Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR

Click to copy article linkArticle link copied!

This article is cited by 249 publications.

1. Nathaniel E. Larm, Christopher D. Stachurski, Paul C. Trulove, Xiaonan Tang, Yun Shen, David P. Durkin, Gary A. Baker. Role of Heavy Water in the Synthesis and Nanocatalytic Activity of Gold Nanoparticles. ACS Nanoscience Au 2025, Article ASAP.
2. Radha P. Somarathne, Sandeep K. Misra, Chathuri S. Kariyawasam, Jacques J. Kessl, Joshua S. Sharp, Nicholas C. Fitzkee. Exploring Residue-Level Interactions between the Biofilm-Driving R2ab Protein and Polystyrene Nanoparticles. Langmuir 2024, 40 (2) , 1213-1222. https://doi.org/10.1021/acs.langmuir.3c02609
3. Juan F. Araneda, Thaís Mendonça Barbosa, Paul Hui, Matthew C. Leclerc, Jonathan Ma, Alexander F. G. Maier, Susanne D. Riegel. Incorporating Benchtop NMR Spectrometers in the Undergraduate Lab: Understanding Resolution and Circumventing Second-Order Effects. Journal of Chemical Education 2021, 98 (4) , 1227-1232. https://doi.org/10.1021/acs.jchemed.0c01182
4. Travis A. Danielson, Jessica M. Stine, Tanveer A. Dar, Klara Briknarova, and Bruce E. Bowler . Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c. Biochemistry 2017, 56 (51) , 6662-6676. https://doi.org/10.1021/acs.biochem.7b01002
5. Damián Alvarez-Paggi, Luciana Hannibal, María A. Castro, Santiago Oviedo-Rouco, Veronica Demicheli, Veronica Tórtora, Florencia Tomasina, Rafael Radi, and Daniel H. Murgida . Multifunctional Cytochrome c: Learning New Tricks from an Old Dog. Chemical Reviews 2017, 117 (21) , 13382-13460. https://doi.org/10.1021/acs.chemrev.7b00257
6. Wayne Yu, Phillip E. Dawson, Jörg Zimmermann, and Floyd E. Romesberg . Carbon–Deuterium Bonds as Probes of Protein Thermal Unfolding. The Journal of Physical Chemistry B 2012, 116 (22) , 6397-6403. https://doi.org/10.1021/jp303521t
7. Shigeyoshi Nakamura and Shun-ichi Kidokoro . Volumetric Properties of the Molten Globule State of Cytochrome c in the Thermal Three-State Transition Evaluated by Pressure Perturbation Calorimetry. The Journal of Physical Chemistry B 2012, 116 (6) , 1927-1932. https://doi.org/10.1021/jp209686e
8. Samuel I. Merenbloom, Tawnya G. Flick, Michael P. Daly, Evan R. Williams. Effects of Select Anions from the Hofmeister Series on the Gas-Phase Conformations of Protein Ions Measured with Traveling-Wave Ion Mobility Spectrometry/Mass Spectrometry. Journal of the American Society for Mass Spectrometry 2011, 22 (11) https://doi.org/10.1007/s13361-011-0238-1
9. Jean K. Chung, Megan C. Thielges, Sarah E. J. Bowman, Kara L. Bren, and M. D. Fayer . Temperature Dependent Equilibrium Native to Unfolded Protein Dynamics and Properties Observed with IR Absorption and 2D IR Vibrational Echo Experiments. Journal of the American Chemical Society 2011, 133 (17) , 6681-6691. https://doi.org/10.1021/ja111009s
10. Shigeyoshi Nakamura, Yasutaka Seki, Etsuko Katoh, and Shun-ichi Kidokoro . Thermodynamic and Structural Properties of the Acid Molten Globule State of Horse Cytochrome c. Biochemistry 2011, 50 (15) , 3116-3126. https://doi.org/10.1021/bi101806b
11. Abani K. Bhuyan. Off-Pathway Status for the Alkali Molten Globule of Horse Ferricytochrome c. Biochemistry 2010, 49 (36) , 7764-7773. https://doi.org/10.1021/bi100880d
12. Kenneth J. Barns, Sanela Lampa-Pastirk, Kevin L. Dillman and Warren F. Beck. Intramolecular Vibrational Excitation of Unfolding Reactions in ZnII-Substituted and Metal-Free Cytochromes c: Activation Enthalpies from Integrated Fluorescence Stokes Shift and Line Shape Excitation Profiles. The Journal of Physical Chemistry B 2008, 112 (47) , 15108-15115. https://doi.org/10.1021/jp803756n
