Our group is interested in understanding the behaviour of membrane proteins at the level of individual molecules. By attaching a fluorescent tag to a membrane protein, we are able to see individual molecules. This allows us to observe sub-populations and kinetic intermediates that would be undetectable in an ensemble measurement.
We have also developed new methods to create artificial models of cell membranes. By contacting water droplets with a gel support immersed in a solution of lipid in oil we can create lipid bilayers that mimic the cell membrane.
We use these methods to try and understand study the behaviour of a variety of model membrane proteins.
Using single-molecule imaging we are studying pore-forming bacterial toxins such as alpha-hemolysin. These proteins provide an model of how multisubunit membrane protein complexes assemble.
Using simultaneous single-molecule fluorescence and single-channel electrical recording we can study the mechanism by which ion-channel gating is regulated by ligand binding.
Around one third of all drugs target G-protein Coupled Receptors. We are using single-molecule fluorescence imaging to understand the mechanism of ligand-binding in GPCRs, and how this results in cell signalling.