Two-State Folding Kinetics of Small Proteins in the Sequential Collapse Model: Dependence of the Folding Rate on Contact Order and Temperature

Fernando Bergasa-Caceres, Herschel A. Rabitz

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

In this paper, the dynamics of the collapse-like folding transitions of globular proteins with two-state kinetics is studied. The analyses rely on a simple free energy functional for the formation of protein contacts developed for the study of multistate folding pathways in the sequential collapse model (SCM). The resulting model predicts an approximate linear dependence of the folding rate with the contact order of the native structure. It is also consistent with experimental results that show an Arrhenius-like temperature dependence for the collapse rate when corrected for the effect of protein stability.

Original languageEnglish (US)
Pages (from-to)12874-12877
Number of pages4
JournalJournal of Physical Chemistry B
Volume107
Issue number46
DOIs
StatePublished - Nov 20 2003

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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