Journal article
Enzyme evolution explained (sort of).
Abstract
Sites in proteins evolve at markedly different rates; some are highly conserved, others change rapidly. We have developed a maximum likelihood method to identify regions of a protein that evolve rapidly or slowly relative to the remaining structure. We also show that solvent accessibility and distance from the catalytic site are major determinants of evolutionary rate in eubacterial isocitrate dehydrogenases. These two variables account for …
Authors
DEAN AM; BRIAN GOLDING G
Journal
Biocomputing, , , pp. 6–17
Publisher
World Scientific Publishing
Publication Date
December 1999
DOI
10.1142/9789814447331_0002
ISSN
2335-6928