A Limiting Speed for Protein Folding at Low Solvent Viscosity

Because protein folding dynamics are heavily overdamped, Kramers theory predicts the rate of folding to scale inversely with the reaction friction, which is usually interpreted to mean the solvent viscosity. This does not mean, however, that the speed of folding can increase without limit as solvent...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2004-03, Vol.126 (11), p.3398-3399
Main Authors: Qiu, Linlin, Hagen, Stephen J
Format: Article
Language:English
Subjects:
Biological and medical sciences
Conformational dynamics in molecular biology
Fundamental and applied biological sciences. Psychology
Glucose - chemistry
Kinetics
Molecular biophysics
Peptides - chemistry
Protein Folding
Protein Structure, Secondary
Recombinant Proteins - chemistry
Solvents - chemistry
Thermodynamics
Viscosity
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Summary:Because protein folding dynamics are heavily overdamped, Kramers theory predicts the rate of folding to scale inversely with the reaction friction, which is usually interpreted to mean the solvent viscosity. This does not mean, however, that the speed of folding can increase without limit as solvent viscosity decreases. We show that, in a sufficiently fast-folding protein, the folding speed approaches a finite limit at low solvent viscosity, indicating a reaction controlled by internal friction.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja049966r