A novel method to detect proteins evolving at correlated rates: identifying new functional relationships between coevolving proteins.

ABSTRACT: Interacting proteins evolve at correlated rates, possibly as the result of evolutionary pressures shared by functional groups and/or coevolution between interacting proteins. This evolutionary signature can be exploited to learn more about protein networks and to infer functional relationships between proteins on a genome-wide scale. Multiple methods have been introduced that detect correlated evolution using amino acid distances. One assumption made by these methods is that the neutral rate of nucleotide substitution is uniform over time; however, this is unlikely and such rate heterogeneity would adversely affect amino acid distance methods. We explored alternative methods that detect correlated rates using protein-coding nucleotide sequences in order to better estimate the rate of nonsy

SUBMITTER: Clark NL 

PROVIDER: S-EPMC2877527 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature