Identification of Characteristic Protein Folding Channels in a Coarse-Grained Hydrophobic-Polar Peptide Model

TL;DR

This paper explores how different arrangements of hydrophobic and polar monomers in a simplified peptide model influence folding pathways and energy landscapes, revealing diverse folding behaviors like two-state, intermediates, and metastability.

Contribution

It introduces a minimalistic off-lattice coarse-grained model to analyze folding channels and energy landscapes of hydrophobic-polar heteropolymers, demonstrating varied folding behaviors based on monomer arrangements.

Findings

Reproduces two-state folding, intermediates, and metastability.

Shows folding behavior depends on monomer sequence arrangement.

Provides insights into folding mechanisms using a simple model.

Abstract

Folding channels and free-energy landscapes of hydrophobic-polar heteropolymers are discussed on the basis of a minimalistic off-lattice coarse-grained model. We investigate how rearrangements of hydrophobic and polar monomers in a heteropolymer sequence lead to completely different folding behaviors. Studying three exemplified sequences with the same content of hydrophobic and polar residues, we can reproduce within this simple model two-state folding, folding through intermediates, as well as metastability.