13. Ravindra Singh Prajapati,, S. Indu, and, Raghavan Varadarajan. Identification and Thermodynamic Characterization of Molten Globule States of Periplasmic Binding Proteins. Biochemistry 2007, 46 (36) , 10339-10352. https://doi.org/10.1021/bi700577m
14. Beenu Moza,, Shabir Hussain Qureshi,, Asimul Islam,, Rajendrakumar Singh,, Farah Anjum,, Ali Akbar Moosavi-Movahedi, and, Faizan Ahmad. A Unique Molten Globule State Occurs during Unfolding of Cytochrome c by LiClO4 Near Physiological pH and Temperature: Structural and Thermodynamic Characterization. Biochemistry 2006, 45 (14) , 4695-4702. https://doi.org/10.1021/bi052357r
15. D. Krishna Rao,, Rajesh Kumar,, M. Yadaiah, and, Abani K. Bhuyan. The Alkali Molten Globule State of Ferrocytochrome c:  Extraordinary Stability, Persistent Structure, and Constrained Overall Dynamics. Biochemistry 2006, 45 (10) , 3412-3420. https://doi.org/10.1021/bi051882n
16. Ekaterina V. Pletneva,, Harry B. Gray, and, Jay R. Winkler. Nature of the Cytochrome c Molten Globule. Journal of the American Chemical Society 2005, 127 (44) , 15370-15371. https://doi.org/10.1021/ja0555318
17. Heinz-Bernhard Kraatz,, Irene Bediako-Amoa,, Samuel H. Gyepi-Garbrah, and, Todd C. Sutherland. Electron Transfer through H-bonded Peptide Assemblies. The Journal of Physical Chemistry B 2004, 108 (52) , 20164-20172. https://doi.org/10.1021/jp047900c
18. H. Jane Dyson and, Peter E. Wright. Unfolded Proteins and Protein Folding Studied by NMR. Chemical Reviews 2004, 104 (8) , 3607-3622. https://doi.org/10.1021/cr030403s
19. Irina M. Kuznetsova,, Konstantin K. Turoverov, and, Vladimir N. Uversky. Use of the Phase Diagram Method to Analyze the Protein Unfolding-Refolding Reactions:  Fishing Out the “Invisible” Intermediates. Journal of Proteome Research 2004, 3 (3) , 485-494. https://doi.org/10.1021/pr034094y
20. Daniel King,, Carl Bergmann,, Ron Orlando,, Jacques A. E. Benen,, Harry C. M. Kester, and, Jaap Visser. Use of Amide Exchange Mass Spectrometry To Study Conformational Changes within the Endopolygalacturonase II−Homogalacturonan−Polygalacturonase Inhibiting Protein System. Biochemistry 2002, 41 (32) , 10225-10233. https://doi.org/10.1021/bi020119f
21. Scott M. Tremain and, Nenad M. Kostić. Molten-Globule and Other Conformational Forms of Zinc Cytochrome c. Effect of Partial and Complete Unfolding of the Protein on Its Electron-Transfer Reactivity. Inorganic Chemistry 2002, 41 (12) , 3291-3301. https://doi.org/10.1021/ic010893b
22. Silke Oellerich,, Hainer Wackerbarth, and, Peter Hildebrandt. Spectroscopic Characterization of Nonnative Conformational States of Cytochrome c. The Journal of Physical Chemistry B 2002, 106 (25) , 6566-6580. https://doi.org/10.1021/jp013841g
23. Stephen J. Valentine, David E. Clemmer. Temperature-dependent H/D exchange of compact and elongated cytochrome c ions in the gas phase. Journal of the American Society for Mass Spectrometry 2002, 13 (5) , 506-517. https://doi.org/10.1016/S1044-0305(02)00372-0
24. Adam R. Mezo and, John C. Sherman. Cavitands Are Effective Templates for Inducing Stability and Nativelike Structure in de Novo Four-Helix Bundles. Journal of the American Chemical Society 1999, 121 (39) , 8983-8994. https://doi.org/10.1021/ja990487f
25. M. C. Ramachandra Shastry,, J. Michael Sauder, and, Heinrich Roder. Kinetic and Structural Analysis of Submillisecond Folding Events in Cytochrome c. Accounts of Chemical Research 1998, 31 (11) , 717-725. https://doi.org/10.1021/ar970086+
