Picture of two heads

Open Access research that challenges the mind...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including those from the School of Psychological Sciences & Health - but also papers by researchers based within the Faculties of Science, Engineering, Humanities & Social Sciences, and from the Strathclyde Business School.

Discover more...

Evaluation of a novel method for the identification of coevolving protein residues

Dufton, M.J. and Pritchard, L. and Bladon, P. and Mitchell, J. (2001) Evaluation of a novel method for the identification of coevolving protein residues. Protein Engineering, 14 (6). pp. 549-55. ISSN 0269-2139

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

A novel method for the identification of correlated pairs in aligned homologous protein sequences is presented and evaluated against a model of simulated protein evolution incorporating covariation. Our method is shown to be capable of identifying all coevolutionary pairs of sites, with minimal interference by background correlations, in aligned sequence sets containing ∼60 sequences with a tree depth of at least 30 accepted point mutations. This result is expected even in the presence of a large degree of neutral and non-correlated evolution. It is postulated that, since naturally occurring protein families may be subject to stronger selection pressures and a lesser degree of neutral evolution, this method of covariation analysis may be generally more robust than the model would indicate