The Sanders Lab
Research in my lab is focused on understanding how proteins function, by studying their atomic resolution structures. Using protein X-ray crystallography as a tool for elucidating structures, we combine structural studies with enzymology, site-directed mutagenesis and computer-aided design of inhibitors to understand how proteins function. The determination of the 3-D structures of proteins and their complexes enable us to answer important questions about how these proteins function, and how they interact with their substrates and each other.
At the University of Saskatchewan, we are ideally placed to carry out this research, due to the presence of the Canadian Light Source (CLS), Canada's own synchrotron light source, the Saskatchewan Structural Sciences Center, a facility equipped with instruments for biophysical characterizations of macromolecules, and the Protein Characterization and Crystallization Facility (PCCF).
Protein-protein Interactions
The study of protein-protein interactions is a tremendously large field, but the presence of both the Canadian Light Source and the Saskatchewan Structural Sciences Centre places us in a wonderful position to be able to carry out numerous studies on the molecular basis of how macromolecular assemblies are formed, and the forces that are required to allow molecules to specifically recognize each other and form complexes. Thioredoxins (Trx) are part of the other ubiquitous redox-regulating system and act through Thioredoxin Reductase (TrxR) to reduce protein disulfide bonds. Despite highly similar structures, these systems show species specificity in their recognition, as the proteins from the same organism show better recognition than those from different organisms. We are currently determining the structures of the main components of this system (Trx and TrxR) from different extremophiles (bacteria that grow in hot or cold environments). Our goal is understand how these proteins recognize each other and what contributes towards the recognition specificity.