Water drives peptide conformational transitions

TL;DR

This study demonstrates that water molecules play a crucial role in driving conformational transitions of a dipeptide, as shown through molecular dynamics simulations analyzing water-peptide interactions.

Contribution

It reveals water as the primary driving force behind peptide conformational changes, highlighting the importance of solvent effects in molecular dynamics.

Findings

Water distribution changes precede conformational transitions

Strong dynamical correlations between water and peptide motions

Water acts as the main driver of peptide conformational changes

Abstract

Transitions between metastable conformations of a dipeptide are investigated using classical molecular dynamics simulation with explicit water molecules. The distribution of the surrounding water at different moments before the transitions and the dynamical correlations of water with the peptide's configurational motions indicate that water is the main driving force of the conformational changes.