Exact Solution of the Munoz-Eaton Model for Protein Folding

TL;DR

This paper introduces an exact transfer-matrix method to compute the partition function of the Munoz-Eaton protein folding model, linking folding kinetics to thermodynamics and topology, and demonstrates its application on specific proteins.

Contribution

The paper develops a transfer-matrix formalism for exact calculation of the Munoz-Eaton model's partition function, enabling detailed analysis of protein folding dynamics.

Findings

Exact partition function calculation for specific proteins

Comparison with previous results shows improved accuracy

Method applicable to any protein with known native state

Abstract

A transfer-matrix formalism is introduced to evaluate exactly the partition function of the Munoz-Eaton model, relating the folding kinetics of proteins of known structure to their thermodynamics and topology. This technique can be used for a generic protein, for any choice of the energy and entropy parameters, and in principle allows the model to be used as a first tool to characterize the dynamics of a protein of known native state and equilibrium population. Applications to a $\beta$-hairpin and to protein CI-2, with comparisons to previous results, are also shown.