Thermodynamically important contacts in folding of model proteins

Antonio Scala, Nikolay N. Dokholyan, Sergey S. Buldyrev, Eugene E. Stanley

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

We introduce a quantity, the entropic susceptibility, that measures the thermodynamic importance—for the folding transition—of the contacts between amino acids in model proteins. Using this quantity, we find that only one equilibrium run of a computer simulation of a model protein is sufficient to select a subset of contacts that give rise to the peak in the specific heat observed at the folding transition. To illustrate the method, we identify thermodynamically important contacts in a model 46-mer. We show that only about 50% of all contacts present in the protein native state are responsible for the sharp peak in the specific heat at the folding transition temperature, while the remaining 50% of contacts do not affect the specific heat.

All Science Journal Classification (ASJC) codes

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics

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