By observing trends in the folding kinetics of experimental 2-state proteins
at their transition midpoints, and by observing trends in the barrier heights
of numerous simulations of coarse grained, C-alpha model, Go proteins, we show
that folding rates correlate with the degree of heterogeneity in the formation
of native contacts. Statistically significant correlations are observed between
folding rates and measures of heterogeneity inherent in the native topology, as
well as between rates and the variance in the distribution of either
experimentally measured or simulated phi-values.Comment: 11 pages, 3 figures, 1 tabl

A. R. Fersht

B. Öztop

D. B. Wetlaufer

J. D. Bryngelson

J. N. Onuchic

M. Lindberg

M. R. Ejtehadi

R. R. Matheson

S. S. Plotkin

V. I. Abkevich

English

arXiv

The folding rates of protein were shown to correlate with the degree of heterogeneity in the formation of native contacts. It was shown that both experimental rates and simulated free energy barriers for 2-state proteins depend on the degree of heterogeneity present in the folding process. Heterogeneity due to variance in the distribution of native loop lengths, and variance in the distribution of φ values, were observed to increase folding rates and reduce folding barriers. The observed effect due to φ variance was found to be the most statistically significant, because φ variance captures both heterogeneity arising from native topology and that arising from energetics

Protein folding rates correlate with heterogeneity of folding mechanism

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