26. Sushmita Roy,, Gayathri Ratnaswamy,, Judith A. Boice,, Robert Fairman,, George McLendon, and, Michael H. Hecht. A Protein Designed by Binary Patterning of Polar and Nonpolar Amino Acids Displays Native-like Properties. Journal of the American Chemical Society 1997, 119 (23) , 5302-5306. https://doi.org/10.1021/ja9700717
27. Stephen J. Valentine and, David E. Clemmer. H/D Exchange Levels of Shape-Resolved Cytochrome c Conformers in the Gas Phase. Journal of the American Chemical Society 1997, 119 (15) , 3558-3566. https://doi.org/10.1021/ja9626751
28. Yaoqing Liu, David L. Smith. Probing high order structure of proteins by fast-atom bombardment mass spectrometry. Journal of the American Society for Mass Spectrometry 1994, 5 (1) , 19-28. https://doi.org/10.1016/1044-0305(94)85080-1
29. Marina Warepam, Potshangbam Nongdam, Hamidur Rahaman. Osmolyte-Mediated Protein Stabilization: Unraveling Interactions Across Conformational Landscapes. 2024, 55-72. https://doi.org/10.1007/978-981-97-6001-5_4
30. Valentina E. Bychkova, Dmitry A. Dolgikh, Vitalii A. Balobanov, Alexei V. Finkelstein. Formation of the Native Topology of a Protein is due to the “Conserved but Non-Functional” Residues: A Case of Apomyoglobin Folding. Frontiers in Bioscience-Landmark 2024, 29 (11) https://doi.org/10.31083/j.fbl2911379
31. Munishwar Nath Gupta, Vladimir N. Uversky. Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins. International Journal of Molecular Sciences 2023, 24 (3) , 2424. https://doi.org/10.3390/ijms24032424
32. Yoshiki Yamaguchi, Takumi Yamaguchi, Koichi Kato. Structural Analysis of Oligosaccharides and Glycoconjugates Using NMR. 2023, 163-184. https://doi.org/10.1007/978-3-031-12390-0_6
33. Vladimir N. Uversky. Molten globular enzymes. 2023, 303-325. https://doi.org/10.1016/B978-0-323-99533-7.00010-8
34. Andrej Hovan, Dagmar Sedláková, Martin Berta, Gregor Bánó, Erik Sedlák. Singlet oxygen quenching as a probe for cytochrome c molten globule state formation. Physical Chemistry Chemical Physics 2022, 24 (21) , 13317-13324. https://doi.org/10.1039/D2CP01281B
35. Kunihiro Kuwajima, Maho Yagi-Utsumi, Saeko Yanaka, Koichi Kato. DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science. Molecules 2022, 27 (12) , 3748. https://doi.org/10.3390/molecules27123748
36. Zahoor Ahmad Parray, Mohammad Shahid, Asimul Islam. Insights into Fluctuations of Structure of Proteins: Significance of Intermediary States in Regulating Biological Functions. Polymers 2022, 14 (8) , 1539. https://doi.org/10.3390/polym14081539
37. Vladimir Uversky, Alexei Finkelstein. Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions. Biomolecules 2019, 9 (12) , 842. https://doi.org/10.3390/biom9120842
38. Ali Es-haghi, Mahsa Jahedi Moghaddam, Koorosh Shahpasand. Role of Pre-molten Globule Structure in Protein Amyloid Fibril Formation. Avicenna Journal of Medical Biochemistry 2019, 7 (1) , 35-42. https://doi.org/10.34172/ajmb.2019.07
39. Michelle Redhair, Amanda F. Clouser, William M. Atkins. Hydrogen-deuterium exchange mass spectrometry of membrane proteins in lipid nanodiscs. Chemistry and Physics of Lipids 2019, 220 , 14-22. https://doi.org/10.1016/j.chemphyslip.2019.02.007
40. Chi Wang, Andrei A. Aleksandrov, Zhengrong Yang, Farhad Forouhar, Elizabeth A. Proctor, Pradeep Kota, Jianli An, Anna Kaplan, Netaly Khazanov, Grégory Boël, Brent R. Stockwell, Hanoch Senderowitz, Nikolay V. Dokholyan, John R. Riordan, Christie G. Brouillette, John F. Hunt. Ligand binding to a remote site thermodynamically corrects the F508del mutation in the human cystic fibrosis transmembrane conductance regulator. Journal of Biological Chemistry 2018, 293 (46) , 17685-17704. https://doi.org/10.1074/jbc.RA117.000819
