UNSPECIFIED (1998) Assessing the impact of secondary structure and solvent accessibility on protein evolution. GENETICS, 149 (1). pp. 445-458. ISSN 0016-6731

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Abstract

Empirically derived models of amino acid replacement are employed to study the association between various physical features of proteins and evolution. The strengths of these associations are statistically evaluated by applying the models of protein evolution to 11 diverse sets of protein sequences. Parametric bootstrap tests indicate that the solvent accessibility status of a site has a particularly strong association with the process of amino acid replacement that it experiences. Significant association between secondary structure environment and the amino acid replacement process is also observed. Careful description of the length distribution of secondary structure elements and of the organization of secondary structure and solvent accessibility along a protein did not always significantly improve the fit of the evolutionary models to the data sets that were analyzed. As indicated by the strength of the association of both solvent accessibility and secondary structure with amino acid replacement, the process of protein evolution-both above and below the species level-will not be well understood until the physical constraints that affect protein evolution are identified and characterized.

Item Type:	Journal Article
Subjects:	Q Science > QH Natural history > QH426 Genetics
Journal or Publication Title:	GENETICS
Publisher:	GENETICS
ISSN:	0016-6731
Date:	May 1998
Volume:	149
Number:	1
Number of Pages:	14
Page Range:	pp. 445-458
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/15750

Data sourced from Thomson Reuters' Web of Knowledge

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