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Measuring internal friction of an ultrafast-folding protein.

ABSTRACT: Nanosecond laser T-jump was used to measure the viscosity dependence of the folding kinetics of the villin subdomain under conditions where the viscogen has no effect on its equilibrium properties. The dependence of the unfolding/refolding relaxation time on solvent viscosity indicates a major contribution to the dynamics from internal friction. The internal friction increases with increasing temperature, suggesting a shift in the transition state along the reaction coordinate toward the native state with more compact structures, and therefore, a smaller diffusion coefficient due to increased landscape roughness. Fitting the data with an Ising-like model yields a relatively small position dependence for the diffusion coefficient. This finding is consistent with the excellent correlation found between experimental and calculated folding rates based on free energy barrier heights using the same diffusion coefficient for every protein.

SUBMITTER: Cellmer T

PROVIDER: S-EPMC2587570 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Measuring internal friction of an ultrafast-folding protein.

Cellmer Troy T Henry Eric R ER Hofrichter James J Eaton William A WA

Proceedings of the National Academy of Sciences of the United States of America 20081119 47

Nanosecond laser T-jump was used to measure the viscosity dependence of the folding kinetics of the villin subdomain under conditions where the viscogen has no effect on its equilibrium properties. The dependence of the unfolding/refolding relaxation time on solvent viscosity indicates a major contribution to the dynamics from internal friction. The internal friction increases with increasing temperature, suggesting a shift in the transition state along the reaction coordinate toward the native ...[more]

PMID: 19020085

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