Protein folding rates correlate with heterogeneity of folding mechanism.
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.
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Department of Physics and Astronomy, University of British Columbia, Vancouver, BC V6T-1Z1, Canada.
Ejtehadi
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Plotkin
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D045304:Cytochromes c / Q000737:chemistry; D019206:GTP-Binding Protein alpha Subunits, Gi-Go / Q000737:chemistry; D007700:Kinetics; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D013816:Thermodynamics
C014059:CYC1 protein, S cerevisiae; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D045304:Cytochromes c; D019206:GTP-Binding Protein alpha Subunits, Gi-Go