Statistical Analysis of Native Contact Formation in the Folding of Designed Model Proteins
Condensed Matter
2009-10-31 v1 q-bio
Abstract
The time evolution of the formation probability of native bonds has been studied for designed sequences which fold fast into the native conformation. From this analysis a clear hierarchy of bonds emerge a) local, fast forming highly stable native bonds built by some of the most strongly interacting amino acids of the protein, b) non-local bonds formed late in the folding process, in coincidence with the folding nucleus, and involving essentially the same strongly interacting amino acids already participating in the fast bonds, c) the rest of the native bonds whose behaviour is subordinated, to a large extent, to that of the local- and non-local native contacts.
Cite
@article{arxiv.cond-mat/0010394,
title = {Statistical Analysis of Native Contact Formation in the Folding of Designed Model Proteins},
author = {G. Tiana and R. A. Broglia},
journal= {arXiv preprint arXiv:cond-mat/0010394},
year = {2009}
}