Wilke: Difference between revisions

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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.  

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In the latest issue of the journal PLoS Computational Biology, Claus Wilke [http://www.ploscompbiol.org/article/info%3Adoi%2F10.1371%2Fjournal.pcbi.1002572 reviews] the growing trend in the field of molecular evolution to incorporate molecular structure and function into computational work. This review is part of the popular [http://www.ploscollections.org/article/browseIssue.action?issue=info%3Adoi%2F10.1371%2Fissue.pcol.v03.i08 Editor's Outlook series] of the journal, where PLoS Computational Biology editors take stock of what computational biology has achieved to date and what it can hope to achieve in the near future.  

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