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Abstract:

Enzymes are dynamic molecules, and this flexibility is essential to their catalytic function. Yet, computational enzyme design algorithms are typically performed using a single protein scaffold as design template, ignoring the important contributions of dynamics in enzyme catalysis. For the past few years, my group has developed multistate computational protein design methods that allow proteins to be modelled as structural ensembles that more realistically represent the range of conformations that these molecules can adopt in solution. Here, I will show our recent work in the development of ensemble-based computational enzyme design algorithms and their application in the design of enzyme catalysis, multisubstrate specificity, and conformational equilibrium.

Bio:

Roberto Chica received his B.Sc. in biochemistry from Universit茅 de Montr茅al in 2001 and his Ph.D. from the same institution in 2007 under the mentorship of Joelle Pelletier and Jeffrey Keillor. After working at Caltech as postdoctoral fellow with Stephen Mayo, he joined the Department of Chemistry at the University of Ottawa in 2010, where he is now Full Professor. Since establishing his independent research program, Dr. Chica has been pushing the boundaries of protein engineering through his pioneering work in the development and experimental validation of multistate approaches to computational protein design. In 2019 he was awarded the Melanie O鈥橬eill Young Investigator Award in Biological Chemistry from the Canadian Society for Chemistry, as well as the Young Investigator Award of the Biophysical Society of Canada for his advances in protein design. His current research interests include the computational design of de novo enzymes and protein-based biosensors.