Consistent treatment of hydrophobicity in protein lattice models accounts for cold denaturation

TL;DR

This paper presents a new implicit solvent model that explicitly incorporates the hydrophobic effect's entropic and enthalpic contributions, successfully explaining cold denaturation and temperature-dependent heat capacity in proteins.

Contribution

It introduces a consistent treatment of hydrophobicity in protein lattice models, accounting for length-scale and temperature dependence of solvation effects.

Findings

The model explains cold denaturation phenomena.

It reproduces heat capacity measurements of proteins.

The approach captures key thermodynamic effects of hydrophobic interactions.

Abstract

The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavourable interactions between hydrophobic residues and water through the formation of a hydrophobic core. Here we include the entropic and enthalpic contributions of the hydrophobic effect explicitly in an implicit solvent model. This allows us to capture two important effects: a length-scale dependence and a temperature dependence for the solvation of a hydrophobic particle. This consistent treatment of the hydrophobic effect explains cold denaturation and heat capacity measurements of solvated proteins.