Dominant folding pathways of a peptide chain, from ab-initio quantum-mechanical simulations

TL;DR

This paper introduces a novel ab-initio quantum-mechanical simulation method to study the dominant folding pathways of a peptide chain, enabling analysis of out-of-equilibrium dynamics and electronic structure rearrangements without empirical force fields.

Contribution

The proposed method allows direct investigation of peptide conformational transitions and electronic changes, surpassing traditional force field limitations.

Findings

Ab-initio simulations reveal detailed folding pathways.

Comparison shows advantages over standard force fields.

Method captures electronic structure rearrangements during transitions.

Abstract

Using the Dominant Reaction Pathways method, we perform an ab-initio quantum-mechanical simulation of a conformational transition of a peptide chain. The method we propose makes it possible to investigate the out-of-equilibrium dynamics of these systems, without resorting to an empirical representation of the molecular force field. It also allows to study rare transitions involving rearrangements in the electronic structure. By comparing the results of the ab-initio simulation with those obtained employing a standard force field, we discuss its capability to describe the non-equilibrium dynamics of conformational transitions.