Stability of Designed Proteins Against Mutations
Soft Condensed Matter
2009-10-31 v1 q-bio
Abstract
The stability of model proteins with designed sequences is assessed in terms of the number of sequences (obtained from the designed sequence through mutations), which fold into 5the ``native'' conformation. By a complete enumeration of the total number of sequences obtained by introducing up to 4 point mutations and up to 7 composition--conserving mutations (swapping of amino acids) in a 36mers chain, it is found that there are sequences which in the folding process target onto the ``native'' conformation. Consequently, proteins with designed sequences display a remarkable degree of stability and, to a large extent, of designability.
Keywords
Cite
@article{arxiv.cond-mat/9809410,
title = {Stability of Designed Proteins Against Mutations},
author = {R. A Broglia and G. Tiana and H. E. Roman and E. Vigezzi and E. I. Shakhnovich},
journal= {arXiv preprint arXiv:cond-mat/9809410},
year = {2009}
}