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Enzyme evolution explained (sort of).
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