An exactly solvable model for a beta-hairpin with random interactions

TL;DR

This paper presents an exactly solvable disordered model for protein beta-hairpins, analyzing its free-energy and demonstrating self-averaging, providing insights into the effects of randomness on protein folding.

Contribution

It introduces a novel exactly solvable model for disordered protein folding, specifically for beta-hairpins, with exact free-energy calculation and proof of self-averaging.

Findings

Exact free-energy calculation for the disordered model

Proof of self-averaging property in the model

Insights into the role of random contact energies in protein folding

Abstract

I investigate a disordered version of a simplified model of protein folding, with binary degrees of freedom, applied to an ideal beta-hairpin structure. Disorder is introduced by assuming that the contact energies are independent and identically distributed random variables. The equilibrium free-energy of the model is studied, performing the exact calculation of its quenched value and proving the self-averaging feature.