Molecular Biology and Evolution, Vol 16, 1696-1710, Copyright © 1999 by Society for Molecular Biology and Evolution
P Lio and N Goldman
We present a model of amino acid sequence evolution based on a hidden
Markov model that extends to transmembrane proteins previous methods that
incorporate protein structural information into phylogenetics. Our model
aims to give a better understanding of processes of molecular evolution and
to extract structural information from multiple alignments of transmembrane
sequences and use such information to improve phylogenetic analyses. This
should be of value in phylogenetic studies of transmembrane proteins: for
example, mitochondrial proteins have acquired a special importance in
phylogenetics and are mostly transmembrane proteins. The improvement in fit
to example data sets of our new model relative to less complex models of
amino acid sequence evolution is statistically tested. To further
illustrate the potential utility of our method, phylogeny estimation is
performed on primate CCR5 receptor sequences, sequences of l and m subunits
of the light reaction center in purple bacteria, guinea pig sequences with
respect to lagomorph and rodent sequences of calcitonin receptor and K-
substance receptor, and cetacean sequences of cytochrome b.
ORIGINAL ARTICLE
Using protein structural information in evolutionary inference: transmembrane proteins
Department of Genetics, University of Cambridge, England.
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