Monitoring the conformational changes of proteins
Conformation changes are critical to the function of many proteins yet are difficult characterise at an atomic level because proteins are so small.
Our main interest is in being able to follow the structural changes that take place in gating ion channels, the proteins that regulate electrical signalling in the body. To better understand these structural alterations we are combining experimental methods with simulation in order to characterise protein states that are hard to study by other methods. In particular we use and develop fluorescence methods (FRET) to monitor the changes taking place in different parts of the protein and combine this with molecular simulation to map out the structural changes taking place.
We are particularly interested in the family of bacterial mechanosensitive channels that form safety valves that protect cells from hypo-osmotic shock, opening a wide pore under membrane tension to relieve excessive turgor pressure within the cell.