Quantitative thermodynamic model for globular protein folding

Regular Article

DOI: 10.1140/epjd/e2014-50097-3

Cite this article as:
Yakubovich, A. & Solov’yov, A. Eur. Phys. J. D (2014) 68: 145. doi:10.1140/epjd/e2014-50097-3
Part of the following topical collections:
  1. Topical Issue: Nano-scale Insights into Ion-beam Cancer Therapy

Abstract

We present a statistical mechanics formalism for theoretical description of the process of protein folding ↔ unfolding transition in water environment. The formalism is based on the construction of the partition function of a protein obeying two-stage-like folding kinetics. Using the statistical mechanics model of solvation of hydrophobic hydrocarbons we obtain the partition function of infinitely diluted solution of proteins in water environment. The calculated dependencies of the protein heat capacities upon temperature are compared with the corresponding results of experimental measurements for staphylococcal nuclease and metmyoglobin.

Copyright information

© EDP Sciences, SIF, Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Alexander V. Yakubovich
    • 1
  • Andrey V. Solov’yov
    • 1
  1. 1.MBN Research Center, Altenhöferallee 3Frankfurt am MainGermany