Effective potentials for Folding Proteins
Statistical Mechanics
2009-11-11 v2 Soft Condensed Matter
Abstract
A coarse-grained off-lattice model that is not biased in any way to the native state is proposed to fold proteins. To predict the native structure in a reasonable time, the model has included the essential effects of water in an effective potential. Two new ingredients, the dipole-dipole interaction and the local hydrophobic interaction, are introduced and are shown to be as crucial as the hydrogen bonding. The model allows successful folding of the wild-type sequence of protein G and may have provided important hints to the study of protein folding.
Cite
@article{arxiv.cond-mat/0601533,
title = {Effective potentials for Folding Proteins},
author = {Nan-yow Chen and Zheng-Yao Su and Chung-Yu Mou},
journal= {arXiv preprint arXiv:cond-mat/0601533},
year = {2009}
}
Comments
4 pages, 4 figures, to appear in Physical Review Letters