Function-structure analysis of proteins using covarion-based evolutionary approaches: Elongation factors.

ABSTRACT: The divergent evolution of protein sequences from genomic databases can be analyzed by the use of different mathematical models. The most common treat all sites in a protein sequence as equally variable. More sophisticated models acknowledge the fact that purifying selection generally tolerates variable amounts of amino acid replacement at different positions in a protein sequence. In their "stationary" versions, such models assume that the replacement rate at individual positions remains constant throughout evolutionary history. "Nonstationary" covarion versions, however, allow the replacement rate at a position to vary in different branches of the evolutionary tree. Recently, statistical methods have been developed that highlight this type of variation in replacement rates. Here, we show

SUBMITTER: Gaucher EA 

PROVIDER: S-EPMC14624 | biostudies-literature | 2001 Jan

REPOSITORIES: biostudies-literature