Protein folding rates correlate with heterogeneity of folding mechanism
Ejtehadi, M. R.
Plotkin, S. S.
Physical Review Letters
American Physical Society
208105-1 - 208105-4
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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.
Probability density function
CYC1 protein, S cerevisiae
Inhibitory guanine nucleotide binding protein
Saccharomyces cerevisiae protein
Published Version (Please cite this version)http://dx.doi.org/10.1103/PhysRevLett.93.208105
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