc5566069f3519Transfer of labile organic matter and microbes from the ocean surface to the marine aerosol: an experimental approachRastelli, Eugenio; Corinaldesi, Cinzia; Dell'Anno, Antonio; Lo Martire, Marco; Greco, Silvestro; Cristina Facchini, Maria; Rinaldi, Matteo; O'Dowd, Colin; Ceburnis, Darius; Danovaro, RobertoScientific Reports (2017), 7 (1), 1-10CODEN: SRCEC3; ISSN:2045-2322. (Nature Research)Surface ocean bubble-bursting generates aerosols composed of microscopic salt-water droplets, enriched in marine org. matter. The org. fraction profoundly influences aerosols' properties, by scattering solar radiations and nucleating water particles. Still little is known on the biochem. and microbiol. compn. of these org. particles. In the present study, we exptl. simulated the bursting of bubbles at the seawater surface of the North-Eastern Atlantic Ocean, analyzing the org. materials and the diversity of the bacteria in the source-seawaters and in the produced aerosols. We show that, compared with seawater, the sub-micron aerosol particles were highly enriched in org. matter (up to 140,000x for lipids, 120,000x for proteins and 100,000x for carbohydrates). Also DNA, viruses and prokaryotes were significantly enriched (up to 30,000, 250 and 45x, resp.). The relative importance of the org. components in the aerosol did not reflect those in the seawater, suggesting their selective transfer. Mol. analyses indicate the presence of selective transfers also for bacterial genotypes, highlighting higher contribution of less abundant seawater bacterial taxa to the marine aerosol. Overall, our results open new perspectives in the study of microbial dispersal through marine aerosol and provide new insights for a better understanding of climate-regulating processes of global relevance.
- 82Schiffer, J. M.; Luo, M.; Dommer, A. C.; Thoron, G.; Pendergraft, M.; Santander, M. V.; Lucero, D.; Pecora De Barros, E.; Prather, K. A.; Grassian, V. H.; Amaro, R. E. Impacts of Lipase Enzyme on the Surface Properties of Marine Aerosols. J. Phys. Chem. Lett. 2018, 9 (14), 3839– 3849, DOI: 10.1021/acs.jpclett.8b0136382https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXhtFKlsr%252FN&md5=f30afeed06f7821398f3d4025c8fc8b6Impacts of Lipase Enzyme on the Surface Properties of Marine AerosolsSchiffer, J. M.; Luo, M.; Dommer, A. C.; Thoron, G.; Pendergraft, M.; Santander, M. V.; Lucero, D.; Pecora de Barros, E.; Prather, K. A.; Grassian, V. H.; Amaro, R. E.Journal of Physical Chemistry Letters (2018), 9 (14), 3839-3849CODEN: JPCLCD; ISSN:1948-7185. (American Chemical Society)Triacylglycerol lipases have recently been shown to be transferred from the ocean to the atm. in atm. sea spray aerosol (SSA). Lipases have the potential to alter the compn. of SSA, however the structure and properties of enzymes in the high salt, high ionic strength and low pH conditions found in SSA have never been explored. Here, we study the dynamics of Burkholderia cepacia triacylglycerol lipase (BCL) at SSA model surfaces comprised of palmitic acid and dipalmitoylphosphatidic acid (DPPA), two commonly found lipids at SSA surfaces. Surface adsorption Langmuir isotherm expts. and all-atom explicit solvent mol. dynamics simulations together illuminate how and why BCL expands the ordering of lipids at palmitic acid surfaces the most at pH <4 and the least in DPPA surfaces at pH 6. Taken together, these results represent a first glimpse into the complex interplay between lipid surface structure and protein dynamics within enzyme-contg. aerosols.
- 83Orellana, M. V.; Hansell, D. A. Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (RuBisCO): A Long-Lived Protein in the Deep Ocean. Limnol. Oceanogr. 2012, 57 (3), 826– 834, DOI: 10.4319/lo.2012.57.3.082683https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38XhtVOmt77O&md5=6e4452aea99a0acdd54ab7bd7fb0f061Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): a long-lived protein in the deep oceanOrellana, Monica V.; Hansell, Dennis A.Limnology and Oceanography (2012), 57 (3), 826-834CODEN: LIOCAH; ISSN:0024-3590. (American Society of Limnology and Oceanography)We demonstrate that the distribution of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) in the deep North Pacific is a unique tracer for the accumulation of biochem. identifiable org. residue of the export flux. RuBisCO is found both dissolved and assembled in microgels in a dynamic gel-to-dissolved-to-gel continuum that may protect RuBisCO from degrdn. in the water column. High concns. are located below biol. productive equatorial and subarctic systems, and low concns. are assocd. with the subtropical gyre. RuBisCO tracks the advective transport of export products along deep circulation pathways of the ocean interior, serving as a quantifiable biochem. tracer of modern org. carbon exported to and resident in the deep ocean.
