Proteins at the centre of human health and disease
Our laboratory seeks to understand the molecular structure and function of proteins, including those involved in human health and disease. One area of focus is on members of the DP1/reticulon family, which are integral membrane proteins responsible for maintaining the high curvature of the tubular ER. Mutations in DP1/reticulon proteins are associated with neuronal diseases such as Hereditary Spastic Paraplegia. We also have a long-standing in interest in determining the molecular mechanisms by which Influenza virus proteins function. We are studying the protein-protein and lipid interactions of ‘flu’ proteins to better understand their role in the virus life cycle and to identify potential therapeutic targets. More recently, we have begun to study the structure and function of chaperone proteins, especially J-domain proteins, to understand how they interact with misfolded/unfolded clients and with the HSP70 machinery.
A central technique of our laboratory is solution nuclear magnetic resonance (NMR) spectroscopy, which allows atomic-level studies of protein structures and their interactions. NMR can be uniquely informative in situations where the molecular conformations or interactions are dynamic or heterogeneous. However, we also use a wide variety of other biochemical and biophysical tools to support our investigations. We also have collaborations with various research groups around the world including virologists, cell biologists, and computational biologists.