Cooperativity and Stability in a Langevin Model of Protein Folding
Statistical Mechanics
2009-10-28 v2 q-bio
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.
Keywords
Cite
@article{arxiv.cond-mat/9610105,
title = {Cooperativity and Stability in a Langevin Model of Protein Folding},
author = {Gabriel F. Berriz and Alexander M. Gutin and Eugene I. Shakhnovich},
journal= {arXiv preprint arXiv:cond-mat/9610105},
year = {2009}
}
Comments
45 pages, 16 figures, 2 tables. LaTeX. Submitted to the Journal of Chemical Physics