41. Niki S. Jha, Eva Judy, Nand Kishore. 1,1,1,3,3,3-Hexafluoroisopropanol and 2,2,2-trifluoroethanol act more effectively on protein in combination than individually: Thermodynamic aspects. The Journal of Chemical Thermodynamics 2018, 121 , 39-48. https://doi.org/10.1016/j.jct.2018.02.011
42. Francesca Caporaletti, Marina Carbonaro, Paola Maselli, Alessandro Nucara. Hydrogen–Deuterium exchange kinetics in β-lactoglobulin (−)-epicatechin complexes studied by FTIR spectroscopy. International Journal of Biological Macromolecules 2017, 104 , 521-526. https://doi.org/10.1016/j.ijbiomac.2017.06.028
43. Mengjun Xue, Ryo Kitahara, Yuichi Yoshimura, Frans A.A. Mulder. Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation. Biochemical and Biophysical Research Communications 2016, 478 (3) , 1185-1188. https://doi.org/10.1016/j.bbrc.2016.08.092
44. Abdullah Naiyer, Md. Imtaiyaz Hassan, Asimul Islam, Monica Sundd, Faizan Ahmad. Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques. Journal of Biomolecular Structure and Dynamics 2015, 33 (10) , 2267-2284. https://doi.org/10.1080/07391102.2014.999354
45. Ryo P. Honda, Ming Xu, Kei-ichi Yamaguchi, Heinrich Roder, Kazuo Kuwata. A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein. Structure 2015, 23 (9) , 1735-1742. https://doi.org/10.1016/j.str.2015.07.001
46. Hamidur Rahaman, Md. Khurshid Alam Khan, Md. Imtaiyaz Hassan, Asimul Islam, Ali Akbar Moosavi-Movahedi, Faizan Ahmad, . Heterogeneity of Equilibrium Molten Globule State of Cytochrome c Induced by Weak Salt Denaturants under Physiological Condition. PLOS ONE 2015, 10 (4) , e0120465. https://doi.org/10.1371/journal.pone.0120465
47. Md. Anzarul Haque, Shah Ubaid-ullah, Sobia Zaidi, Md. Imtaiyaz Hassan, Asimul Islam, Janendra K. Batra, Faizan Ahmad. Characterization of pre-molten globule state of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 °C. International Journal of Biological Macromolecules 2015, 72 , 1406-1418. https://doi.org/10.1016/j.ijbiomac.2014.10.053
48. Ryo P. Honda, Kei-ichi Yamaguchi, Kazuo Kuwata. Acid-induced Molten Globule State of a Prion Protein. Journal of Biological Chemistry 2014, 289 (44) , 30355-30363. https://doi.org/10.1074/jbc.M114.559450
49. NA LI, FAMING GAO, LI HOU. SYNTHESIS OF PLATINUM CLUSTERS ON CYTOCHROME c TEMPLATES: CONDITIONS FOR A TEMPLATE-CONTROLLED CLUSTER GROWTH. Nano 2014, 09 (07) , 1450080. https://doi.org/10.1142/S1793292014500805
50. Reinhard Schweitzer-Stenner. Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility. New Journal of Science 2014, 2014 , 1-28. https://doi.org/10.1155/2014/484538
51. Yoshiki Yamaguchi, Takumi Yamaguchi, Koichi Kato. Structural Analysis of Oligosaccharides and Glycoconjugates Using NMR. 2014, 165-183. https://doi.org/10.1007/978-1-4939-1154-7_8
52. Vladimir N. Uversky. Under‐folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis. Biopolymers 2013, 99 (11) , 870-887. https://doi.org/10.1002/bip.22298
53. Mia C. Brown, Andrew C. Mutter, Ronald L. Koder, Renee D. JiJi, Jason W. Cooley. Observation of persistent α‐helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep‐UV resonance Raman spectroscopy. Journal of Raman Spectroscopy 2013, 44 (7) , 957-962. https://doi.org/10.1002/jrs.4316
54. Unnati Ahluwalia, Shashank Deep. Interaction of ATP with acid-denatured cytochrome c via coupled folding-binding mechanism. The Journal of Chemical Thermodynamics 2012, 52 , 69-77. https://doi.org/10.1016/j.jct.2012.03.006
