Statistical Mechanics Model for Protein Folding

TL;DR

This paper introduces a new statistical mechanics framework to model protein folding and unfolding in water, linking thermodynamic properties with experimental data for specific proteins.

Contribution

It develops a novel formalism based on partition functions for two-stage protein folding kinetics in aqueous environments.

Findings

Heat capacity dependencies match experimental data

Partition function formalism accurately describes folding transitions

Model applies to proteins like staphylococcal nuclease and metmyoglobin

Abstract

We present a novel statistical mechanics formalism for the theoretical description of the process of protein folding$\leftrightarrow$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.