The cooperative nature of hydrophobic forces and protein folding kinetics

Jin Wang, Chilun Lee, George Stell

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

We study the effects of cooperative forces on protein folding kinetics using statistical energy landscape theory. We find that the mean first passage time for folding changes the shape from V to U-like curve dependence on the temperature when the effects of the cooperative forces are important, which is consistent with kinetic experiments. This supports the necessity for cooperative force. In addition, we find that cooperative forces tend to increase the free energy barrier so the kinetics is in general slower. Furthermore, we find that cooperative forces tend to suppress the fluctuations in kinetics more than non-cooperative forces. The cooperativity causes to the protein folding kinetics to be more two state-like.

Original languageEnglish
Pages (from-to)53-60
Number of pages8
JournalChemical Physics
Volume316
Issue number1-3
DOIs
StatePublished - 19 Sep 2005

Keywords

  • Cooperativity
  • Kinetic fluctuations
  • Protein folding kinetics

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