55. Paolo Neyroz, Stefano Ciurli, Vladimir N. Uversky. Denaturant-Induced Conformational Transitions in Intrinsically Disordered Proteins. 2012, 197-213. https://doi.org/10.1007/978-1-4614-3704-8_12
56. V.N. Uversky, A.K. Dunker. 3.9 Intrinsically Disordered Proteins. 2012, 170-211. https://doi.org/10.1016/B978-0-12-374920-8.00312-X
57. Ramil F. Latypov, Sabine Hogan, Hollis Lau, Himanshu Gadgil, Dingjiang Liu. Elucidation of Acid-induced Unfolding and Aggregation of Human Immunoglobulin IgG1 and IgG2 Fc. Journal of Biological Chemistry 2012, 287 (2) , 1381-1396. https://doi.org/10.1074/jbc.M111.297697
58. Unnati Ahluwalia, Chetan Prakash, Rakhi Agrawal, Shashank Deep. Characterization of cytochrome c folding intermediates induced by sucrose and phosphate. International Journal of Biological Macromolecules 2011, 49 (4) , 752-760. https://doi.org/10.1016/j.ijbiomac.2011.07.010
59. Unnati Ahluwalia, Shahid M. Nayeem, Shashank Deep. The non-native conformations of cytochrome c in sodium dodecyl sulfate and their modulation by ATP. European Biophysics Journal 2011, 40 (3) , 259-271. https://doi.org/10.1007/s00249-010-0643-6
60. Md. Khurshid Alam Khan, Hamidur Rahaman, Faizan Ahmad. Conformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c. Metallomics 2011, 3 (4) , 327. https://doi.org/10.1039/c0mt00078g
61. Md. Khurshid Alam Khan, Md. Hamidur Rahaman, Md. Imtaiyaz Hassan, Tej P. Singh, Ali A. Moosavi-Movahedi, Faizan Ahmad. Conformational and thermodynamic characterization of the premolten globule state occurring during unfolding of the molten globule state of cytochrome c. JBIC Journal of Biological Inorganic Chemistry 2010, 15 (8) , 1319-1329. https://doi.org/10.1007/s00775-010-0691-5
62. Vladimir N. Uversky, A. Keith Dunker. Understanding protein non-folding. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2010, 1804 (6) , 1231-1264. https://doi.org/10.1016/j.bbapap.2010.01.017
63. Heidi E.K. Huttunen-Hennelly. An investigation into the N- and C-capping effects of glycine in cavitand-based four-helix bundle proteins. Bioorganic Chemistry 2010, 38 (3) , 98-107. https://doi.org/10.1016/j.bioorg.2010.01.004
64. Vladimir N. Uversky. Conformational Behavior of Intrinsically Disordered Proteins: Effects of Strong Denaturants, Temperature, PH, Counterions, and Macromolecular Crowding. 2010, 545-568. https://doi.org/10.1002/9780470602614.ch19
65. Christopher R. Morgan, John R. Engen. Investigating Solution‐Phase Protein Structure and Dynamics by Hydrogen Exchange Mass Spectrometry. Current Protocols in Protein Science 2009, 58 (1) https://doi.org/10.1002/0471140864.ps1706s58
66. Vladimir N. Uversky. Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding. The Protein Journal 2009, 28 (7-8) , 305-325. https://doi.org/10.1007/s10930-009-9201-4
67. Megan C. Thielges, Jörg Zimmermann, Philip E. Dawson, Floyd E. Romesberg. The Determinants of Stability and Folding in Evolutionarily Diverged Cytochromes c. Journal of Molecular Biology 2009, 388 (1) , 159-167. https://doi.org/10.1016/j.jmb.2009.02.059
68. Daniela Deriu, Sara Emanuela Pagnotta, Roberto Santucci, Nicola Rosato. Spectroscopic and electrochemical characterization of cytochrome c encapsulated in a bio sol–gel matrix. BioMetals 2008, 21 (4) , 417-423. https://doi.org/10.1007/s10534-007-9130-7
69. Heidi E. K. Huttunen‐Hennelly, John C. Sherman. An investigation into the native‐like properties of de novo designed cavitand‐based four‐helix bundle proteins. Peptide Science 2008, 90 (1) , 37-50. https://doi.org/10.1002/bip.20883
