Different Kinds of Protein Folding Identified with a Coarse-Grained Heteropolymer Model

TL;DR

This study uses multicanonical simulations on a coarse-grained heteropolymer model to explore diverse folding behaviors in peptides, revealing how sequence variations influence folding pathways and stability.

Contribution

It introduces a mesoscopic hydrophobic-polar model combined with multicanonical simulations to analyze folding channels in heteropolymers, highlighting sequence-dependent folding diversity.

Findings

Different folding channels identified for various sequences

Folding behaviors resemble those of realistic peptides

Sequence composition influences folding pathways

Abstract

Applying multicanonical simulations we investigated folding properties of off-lattice heteropolymers employing a mesoscopic hydrophobic-polar model. We study for various sequences folding channels in the free-energy landscape by comparing the equilibrium conformations with the folded state in terms of an angular overlap parameter. Although all investigated heteropolymer sequences contain the same content of hydrophobic and polar monomers, our analysis of the folding channels reveals a variety of characteristic folding behaviors known from realistic peptides.