Chain length scaling of protein folding time
Condensed Matter
2009-10-28 v1 q-bio
Abstract
Folding of protein-like heteropolymers into unique 3D structures is investigated using Monte Carlo simulations on a cubic lattice. We found that folding time of chains of length scales as at temperature of fastest folding. For chains with random sequences of monomers , and for chains with sequences designed to provide a pronounced minimum of energy to their ground state conformation . Folding at low temperatures exhibits an Arrhenius-like behavior with the energy barrier , where is the energy of the native conformation. both for random and designed sequences.
Keywords
Cite
@article{arxiv.cond-mat/9606180,
title = {Chain length scaling of protein folding time},
author = {A. M. Gutin and V. I. Abkevich and E. I. Shakhnovich},
journal= {arXiv preprint arXiv:cond-mat/9606180},
year = {2009}
}