Dominant Folding Pathways of a Beta-Hairpin

TL;DR

This paper applies the Dominant Reaction Pathway method to study beta-hairpin folding, comparing it with molecular dynamics simulations, and finds consistent results with minimal influence from non-native hydrophobic interactions.

Contribution

It demonstrates the effectiveness of the DRP approach in modeling protein folding pathways and validates it against MD simulations for a beta-hairpin.

Findings

DRP and MD yield consistent folding pathways

Non-native hydrophobic interactions have small effects

DRP is a reliable alternative to MD for folding studies

Abstract

We use the Dominant Reaction Pathway (DRP) approach to study the dynamics of the folding of a beta-hairpin, within a model which accounts for both native and non-native interactions. We compare the most probable folding pathways calculated with the DRP method with those obtained directly from molecular dynamics (MD) simulations. We find that the two approaches give completely consistent results. We investigate the effects of the non-native hydrophobic interactions on the folding dynamics found them to be small.