Evolution of Proteins / Statistics of the
Evolutionary Trace
The evolutionary trace method is a systematic, transparent and novel
predictive technique that identifies active sites and functional interfaces
in proteins with known structre. It is based on the extraction of
functionally important residues from sequence conservation and variation
patterns in homologous proteins, and on their mapping onto the protein
surface to generate clusters identifying functional interfaces. The
evolutionary trace has the ability to delineate functional epitopes and
identify residues critical to binding specificity. Based on mutational
evolutinary analysis and on the structural homology of protein families,
this versatile approach should help focus site-directed mutagenesis studies
of structure-function relationships in macromolecules, as well as studies of
specificity in molecular recognition. More generally, it provides an
evolutionary perspective for judging the functional or structural role of
each residue in a protein structure.
The evolutionary trace was created by Olivier Lichtarge. Click here to
learn more about Dr. Lichtarge and his lab.
Some preliminary statistical analysis has been done on the evolutionary trace
procedure as well. The see the thesis proposal written by Heidi Spratt describing the statistical
analysis click here.