https://doi.org/10.1140/epjd/e2014-50097-3
Regular Article
Quantitative thermodynamic model for globular protein folding*
MBN Research Center, Altenhöferallee 3,
60438
Frankfurt am Main,
Germany
a e-mail: sasha@mbnexplorer.com
Received:
2
February
2014
Received in final form:
27
March
2014
Published online:
23
June
2014
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.
© EDP Sciences, Società Italiana di Fisica, Springer-Verlag 2014
