Two State Behavior in a Solvable Model of $\beta$-hairpin folding

TL;DR

This paper presents a simple, solvable model for $eta$-hairpin folding that captures the all-or-none two-state behavior driven by backbone stiffness and contact formation, providing insights into protein secondary structure formation.

Contribution

It introduces a new model linking backbone stiffness and contact formation to two-state folding, with a recursive method for phase diagram and rate calculations.

Findings

Reveals two-state folding behavior in the model

Provides a recursive relation for phase diagram computation

Derives exponential folding/unfolding rates

Abstract

Understanding the mechanism of protein secondary structure formation is an essential part of protein-folding puzzle. Here we describe a simple model for the formation of the $\beta$-hairpin, motivated by the fact that folding of a $\beta$-hairpin captures much of the basic physics of protein folding. We argue that the coupling of ``primary'' backbone stiffness and ``secondary'' contact formation (similar to the coupling between the ``secondary'' and ``tertiary'' structure in globular proteins), caused for example by side-chain packing regularities, is responsible for producing an all-or-none 2-state $\beta$-hairpin formation. We also develop a recursive relation to compute the phase diagram and single exponential folding/unfolding rate arising via a dominant transition state.