English

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 NN scales as NλN^\lambda at temperature of fastest folding. For chains with random sequences of monomers λ6\lambda \approx 6, and for chains with sequences designed to provide a pronounced minimum of energy to their ground state conformation λ4\lambda \approx 4. Folding at low temperatures exhibits an Arrhenius-like behavior with the energy barrier EbϕEnE_b \approx \phi |E_n|, where EnE_n is the energy of the native conformation. ϕ0.18\phi \approx 0.18 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}
}