PMID: 11308693Apr 20, 2001Paper

Thermodynamically important contacts in folding of model proteins

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
A ScalaH E Stanley

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.

References

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Mar 4, 2000·Journal of Molecular Biology·N V DokholyanE I Shakhnovich

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Citations

May 2, 2006·Biophysical Journal·Fabio CecconiRoberto Livi
Sep 8, 2001·Journal of Molecular Biology·N V Dokholyan, E I Shakhnovich

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