Folding Mechanism of Small Proteins

TL;DR

This study uses Monte Carlo simulations to explore how small proteins fold, revealing that both thermodynamics and kinetics influence the folding pathway, with early folding trajectories playing a crucial role.

Contribution

It demonstrates that protein folding mechanisms are governed by both thermodynamic and kinetic factors, emphasizing the importance of early folding trajectories.

Findings

Collapse occurs early in folding process

Proteins fold into native-like conformations at suitable temperatures

Early folding trajectories determine the folding pathway

Abstract

Extensive Monte Carlo folding simulations for four proteins of various structural classes are carried out, using a single atomistic potential. In all cases, collapse occurs at a very early stage, and proteins fold into their native-like conformations at appropriate temperatures. The results demonstrate that the folding mechanism is controlled not only by thermodynamic factors but also by kinetic factors: The way a protein folds into its native structure, is also determined by the convergence point of early folding trajectories, which cannot be obtained by the free energy surface.