70. S. Walter Englander, Leland Mayne, Mallela M. G. Krishna. Protein folding and misfolding: mechanism and principles. Quarterly Reviews of Biophysics 2007, 40 (4) , 1-41. https://doi.org/10.1017/S0033583508004654
71. Christopher M. Dobson. NMR Spectroscopy and Protein Folding: Studies of Lysozyme and α‐Lactalbumin. 2007, 167-189. https://doi.org/10.1002/9780470514146.ch11
72. Robert L. Baldwin. Experimental Studies of Pathways of Protein Folding. 2007, 190-205. https://doi.org/10.1002/9780470514146.ch12
73. Stéphane Duquerroy, Jacqueline Cherfils, Joël Janin. Protein‐Protein Interaction: An Analysis by Computer Simulation. 2007, 237-259. https://doi.org/10.1002/9780470514146.ch15
74. Jie-rong Huang, Timothy D. Craggs, John Christodoulou, Sophie E. Jackson. Stable Intermediate States and High Energy Barriers in the Unfolding of GFP. Journal of Molecular Biology 2007, 370 (2) , 356-371. https://doi.org/10.1016/j.jmb.2007.04.039
75. Emily S. Seo, Walter R. P. Scott, Suzana K. Straus, John C. Sherman. Optimal Attachment Position and Linker Length Promote Native‐like Character of Cavitand‐Based Template‐Assembled Synthetic Proteins (TASPs). Chemistry – A European Journal 2007, 13 (13) , 3596-3605. https://doi.org/10.1002/chem.200601784
76. Shigeyoshi Nakamura, Takayuki Baba, Shun-ichi Kidokoro. A molten globule-like intermediate state detected in the thermal transition of cytochrome c under low salt concentration. Biophysical Chemistry 2007, 127 (1-2) , 103-112. https://doi.org/10.1016/j.bpc.2007.01.002
77. A. Joshua Wand. Mitochondrial Cytochrome c. 2007https://doi.org/10.1002/9780470034590.emrstm0313
78. H. Jane Dyson, Peter E. Wright. Proteins and Protein Fragments: Folding. 2007https://doi.org/10.1002/9780470034590.emrstm0424
79. Heidi E. K. Huttunen-Hennelly, John C. Sherman. The design, synthesis, and characterization of the first cavitand-based de novo hetero-template-assembled synthetic proteins (Hetero-TASPs). Organic & Biomolecular Chemistry 2007, 5 (22) , 3637. https://doi.org/10.1039/b711869d
80. Veerappan Anbazhagan, Pamanji Sudhakar Reddy, Chin Yu. CARDIOTOXIN FROM TAIWAN COBRA ( NAJA NAJA ATRA ): STRUCTURE, DYNAMICS, INTERACTION AND PROTEIN FOLDING. Toxin Reviews 2007, 26 (2) , 203-229. https://doi.org/10.1080/15569540701209831
81. Emily S. Seo, John C. Sherman. Analysis of peptide design in four‐, five‐, and six‐helix bundle template assembled synthetic protein molecules. Peptide Science 2007, 88 (5) , 774-779. https://doi.org/10.1002/bip.20791
82. Jon O. Freeman, Diana Wallhorn, John C. Sherman. Four‐helix bundle cavitein reveals middle leucine as linchpin. Peptide Science 2007, 88 (5) , 725-732. https://doi.org/10.1002/bip.20718
83. Federica Sinibaldi, Maria C. Piro, Massimo Coletta, Roberto Santucci. Salt‐induced formation of the A‐state of ferricytochrome  c  – effect of the anion charge on protein structure. The FEBS Journal 2006, 273 (23) , 5347-5357. https://doi.org/10.1111/j.1742-4658.2006.05527.x
84. Rajesh Kumar, N. Prakash Prabhu, D. Krishna Rao, Abani K. Bhuyan. The Alkali Molten Globule State of Horse Ferricytochrome c: Observation of Cold Denaturation. Journal of Molecular Biology 2006, 364 (3) , 483-495. https://doi.org/10.1016/j.jmb.2006.09.025
85. Aabgeena Naeem, Mohd. Tashfeen Ashraf, Mohd. Akram, Rizwan Hasan Khan. Comparative study of effects of polyols, salts, and alcohols on trichloroacetic acid-induced state of cytochrome c. Biochemistry (Moscow) 2006, 71 (10) , 1101-1109. https://doi.org/10.1134/S0006297906100075
