Nonlinear Dynamics Seminar

Claus Wilke, Department of Integrative Biology and ICMB, UT-Austin

"Structural and functional constraints on protein evolution"

1:00pm, RLM 11.204

Abstract: Protein-coding genes evolve under constraints imposed by the structural and functional properties of the encoded protein. In particular, buried residues, residues in or near active sites in enzymes, and residues involved in protein-protein interfaces experience increased purifying selection and evolve more slowly than other residues. In this talk, I will discuss the relative strengths of these effects. In particular, I will show that even though most active sites of enzymes are located in the protein core, we can disentangle conservation due to solvent accessibility and conservation due to enzymatic activity. We also find that catalytic residues in enzymes exert a long-range effect, causing increased conservation of residues throughout 80% of a typical enzyme structure. Finally, I will show that protein-protein interfaces show surprisingly little sequence divergence, and that interfaces can diverge substantially yet retain the ability to bind to ancestral binding partners.