Family specific rates of protein evolution.
BACKGROUND
Amino acid changing mutations in proteins are contstrained by purifying selection and accumulate at different rates. We estimate evolutionary rates on multiple alignments of eukaryotic protein families in a maximum likelihood framework and spot sets of slow and fast evolving proteins.


RESULTS
We find that the evolution of indispensable proteins is constrained by selection and that protein secretion is coupled to an increased evolutionary rate.
Luz
Hannes
H
Max Planck Institute for Molecular Genetics Ihnestrasse 73, 14195 Berlin, Germany. luz@molgen.mpg.de
Vingron
Martin
M
D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D003198:Computer Simulation; D017124:Conserved Sequence; D019143:Evolution, Molecular; D006801:Humans; D008957:Models, Genetic; D008969:Molecular Sequence Data; D020543:Proteome / Q000145:classification / Q000235:genetics* / Q000378:metabolism*; D016415:Sequence Alignment / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D020543:Proteome