ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

Figure 1Loading Img

Comparison of .alpha.-lactalbumin and lysozyme using vibrational circular dichroism. Evidence for a difference in crystal and solution structures

Cite this: Biochemistry 1991, 30, 43, 10479–10485
Publication Date (Print):October 1, 1991
https://doi.org/10.1021/bi00107a016
    ACS Legacy Archive

    Article Views

    243

    Altmetric

    -

    Citations

    LEARN ABOUT THESE METRICS
    Other access options

    Note: In lieu of an abstract, this is the article's first page.

    Free first page

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    Cited By

    This article is cited by 45 publications.

    1. Yamuna Phal, Kevin Yeh, Rohit Bhargava. Concurrent Vibrational Circular Dichroism Measurements with Infrared Spectroscopic Imaging. Analytical Chemistry 2021, 93 (3) , 1294-1303. https://doi.org/10.1021/acs.analchem.0c00323
    2. Timothy A. Keiderling. Structure of Condensed Phase Peptides: Insights from Vibrational Circular Dichroism and Raman Optical Activity Techniques. Chemical Reviews 2020, 120 (7) , 3381-3419. https://doi.org/10.1021/acs.chemrev.9b00636
    3. Alessandra Giugliarelli, Paola Sassi, Marco Paolantoni, Assunta Morresi, Rina Dukor, and Laurence Nafie . Vibrational Circular Dichroism Spectra of Lysozyme Solutions: Solvent Effects on Thermal Denaturation Processes. The Journal of Physical Chemistry B 2013, 117 (9) , 2645-2652. https://doi.org/10.1021/jp311268x
    4. Elizabeth M. Storch and Valerie Daggett. Molecular Dynamics Simulation of Cytochrome b5: Implications for Protein-Protein Recognition. Biochemistry 1995, 34 (30) , 9682-9693. https://doi.org/10.1021/bi00030a005
    5. Petr Pancoska, Martin Blazek, and Timothy A. Keiderling. Relationships between secondary structure fractions for globular proteins. Neural network analyses of crystallographic data sets. Biochemistry 1992, 31 (42) , 10250-10257. https://doi.org/10.1021/bi00157a011
    6. Monika Krupová, Patrycja Leszczenko, Ewa Sierka, Sára Emma Hamplová, Blanka Klepetářová, Radek Pelc, Valery Andrushchenko. Vibrational circular dichroism of adenosine crystals. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2024, 232 , 124381. https://doi.org/10.1016/j.saa.2024.124381
    7. Monika Krupová, Patrycja Leszczenko, Ewa Sierka, Sára Emma Hamplová, Radek Pelc, Valery Andrushchenko. Vibrational Circular Dichroism Unravels Supramolecular Chirality and Hydration Polymorphism of Nucleoside Crystals. Chemistry – A European Journal 2022, 28 (63) https://doi.org/10.1002/chem.202201922
    8. Dmitry Kurouski. Advances of Vibrational Circular Dichroism (VCD) in bioanalytical chemistry. A review. Analytica Chimica Acta 2017, 990 , 54-66. https://doi.org/10.1016/j.aca.2017.08.014
    9. Celia Duce, Valentina Della Porta, Emilia Bramanti, Beatrice Campanella, Alessio Spepi, Maria Rosaria Tiné. Loading of halloysite nanotubes with BSA, α -Lac and β -Lg: a Fourier transform infrared spectroscopic and thermogravimetric study. Nanotechnology 2017, 28 (5) , 055706. https://doi.org/10.1088/1361-6528/28/5/055706
    10. Weiming Bu, Luis M. Pereira, Roderic G. Eckenhoff, Koichi Yuki, . Stereoselectivity of Isoflurane in Adhesion Molecule Leukocyte Function-Associated Antigen-1. PLoS ONE 2014, 9 (5) , e96649. https://doi.org/10.1371/journal.pone.0096649
    11. Jin-Song He, Tai-Hua Mu, Xishan Guo, Songming Zhu, Norihiro Azuma, Choemon Kanno. Comparison of the gel-forming ability and gel properties of α-lactalbumin, lysozyme and myoglobin in the presence of β-lactoglobulin under high pressure. Food Hydrocolloids 2013, 33 (2) , 415-424. https://doi.org/10.1016/j.foodhyd.2013.04.010
    12. Karel D. Klika, Petri Tähtinen, Pekka Mäntsälä, Jarmo Niemi, Mikko Metsä-Ketelä. The potential of VCD to resolve the epimer vs. inverse epimer quandary. Computational and Theoretical Chemistry 2012, 992 , 156-163. https://doi.org/10.1016/j.comptc.2012.05.031
