Protein folding rates correlate with heterogeneity of folding mechanism
Date
2004
Authors
Öztop, B.
Ejtehadi, M. R.
Plotkin, S. S.
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Supervisor
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Instructor
Source Title
Physical Review Letters
Print ISSN
0031-9007
Electronic ISSN
1079-7114
Publisher
American Physical Society
Volume
93
Issue
20
Pages
208105-1 - 208105-4
Language
English
Type
Journal Title
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Volume Title
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Abstract
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.
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Keywords
Amino acids , Chemical relaxation , Computer simulation , Concentration (process) , Conformations , Data acquisition , Data reduction , Free energy , Mathematical models , Probability density function , Folding rates , Heterogeneity , Native contacts , Transition state , Proteins , CYC1 protein, S cerevisiae , Inhibitory guanine nucleotide binding protein , Protein , Saccharomyces cerevisiae protein