Kinetics of protein folding: Nucleation mechanism, time scales, and pathways

Biopolymers ◽  
1995 ◽  
Vol 36 (1) ◽  
pp. 83-102 ◽  
Author(s):  
Zhuyan Guo ◽  
D. Thirumalai
Keyword(s):  
Protein Folding ◽  
Time Scales ◽  
Nucleation Mechanism ◽  
Kinetics Of

Preparation, optimization and evolution of the kinetic mechanism of an Fe-MIL-88A metal–organic framework

CrystEngComm ◽  
2019 ◽  
Vol 21 (3) ◽  
pp. 544-553 ◽  
Author(s):  
Elham Bagherzadeh ◽  
Seyed Mojtaba Zebarjad ◽  
Hamid Reza Madaah Hosseini ◽  
Pierre Chagnon
Keyword(s):  
Morphological Changes ◽  
Metal Organic Framework ◽  
Kinetic Mechanism ◽  
Nucleation Mechanism ◽  
Growth Behavior ◽  
Kinetics Of Crystallization ◽  
Metal Organic ◽  
Statistical Studies ◽  
Kinetics Of ◽  
Organic Framework

Investigating the kinetics of crystallization, growth behavior and morphological changes through statistical studies of Fe-MIL-88A suggested an autocatalytic nucleation mechanism.

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 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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