    13. Soo Ryeon Ryu, Bogusława Czarnik-Matusewicz, Rina K. Dukor, Laurence A. Nafie, Young Mee Jung. Analysis of the molten globule state of bovine α-lactalbumin by using vibrational circular dichroism. Vibrational Spectroscopy 2012, 60 , 68-72. https://doi.org/10.1016/j.vibspec.2012.02.006
    14. Timothy A. Keiderling, Ahmed Lakhani. Conformational Studies of Biopolymers, Peptides, Proteins, and Nucleic Acids. A Role for Vibrational Circular Dichroism. 2012, 707-758. https://doi.org/10.1002/9781118120392.ch22
    15. Marie Urbanová, Petr Maloň. Circular Dichroism Spectroscopy. 2012, 337-369. https://doi.org/10.1002/9783527644131.ch8
    16. Marie Urbanová. Bioinspired interactions studied by vibrational circular dichroism. Chirality 2009, 21 (1E) https://doi.org/10.1002/chir.20803
    17. Ganesh Shanmugam, Prasad L. Polavarapu. Structural transition during thermal denaturation of collagen in the solution and film states. Chirality 2009, 21 (1) , 152-159. https://doi.org/10.1002/chir.20598
    18. Jovencio Hilario, Jan Kubelka, Timothy Keiderling. Vibrational Circular Dichroism of Biopolymers. 2005, 253-324. https://doi.org/10.1201/9781420027549.ch6
    19. Klaus Brandenburg, Patrick Garidel, Andra B. Schromm, J�rg Andr�, Arjen Kramer, Maarten Egmond, Andre Wiese. Investigation into the interaction of the bacterial protease OmpT with outer membrane lipids and biological activity of OmpT:lipopolysaccharide complexes. European Biophysics Journal 2005, 34 (1) , 28-41. https://doi.org/10.1007/s00249-004-0422-3
    20. Ganesh Shanmugam, Prasad L. Polavarapu, D. Gopinath, R. Jayakumar. The structure of antimicrobial pexiganan peptide in solution probed by Fourier transform infrared absorption, vibrational circular dichroism, and electronic circular dichroism spectroscopy. Peptide Science 2005, 80 (5) , 636-642. https://doi.org/10.1002/bip.20132
    21. RyangGug Kim, Cha-Yong Choi. Minimally complex problem set for anAb Initio protein structure prediction study. Biotechnology and Bioprocess Engineering 2004, 9 (5) , 414-418. https://doi.org/10.1007/BF02933067
    22. Ganesh Shanmugam, Prasad L. Polavarapu. Vibrational circular dichroism spectra of protein films: thermal denaturation of bovine serum albumin. Biophysical Chemistry 2004, 111 (1) , 73-77. https://doi.org/10.1016/j.bpc.2004.04.005
    23. Ganesh Shanmugam, Prasad L. Polavarapu. Vibrational Circular Dichroism of Protein Films. Journal of the American Chemical Society 2004, 126 (33) , 10292-10295. https://doi.org/10.1021/ja048343a
    24. Qi Xu, Timothy A. Keiderling. Optical spectroscopic differentiation of various equilibrium denatured states of horse cytochrome c. Biopolymers 2004, 73 (6) , 716-726. https://doi.org/10.1002/bip.20011
    25. Timothy A. Keiderling, Qi Xu. Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra. 2002, 111-161. https://doi.org/10.1016/S0065-3233(02)62007-8
    26. Marie Urbanov�, Vladim�r Setni?ka, Vladim�r Kr�l, Karel Volka. Noncovalent interactions of peptides with porphyrins in aqueous solution: Conformational study using vibrational CD spectroscopy. Biopolymers 2001, 60 (4) , 307-316. https://doi.org/10.1002/1097-0282(2001)60:4<307::AID-BIP9992>3.0.CO;2-1
    27. Jonas Johansson, Roderic Eckenhoff. Experimental Approaches to the Study of Volatile Anesthetic-ProteinInteractions. 2000, 37-68. https://doi.org/10.1201/9781420036800.ch2
    28. Stefka G. Taneva, Anthony A. Donchev, Mitko I. Dimitrov, Arturo Muga. Redox- and pH-dependent association of plastocyanin with lipid bilayers: effect on protein conformation and thermal stability. Biochimica et Biophysica Acta (BBA) - Biomembranes 2000, 1463 (2) , 429-438. https://doi.org/10.1016/S0005-2736(99)00230-8
    29. Marie Urbanov�, Vladim�r Setni?ka, Karel Volka. Measurements of concentration dependence and enantiomeric purity of terpene solutions as a test of a new commercial VCD spectrometer. Chirality 2000, 12 (4) , 199-203. https://doi.org/10.1002/(SICI)1520-636X(2000)12:4<199::AID-CHIR6>3.0.CO;2-L