86. Francisco J.R. Sousa, Luis M.T.R. Lima, Ana B.F. Pacheco, Cristiano L.P. Oliveira, Iris Torriani, Darcy F. Almeida, Debora Foguel, Jerson L. Silva, Ronaldo Mohana-Borges. Tetramerization of the LexA Repressor in Solution: Implications for Gene Regulation of the E.coli SOS System at Acidic pH. Journal of Molecular Biology 2006, 359 (4) , 1059-1074. https://doi.org/10.1016/j.jmb.2006.03.069
87. J. Chamani, A.A. Moosavi-Movahedi. Effect of n-alkyl trimethylammonium bromides on folding and stability of alkaline and acid-denatured cytochrome c: A spectroscopic approach. Journal of Colloid and Interface Science 2006, 297 (2) , 561-569. https://doi.org/10.1016/j.jcis.2005.11.035
88. Ramil F. Latypov, Hong Cheng, Navid A. Roder, Jiaru Zhang, Heinrich Roder. Structural Characterization of an Equilibrium Unfolding Intermediate in Cytochrome c. Journal of Molecular Biology 2006, 357 (3) , 1009-1025. https://doi.org/10.1016/j.jmb.2006.01.055
89. Véronique Receveur‐Bréchot, Jean‐Marie Bourhis, Vladimir N. Uversky, Bruno Canard, Sonia Longhi. Assessing protein disorder and induced folding. Proteins: Structure, Function, and Bioinformatics 2006, 62 (1) , 24-45. https://doi.org/10.1002/prot.20750
90. Shao‐Wei Huang, Jenn‐Kang Hwang. Computation of conformational entropy from protein sequences using the machine‐learning method—Application to the study of the relationship between structural conservation and local structural stability. Proteins: Structure, Function, and Bioinformatics 2005, 59 (4) , 802-809. https://doi.org/10.1002/prot.20462
91. Aichun Dong, Troy Lam. Equilibrium titrations of acid-induced unfolding–refolding and salt-induced molten globule of cytochrome c by FT-IR spectroscopy. Archives of Biochemistry and Biophysics 2005, 436 (1) , 154-160. https://doi.org/10.1016/j.abb.2005.01.006
92. Shigeyoshi Nakamura, Shun-ichi Kidokoro. Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry. Biophysical Chemistry 2005, 113 (2) , 161-168. https://doi.org/10.1016/j.bpc.2004.09.002
93. Robert L. Baldwin. Early Days of Studying the Mechanism of Protein Folding. 2005, 1-21. https://doi.org/10.1002/9783527619498.ch1
94. Kosuke Maki, Kiyoto Kamagata, Kunihiro Kuwajima. Equilibrium and Kinetically Observed Molten Globule States. 2005, 856-883. https://doi.org/10.1002/9783527619498.ch23
95. Claudia S. Maier, Max L. Deinzer. Protein Conformations, Interactions, and H/D Exchange. 2005, 312-360. https://doi.org/10.1016/S0076-6879(05)02010-0
96. Aabgeena Naeem, Rizwan Hasan Khan. Characterization of molten globule state of cytochrome c at alkaline, native and acidic pH induced by butanol and SDS. The International Journal of Biochemistry & Cell Biology 2004, 36 (11) , 2281-2292. https://doi.org/10.1016/j.biocel.2004.04.023
97. Qi Xu, Timothy A. Keiderling. Effect of sodium dodecyl sulfate on folding and thermal stability of acid‐denatured cytochrome c: A spectroscopic approach. Protein Science 2004, 13 (11) , 2949-2959. https://doi.org/10.1110/ps.04827604
98. 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
99. Aabgeena Naeem, Mohammad Akram, Rizwan Hasan Khan. Conformational States of Trifluoroacetic Acid–Treated Cytochrome c in the Presence of Salts and Alcohols. The Protein Journal 2004, 23 (3) , 185-195. https://doi.org/10.1023/B:JOPC.0000026414.34366.33
100. Agnita Kundu, Nand Kishore. 1,1,1,3,3,3‐hexafluoroisopropanol induced thermal unfolding and molten globule state of bovine α‐lactalbumin: Calorimetric and spectroscopic studies. Biopolymers 2004, 73 (4) , 405-420. https://doi.org/10.1002/bip.20014