Conformational Transitions of Heteropolymers

TL;DR

This paper investigates the conformational transitions of protein-like heteropolymers using multicanonical sampling on lattice and off-lattice models, revealing general folding properties without requiring native topology.

Contribution

It introduces a multicanonical sampling approach to study heteropolymer folding on lattice and off-lattice models without native topology dependence.

Findings

Effective hydrophobic/polar models elucidate folding behavior.

Models operate without native topology input.

Applicable to general heteropolymer folding studies.

Abstract

We study conformational transitions of simple coarse-grained models for protein-like heteropolymers on the simple cubic lattice and off-lattice, respectively, by means of multicanonical sampling algorithms. The effective hydrophobic/polar models do not require the knowledge of the native topology for a given sequence of residues as input. Therefore these models are eligible to investigate general properties of the tertiary folding behaviour of such protein-like heteropolymers.