- 84Vlasak, J.; Ionescu, R. Fragmentation of monoclonal antibodies. mAbs 2011, 3 (3), 253– 263, DOI: 10.4161/mabs.3.3.1560884https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A280%3ADC%252BC3MnmtVShuw%253D%253D&md5=8dc0db491ca9207313bdd613771a18cbFragmentation of monoclonal antibodiesVlasak Josef; Ionescu RoxanamAbs (2011), 3 (3), 253-63 ISSN:.Fragmentation is a degradation pathway ubiquitously observed in proteins despite the remarkable stability of peptide bond; proteins differ only by how much and where cleavage occurs. The goal of this review is to summarize reports regarding the non-enzymatic fragmentation of the peptide backbone of monoclonal antibodies (mAbs). The sites in the polypeptide chain susceptible to fragmentation are determined by a multitude of factors. Insights are provided on the intimate chemical mechanisms that can make some bonds prone to cleavage due to the presence of specific side-chains. In addition to primary structure, the secondary, tertiary and quaternary structures have a significant impact in modulating the distribution of cleavage sites by altering local flexibility, accessibility to solvent or bringing in close proximity side chains that are remote in sequence. This review focuses on cleavage sites observed in the constant regions of mAbs, with special emphasis on hinge fragmentation. The mechanisms responsible for backbone cleavage are strongly dependent on pH and can be catalyzed by metals or radicals. The distribution of cleavage sites are different under acidic compared to basic conditions, with fragmentation rates exhibiting a minimum in the pH range 5 to 6; therefore, the overall fragmentation pattern observed for a mAb is a complex result of structural and solvent conditions. A critical review of the techniques used to monitor fragmentation is also presented; usually a compromise has to be made between a highly sensitive method with good fragment separation and the capability to identify the cleavage site. The effect of fragmentation on the function of a mAb must be evaluated on a case-by-case basis depending on whether cleavage sites are observed in the variable or constant regions, and on the mechanism of action of the molecule.
- 85Schuster, J.; Mahler, H. C.; Joerg, S.; Huwyler, J.; Mathaes, R. Analytical challenges assessing protein aggregation and fragmentation under physiologic conditions. J. Pharm. Sci. 2021, 110 (9), 3103– 3110, DOI: 10.1016/j.xphs.2021.04.01485https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXhsVKks77J&md5=7a4ca9a1aa06ee046dbb202ce59bc2b5Analytical Challenges Assessing Protein Aggregation and Fragmentation Under Physiologic ConditionsSchuster, Joachim; Mahler, Hanns-Christian; Joerg, Susanne; Huwyler, Joerg; Mathaes, RomanJournal of Pharmaceutical Sciences (Philadelphia, PA, United States) (2021), 110 (9), 3103-3110CODEN: JPMSAE; ISSN:0022-3549. (Elsevier Inc.)A review. Therapeutic proteins are administered by injection or infusion. After administration, the physiol. environment in the desired body compartment - fluid or tissue - can impact protein stability and lead to changes in the safety and/or efficacy profile. For example, protein aggregation and fragmentation are crit. quality attributes of the drug product and can occur after administration to patients. In this context, the in vivo stability of therapeutic proteins has gained increasing attention. However, in vivo protein aggregation and fragmentation are difficult to assess and have been rarely investigated. This mini-review summarizes anal. approaches to assess the stability of therapeutic proteins using simulated physiol. conditions. Furthermore, we discuss factors potentially causing in vivo protein aggregation, pptn., and fragmentation in complex biol. fluids. Different anal. approaches are evaluated with respect to their applicability and possible shortcomings when it comes to these degrdn. events in biol. fluids. Tracking protein stability in biol. fluids typically requires purifying or labeling the protein of interest to circumvent matrix interference of biol. fluids. Improved anal. methods are strongly needed to gain knowledge on in vivo protein aggregation and fragmentation. In vitro models can support the selection of lead candidates and accelerate the pre-clin. development of therapeutic proteins.
