Topological complexity, contact order and protein folding rates

TL;DR

This study uses Monte Carlo simulations to explore how topological features like contact order influence protein folding rates, revealing a strong correlation especially in longer, more complex proteins, aligning with experimental observations.

Contribution

It demonstrates a significant correlation between contact order and folding time in proteins, highlighting the importance of topology in folding kinetics through simulation and experimental comparison.

Findings

Higher contact order correlates with longer folding times.

The correlation is strongest for proteins with N=80 amino acids.

Simulation results align with experimental data on protein folding.

Abstract

Monte Carlo simulations of protein folding show the emergence of a strong correlation between the relative contact order parameter, CO, and the folding time, t, of two-state folding proteins for longer chains with number of amino acids, N>=54, and higher contact order, CO > 0.17. The correlation is particularly strong for N=80 corresponding to slow and more complex folding kinetics. These results are qualitatively compatible with experimental data where a general trend towards increasing t with CO is indeed observed in a set of proteins with chain length ranging from 41 to 154 amino acids.