Cooperativity and Stability in a Langevin Model of Protein Folding

TL;DR

This paper investigates how the symmetry of potential energy functions affects protein folding dynamics, demonstrating that anisotropic potentials enhance cooperativity more effectively than isotropic ones.

Contribution

It introduces simplified Langevin-based models showing the impact of potential symmetry on folding cooperativity and stability.

Findings

Isotropic potentials yield modest cooperativity.

Anisotropic potentials produce strong cooperativity.

Potential symmetry influences folding thermodynamics.

Abstract

We present two simplified models of protein dynamics based on Langevin's equation of motion in a viscous medium. We explore the effect of the potential energy function's symmetry on the kinetics and thermodynamics of simulated folding. We find that an isotropic potential energy function produces, at best, a modest degree of cooperativity. In contrast, a suitable anisotropic potential energy function delivers strong cooperativity.