Quantifying the effect of burial of amino acid residues on protein stability.

TitleQuantifying the effect of burial of amino acid residues on protein stability.
Publication TypeJournal Article
Year of Publication2004
AuthorsZhou, H, Zhou Y
JournalProteins
Volume54
Pagination315-22
Date Published2004 Feb 1
Abstract

The average contribution of individual residue to folding stability and its dependence on buried accessible surface area (ASA) are obtained by two different approaches. One is based on experimental mutation data, and the other uses a new knowledge-based atom-atom potential of mean force. We show that the contribution of a residue has a significant correlation with buried ASA and the regression slopes of 20 amino acid residues (called the buriability) are all positive (pro-burial). The buriability parameter provides a quantitative measure of the driving force for the burial of a residue. The large buriability gap observed between hydrophobic and hydrophilic residues is responsible for the burial of hydrophobic residues in soluble proteins. Possible factors that contribute to the buriability gap are discussed.

Pub Med Link

http://www.ncbi.nlm.nih.gov/pubmed/14696193?dopt=Abstract

Alternate JournalProteins
Citekey14696193