Our first area of research examines the mechanisms underlying the ubiquitin-mediated degradation pathway for removing unwanted proteins from cells, with particular focus on Parkinson’s Disease. Key proteins under study include parkin (mutated in Parkinson’s Disease) and other E2 conjugating and E3 ligase enzymes. We use biophysical techniques, such as NMR, to understand the structure, and hence, the function of these proteins. Such information contributes to our understanding of how these proteins normally work and what goes wrong when they are mutated, such as in Parkinson’s Disease.
Our second area of research examines membrane repair and trafficking by calcium-binding proteins. We focus on the S100 family of calcium sensors and in particular, S100A10. We use biophysical methods to determine the structure of this protein in complex with its binding partners. We plan to design small molecules that can influence the interaction and function of such binding partners.