- 86Yang, A. S.; Honig, B. On the pH dependence of protein stability. J. Mol. Biol. 1993, 231 (2), 459– 474, DOI: 10.1006/jmbi.1993.129486https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADyaK3sXkvV2nsL4%253D&md5=7334f6169de93d04c6168841fc597f4bOn the pH dependence of protein stabilityYang, An Suei; Honig, BarryJournal of Molecular Biology (1993), 231 (2), 459-74CODEN: JMOBAK; ISSN:0022-2836.The free energy contribution of ionizable groups to protein stability is treated here. A method is presented for the calcn. of the pH dependence of the denaturation free energy of a protein, which yields results that can be compared directly to expt. The first step in the treatment is the detn. of the av. charges of all the ionizable groups in both the folded and unfolded protein. An expression due to Tanford then relates the pH dependence of the unfolding free energy to the difference in net charge between the two states. In order to det. abs. rather than relative unfolding free energies, it is necessary to calc. the total contribution of ionizable groups to protein stability at some ref. pH. This is accomplished through a statistical mech. treatment similar to the one used previously in the calcn. of pKas. The treatment itself is rigorous but it suffers from uncertainties in the pKa calcns. Nevertheless, the overall shape of exptl. obsd. plots of denaturation free energy as a function of pH are exptl. well reproduced by the calcns. A no. of general conclusions that arise from the anal. are: (1) knowledge of titrn. curves and/or effective pKa values of ionizable groups in proteins is sufficient to calc. the pH dependence of the denaturation free energy with resp. to some ref. pH value. However, in order to calc. the abs. contribution of ionizable groups to protein stability, it is necessary to also know the intrinsic pKa of each group. This is defined as the pKa of a group in a hypothetical state of the protein where all other groups are neutral. (2) Due to desolvation effects, ionizable groups destabilize proteins, although the effect is strongly dependent on pH. There are however, strongly stabilizing pairwise Coulombic interactions on the surface of proteins. (3) Plots of stability vs. pH should not be interpreted in terms of a group whose pKa corresponds to the titrn. midpoint, but rather to a group with different pKas (that correspond approx. to the titrn. end points) in each state. (4) Any residual structure in the GuHCl-denatured state of proteins appears to have little effect on the pH dependence of stability. (5) PH-dependent unfolding, for example to the "molten globule" state, appears due to individual groups with anomalous pKas whose locations on the protein surface may det. the nature of the unfolded state.
- 87Weids, A. J.; Ibstedt, S.; Tamás, M. J.; Grant, C. M. Distinct Stress Conditions Result in Aggregation of Proteins with Similar Properties. Sci. Rep. 2016, 6 (1), 24554, DOI: 10.1038/srep2455487https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28Xmt1ensLs%253D&md5=b30ca7d5196760f8ec785573d97130ffDistinct stress conditions result in aggregation of proteins with similar propertiesWeids, Alan J.; Ibstedt, Sebastian; Tamas, Markus J.; Grant, Chris M.Scientific Reports (2016), 6 (), 24554CODEN: SRCEC3; ISSN:2045-2322. (Nature Publishing Group)Protein aggregation is the abnormal assocn. of proteins into larger aggregate structures which tend to be insol. This occurs during normal physiol. conditions and in response to age or stress-induced protein misfolding and denaturation. In this present study we have defined the range of proteins that aggregate in yeast cells during normal growth and after exposure to stress conditions including an oxidative stress (hydrogen peroxide), a heavy metal stress (arsenite) and an amino acid analog (azetidine-2-carboxylic acid). Our data indicate that these three stress conditions, which work by distinct mechanisms, promote the aggregation of similar types of proteins probably by lowering the threshold of protein aggregation. The proteins that aggregate during physiol. conditions and stress share several features; however, stress conditions shift the criteria for protein aggregation propensity. This suggests that the proteins in aggregates are intrinsically aggregation-prone, rather than being proteins which are affected in a stress-specific manner. We addnl. identified significant overlaps between stress aggregating yeast proteins and proteins that aggregate during ageing in yeast and C. elegans. We suggest that similar mechanisms may apply in disease- and non-disease settings and that the factors and components that control protein aggregation may be evolutionary conserved.
- 88Mauri, S.; Pandey, R.; Rzeznicka, I.; Lu, H.; Bonn, M.; Weidner, T. Bovine and Human Insulin Adsorption at Lipid Monolayers: A Comparison. Front Phys. 2015, 3, 51, DOI: 10.3389/fphy.2015.00051There is no corresponding record for this reference.
Supporting Information
Supporting Information
The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.est.3c06835.
Immersion mode ice nucleation data (Supporting Table 1), non-parametric ANOVA of the nucleation temperature (Supporting Table 2), freezing temperature of RuBisCO (2 × 10–1) and the procedural blank over repeated freeze–thaw cycles (Supporting Figure 1), hydrodynamic diameter distribution by number-derived intensity (Supporting Figure 2), fraction of droplets frozen of RuBisCO from this study from 2 × 10–1 to 2 × 10–5 mg mL–1 and Alsante et al. (33) at 5 × 10–1 mg mL–1 (Supporting Figure 3), relative frequency of the 20 amino acids from each protein (Supporting Figure 4), and relative frequency of amino acid functional groups for each protein (Supporting Figure 5) (PDF)
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