Scoring residue conservation.
The importance of a residue for maintaining the structure and function of a protein can usually be inferred from how conserved it appears in a multiple sequence alignment of that protein and its homologues. A reliable metric for quantifying residue conservation is desirable. Over the last two decades many such scores have been proposed, but none has emerged as a generally accepted standard. This work surveys the range of scores that biologists, biochemists, and, more recently, bioinformatics workers have developed, and reviews the intrinsic problems associated with developing and evaluating such a score. A general formula is proposed that may be used to compare the properties of different particular conservation scores or as a measure of conservation in its own right.
Biomolecular Structure and Modelling Unit, Department of Biochemistry and Molecular Biology, University College London, London, United Kingdom. William.Valdar@well.ox.ac.uk
William S J
WS
Valdar
D000596:Amino Acids / Q000737:chemistry; D017124:Conserved Sequence; D019277:Entropy; D019143:Evolution, Molecular; D009154:Mutation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein / Q000379:methods*; D013237:Stereoisomerism
D000596:Amino Acids; D011506:Proteins