Kinetic non-optimality and vibrational stability of proteins

TL;DR

This paper investigates the folding kinetics and stability of proteins using Go models and Lennard-Jones potentials, revealing non-optimal folding behavior and correlations between mechanical and thermodynamic stability.

Contribution

It demonstrates that protein folding times follow power law trends under optimal conditions and shows the dependence of these trends on native geometry, highlighting non-optimality in the models.

Findings

Folding times follow robust power law trends.

Power law exponent varies with native geometry.

Mechanical and thermodynamic stabilities are correlated.

Abstract

Scaling of folding times in Go models of proteins and of decoy structures with the Lennard-Jones potentials in the native contacts reveal %robust power law trends when studied under optimal folding conditions. The power law exponent depends on the type of native geometry. Its value indicates lack of kinetic optimality in the model proteins. In proteins, mechanical and thermodynamic stabilities are correlated.