MixMD: Mapping Protein Surfaces to Discover Druggable Allosteric Sites

EVENT : C3BI Seminars

MixMD: MAPPING PROTEIN SURFACES TO DISCOVER DRUGABLE ALLOSTERIC SITES


Main speaker : Heather Carlson (Professor of Medicinal Chemistry, Professor of Chemistry), from Department of Chemistry, University of Michigan
Date : 17-05-2018 at 02:00 pm
Location : Auditorium Francois Jacob – BIME (26), Institut Pasteur, Paris


Research in the Carlson lab focuses broadly on the molecular recognition between ligands and proteins, from the fundamental biophysics of ligand binding to applied inhibitor design. Understanding protein flexibility, allosteric control, and ligand binding all require dynamic information at the atomic level. The technique that we prefer is molecular dynamics (MD) simulations. Our most recent projects have focused on developing mixed-solvent MD (MixMD), a surface-mapping technique which samples protein motion in a solution of water and organic probe molecules. This technique identifies possible binding hotspots for ligands and protein-protein interactions. It requires many MD simulations, typically 10-20 independent simulations of 20-100ns, to properly sample the possible configurations. This series of MD simulations must be done for each possible probe types. It is a resource intensive method, but it has the promise of identifying previously unknown regulatory sites on proteins. This could significantly increase the number of drug targets available to treat a wide variety of medical disorders.

 

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