Enzyme evolution explained (sort of).

A. M. Dean, G. B. Golding

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

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 most of the rate heterogeneity not ascribable to stochastic effects.

Original languageEnglish (US)
Pages (from-to)6-17
Number of pages12
JournalPacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
StatePublished - 2000

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