Dr. Laurie Grove

Dr. Laurie Grove

I am an inorganic chemist by training, but became interested in research of a biochemical nature after studying metal-based reaction mechanisms in metalloenzymes. Since then I have been fundamentally interested in how protein structure dictates reactivity and ligand binding. Currently I am working on the problem of active site side chain flexibility, which results in conflicting mapping data for X-ray crystallographic structures of the same protein. The generation of alternative active site side chain conformations through the consideration of energetically favorable side chain rotamers allows us to use FTmap to detect key binding sites that otherwise may not have been predicted. Such an application is important in the field of drug discovery where rational drug design is often based on static X-ray crystallographic structures.