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Evaluating the efficacy of a structure-derived amino acid substitution matrix in detecting protein homologs by BLAST and PSI-BLAST

Authors Goonesekere N

Published 5 June 2009 Volume 2009:2 Pages 71—78

DOI https://doi.org/10.2147/AABC.S5553

Review by Single-blind

Peer reviewer comments 3

Nalin CW Goonesekere

Department of Chemistry and Biochemistry, University of Northern iowa, Cedar Falls, IA, USA

Abstract: The large numbers of protein sequences generated by whole genome sequencing projects require rapid and accurate methods of annotation. The detection of homology through computational sequence analysis is a powerful tool in determining the complex evolutionary and functional relationships that exist between proteins. Homology search algorithms employ amino acid substitution matrices to detect similarity between proteins sequences. The substitution matrices in common use today are constructed using sequences aligned without reference to protein structure. Here we present amino acid substitution matrices constructed from the alignment of a large number of protein domain structures from the structural classification of proteins (SCOP) database. We show that when incorporated into the homology search algorithms BLAST and PSI-blaST, the structure-based substitution matrices enhance the efficacy of detecting remote homologs.

Keywords: computational biology, protein homology, amino acid substitution matrix, protein structure

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