Four-states phase diagram of proteins

TL;DR

This paper develops a four-states phase diagram for protein folding based on an improved lattice model that incorporates temperature-dependent hydrophobic effects, capturing known denaturation phenomena and predicting new transitions.

Contribution

It introduces a novel four-states phase diagram model for protein folding that accounts for temperature-dependent solvent effects and predicts transitions between coil states.

Findings

Reproduces warm and cold denaturation transitions

Identifies a critical point in the phase diagram

Predicts transitions between two coil states

Abstract

A four states phase diagram for protein folding as a function of temperature and solvent quality is derived from an improved 2-d lattice model taking into account the temperature dependence of the hydrophobic effect. The phase diagram exhibits native, globule and two coil-type regions. In agreement with experiment, the model reproduces the phase transitions indicative of both warm and cold denaturations. Finally, it predicts transitions between the two coil states and a critical point.