A Model for the Thermodynamics of Globular Proteins

TL;DR

This paper presents a statistical mechanics model for globular protein stability, capturing hot and cold folding transitions and predicting a novel universality class for a critical point influenced by water interactions.

Contribution

It introduces a simple Hamiltonian model that accounts for protein self-interactions and water effects, revealing new critical phenomena in protein thermodynamics.

Findings

Model predicts hot and cold folding transitions.

Identifies a new universality class for the critical point.

Highlights the role of water interactions in protein stability.

Abstract

Comments: 6 pages RevTeX, 6 Postscript figures. We review a statistical mechanics treatment of the stability of globular proteins based on a simple model Hamiltonian taking into account protein self interactions and protein-water interactions. The model contains both hot and cold folding transitions. In addition it predicts a critical point at a given temperature and chemical potential of the surrounding water. The universality class of this critical point is new.