    30. Yuan Fang, Douglas G. Dalgleish. The conformation of α-lactalbumin as a function of pH, heat treatment and adsorption at hydrophobic surfaces studied by FTIR. Food Hydrocolloids 1998, 12 (2) , 121-126. https://doi.org/10.1016/S0268-005X(98)00003-4
    31. . Chapter 14 Applications and molecular structure. 1998, 321-382. https://doi.org/10.1016/S0167-6881(98)80050-5
    32. Sonia Longhi, Anne Nicolas, Lucia Creveld, Maarten Egmond, C. Theo Verrips, Jakob de Vlieg, Chrislaine Martinez, Christian Cambillau. Dynamics ofFusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Proteins: Structure, Function, and Genetics 1996, 26 (4) , 442-458. https://doi.org/10.1002/(SICI)1097-0134(199612)26:4<442::AID-PROT5>3.0.CO;2-D
    33. Marie Urbanová, Timothy A. Keiderling, Petr Pančoška. Conformational study of some milk proteins. Comparison of the results of electronic circular dichroism and vibrational circular dichroism. Bioelectrochemistry and Bioenergetics 1996, 41 (1) , 77-80. https://doi.org/10.1016/0302-4598(96)01932-0
    34. Sonia Bañuelos, Arturo Muga. Interaction of native and partially folded conformations of α‐lactalbumin with lipid bilayers: characterization of two membrane‐bound states. FEBS Letters 1996, 386 (1) , 21-25. https://doi.org/10.1016/0014-5793(96)00406-1
    35. Ping Xie, Max Diem. Measurement of Dispersive Vibrational Circular Dichroism: Signal Optimization and Artifact Reduction. Applied Spectroscopy 1996, 50 (5) , 675-680. https://doi.org/10.1366/0003702963905925
    36. Laurence D. Barron, Lutz Hecht, Alasdair F. Bell. Vibrational Raman Optical Activity of Biomolecules. 1996, 653-695. https://doi.org/10.1007/978-1-4757-2508-7_19
    37. Timothy A. Keiderling. Vibrational Circular Dichroism. 1996, 555-598. https://doi.org/10.1007/978-1-4757-2508-7_16
    38. Sonia Bañuelos, Arturo Muga. Binding of Molten Globule-like Conformations to Lipid Bilayers. Journal of Biological Chemistry 1995, 270 (50) , 29910-29915. https://doi.org/10.1074/jbc.270.50.29910
    39. Alfonso Valencia, Tim J. Hubbard, Arturo Muga, Sonia Bañuelos, Oscar Llorca, José L. Carrascosa, José Marí Valpuesta. Prediction of the structure of GroES and its interaction with GroEL. Proteins: Structure, Function, and Bioinformatics 1995, 22 (3) , 199-209. https://doi.org/10.1002/prot.340220302
    40. Michael Bloemendal, W. Curtis Johnson. Structural Information on Proteins from Circular Dichroism Spectroscopy Possibilities and Limitations. 1995, 65-100. https://doi.org/10.1007/978-1-4899-1079-0_2
    41. Robert W. Woody. [4] Circular dichroism. 1995, 34-71. https://doi.org/10.1016/0076-6879(95)46006-3
    42. Timothy A. Keiderling, Baoliang Wang, Marie Urbanova, Petr Pancoska, Rina K. Dukor. Empirical studies of protein secondary structure by vibrational circular dichroism and related techniques. α-Lactalbumin and lysozyme as examples. Faraday Discuss. 1994, 99 , 263-285. https://doi.org/10.1039/FD9949900263
    43. Jose Luis R. Arrondo, Arturo Muga, Jose Castresana, Felix M. Goñi. Quantitative studies of the structure of proteins in solution by fourier-transform infrared spectroscopy. Progress in Biophysics and Molecular Biology 1993, 59 (1) , 23-56. https://doi.org/10.1016/0079-6107(93)90006-6
    44. Andrei T. ALEXANDRESCU, R. William BROADHURST, Claire WORMALD, Chia‐Lin CHYAN, Jean BAUM, Christopher M. DOBSON. 1 H‐NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of α‐lactalbumin. European Journal of Biochemistry 1992, 210 (3) , 699-709. https://doi.org/10.1111/j.1432-1033.1992.tb17471.x
    45. Vijai P. Gupta, Timothy A. Keiderling. Vibrational CD of the amide II band in some model polypeptides and proteins. Biopolymers 1992, 32 (3) , 239-248. https://doi.org/10.1002/bip.360320305

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect