Statistical mechanics and kinetics of protein folding and aggregation

2021 ◽  
Author(s):  
John Stephen Schreck
Keyword(s):  
Protein Folding ◽  
Statistical Mechanics ◽  
Kinetics Of

scholarly journals Statistical Mechanics Model for Protein Folding

2009 ◽  
Author(s):  
Alexander Yakubovich ◽  
Andrey V. Solov’yov ◽  
Walter Greiner ◽  
Andrey Solov́yov ◽  
Eugene Surdutovich
Keyword(s):  
Protein Folding ◽  
Statistical Mechanics ◽  
Mechanics Model

scholarly journals Probing the Kinetics of Single Molecule Protein Folding

2004 ◽  
Vol 87 (6) ◽  
pp. 3633-3641 ◽  
Author(s):  
Vitor B.P. Leite ◽  
José N. Onuchic ◽  
George Stell ◽  
Jin Wang
Keyword(s):  
Protein Folding ◽  
Single Molecule ◽  
Kinetics Of

scholarly journals Statistical mechanics of simple models of protein folding and design

1997 ◽  
Vol 73 (6) ◽  
pp. 3192-3210 ◽  
Author(s):  
V.S. Pande ◽  
A.Y. Grosberg ◽  
T. Tanaka
Keyword(s):  
Protein Folding ◽  
Statistical Mechanics ◽  
Simple Models

scholarly journals Oxidative folding of hirudin in human serum

2006 ◽  
Vol 394 (1) ◽  
pp. 249-257 ◽  
Author(s):  
Jui-Yoa Chang ◽  
Bao-Yun Lu ◽  
Por-Hsiung Lai
Keyword(s):  
Amino Acids ◽  
Protein Folding ◽  
Human Serum ◽  
Initial Phase ◽  
Macromolecular Crowding ◽  
Specific Inhibitor ◽  
Crowding Effect ◽  
Oxidative Folding ◽  
Disulphide Bonds ◽  
Kinetics Of

Human serum contains factors that promote oxidative folding of disulphide proteins. We demonstrate this here using hirudin as a model. Hirudin is a leech-derived thrombin-specific inhibitor containing 65 amino acids and three disulphide bonds. Oxidative folding of hirudin in human serum is shown to involve an initial phase of rapid disulphide formation (oxidation) to form the scrambled isomers as intermediates. This is followed by the stage of slow disulphide shuffling of scrambled isomers to attain the native hirudin. The kinetics of regenerating the native hirudin depend on the concentrations of both hirudin and human serum. Quantitative regeneration of native hirudin in undiluted human serum can be completed within 48 h, without any redox supplement. These results cannot be adequately explained by the existing oxidized thiol agents in human serum or the macromolecular crowding effect, and therefore indicate that human serum may contain yet to be identified potent oxidase(s) for assisting protein folding.

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