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Why Do Protein Folding Rates Correlate with Metrics of Native Topology?

Authors
Journal
PLoS ONE
1932-6203
Publisher
Public Library of Science
Publication Date
Volume
7
Issue
4
Identifiers
DOI: 10.1371/journal.pone.0035599
Keywords
  • Research Article
  • Biology
  • Biochemistry
  • Proteins
  • Protein Chemistry
  • Biophysics
  • Biophysics Simulations
  • Protein Folding
  • Computational Biology
  • Biophysic Al Simulations
  • Computer Science
  • Computerized Simulations
  • Physics
Disciplines
  • Biology
  • Mathematics

Abstract

For almost 15 years, the experimental correlation between protein folding rates and the contact order parameter has been under scrutiny. Here, we use a simple simulation model combined with a native-centric interaction potential to investigate the physical roots of this empirical observation. We simulate a large set of circular permutants, thus eliminating dependencies of the folding rate on other protein properties (e.g. stability). We show that the rate-contact order correlation is a consequence of the fact that, in high contact order structures, the contact order of the transition state ensemble closely mirrors the contact order of the native state. This happens because, in these structures, the native topology is represented in the transition state through the formation of a network of tertiary interactions that are distinctively long-ranged.

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