<font size="4">A structural Perspective on Protein Sequence Evolution</font>
Posted on 09/12/2012
Today, the Wilke lab has published two studies on the selective pressures that protein structure exerts on evolving genetic sequences. [http://www.biomedcentral.com/1471-2148/12/179/abstract The first,] published in BMC Evol. Biol., looks at broad evolutionary trends in yeast. This study shows that evolutionary rate varies linearly with relative solvent accessibility of residues (RSA, a measure for how close to the surface or the core of the protein a residue is located). Hence, more exposed residues evolve faster than more buried residues. [http://mbe.oxfordjournals.org/content/early/2012/09/12/molbev.mss217 The second study], published in Mol. Biol. Evol., uses the insight gained from the first to identify individual sites in viral protein that evolve more rapidly or more slowly than expected given their RSA. When applied to two proteins of the influenza virus, hemagglutinin and neuraminidase, this method identified sites involved in cell entry, antibody binding, and drug resistance.