pith. sign in

arxiv: cond-mat/0010394 · v1 · submitted 2000-10-25 · ❄️ cond-mat · q-bio

Statistical Analysis of Native Contact Formation in the Folding of Designed Model Proteins

classification ❄️ cond-mat q-bio
keywords bondsnativefastfoldingacidsaminoanalysisdesigned
0
0 comments X
read the original 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.

This paper has not been read by Pith yet.

discussion (0)

Sign in with ORCID, Apple, or X to comment. Anyone can read and Pith papers without signing in.