Study of a model for the folding of a small protein
Biomolecules
2009-11-11 v2
Abstract
We describe the results obtained from an improved model for protein folding. We find that a good agreement with the native structure of a 46 residue long, five-letter protein segment is obtained by carefully tuning the parameters of the self-avoiding energy. In particular we find an improved free-energy profile. We also compare the efficiency of the multidimensional replica exchange method with the widely used parallel tempering.
Keywords
Cite
@article{arxiv.q-bio/0503034,
title = {Study of a model for the folding of a small protein},
author = {Andrea Nobile and Federico Rapuano},
journal= {arXiv preprint arXiv:q-bio/0503034},
year = {2009}
}
Comments
typos corrected, one figure added