Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 44, Pages 17874-17879Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1311599110
Keywords
funnel; internal friction; frustration; reaction coordinate; Go models
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Funding
- Intramural Research Program of the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health
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The recent availability of long equilibrium simulations of protein folding in atomistic detail for more than 10 proteins allows us to identify the key interactions driving folding. We find that the collective fraction of native amino acid contacts, Q, captures remarkably well the transition states for all the proteins with a folding free energy barrier. Going beyond this global picture, we devise two different measures to quantify the importance of individual interresidue contacts in the folding mechanism: (i) the log-ratio of lifetimes of contacts during folding transition paths and in the unfolded state and (ii) a Bayesian measure of how predictive the formation of each contact is for being on a transition path. Both of these measures indicate that native, or near-native, contacts are important for determining mechanism, as might be expected. More remarkably, however, we found that for almost all the proteins, with the designed protein alpha D-3 being a notable exception, nonnative contacts play no significant part in determining folding mechanisms.
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