Folding of Proteins in Go Models with Angular Interactions

TL;DR

This study investigates protein folding in Go models with angular interactions, revealing that folding times scale with protein size and are influenced by native structure but not contact order, providing insights into folding mechanisms.

Contribution

It introduces analysis of Go models with angular interactions, showing how folding times relate to protein size and structure, expanding understanding of folding dynamics.

Findings

Folding times follow power-law dependence on protein size.

Folding scenarios are mainly governed by contact order.

Folding times do not depend on relative contact order.

Abstract

Molecular dynamics studies of Go models of proteins with the 10-12 contact potential and the bond and dihedral angle terms indicate statistical similarities to other Go models, e.g. with the Lennard-Jones contact potentials. The folding times depend on the protein size as power laws with the exponents depending on the native structural classes. There is no dependence of the folding times on the relative contact order even though the folding scenarios are governed mostly by the contact order.