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Quantifying the effect of burial of amino acid residues on protein stability
Author(s) -
Zhou Hongyi,
Zhou Yaoqi
Publication year - 2003
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10584
Subject(s) - amino acid residue , residue (chemistry) , accessible surface area , chemistry , protein folding , amino acid , folding (dsp implementation) , computational chemistry , peptide sequence , biochemistry , electrical engineering , gene , engineering
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. Proteins 2004;54:000–000. © 2003 Wiley‐Liss, Inc.