Solvent-induced organization: A physical model of folding myoglobin

TL;DR

This paper presents a physical model that captures the solvent-driven folding process of myoglobin, successfully simulating its transition from an extended to native-like structure and extending the approach to leghemoglobin.

Contribution

It introduces a quantitative physical model based on solvent-induced hydrophobic forces to simulate protein folding, validated on myoglobin and leghemoglobin.

Findings

Realistic folding trajectories for myoglobin were generated.

The model accurately predicts key features of the folding process.

Extension of the model to leghemoglobin demonstrates its broader applicability.

Abstract

The essential features of the in vitro refolding of myoglobin are expressed in a solvable physical model. Alpha helices are taken as the fundamental collective coordinates of the system, while the refolding is assumed to be mainly driven by solvent-induced hydrophobic forces. A quantitative model of these forces is developed and compared with experimental and theoretical results. The model is then tested by being employed in a simulation scheme designed to mimic solvent effects. Realistic dynamic trajectories of myoglobin are shown as it folds from an extended conformation to a close approximation of the native state. Various suggestive features of the process are discussed. The tenets of the model are further tested by folding the single-chain plant protein leghemoglobin.