My research employs a combined theoretical and experimental approach to understand membrane protein dynamics.

On the experimental side, we use and develop a time-resolved wide-angle X-ray scattering (TR-WAXS) technique to monitor membrane protein conformational dynamics in solution at high temporal resolution.

We also use molecular dynamics (MD) simulations to model the experimental data and to visualise phenomena that are very hard, if not impossible, to address with existing experimental techniques, such as partitioning in the membrane interface and dynamic patterns in protein salt-bridge/H-bind interactions. Moreover, water and side chain dynamics also add to our understanding of membrane protein function. Any prediction from the simulations should be anchored in experimental results. So in addition to the scattering techniques, we also use functional characterisation techniques that target protein activity to assay mutational phenotypes.

Selected research topics

Refinement methods for time-resolved X-ray scattering methods exemplified by work on archaeal rhodopsins by Andersson et al. 2009

Simulated release mechanisms of (a) a Cu+ transporting P-type ATPase (CopA) and accompanying potential of mean force (PMF) profile of ion release and (b) a Zn2+ transporting P-type ATPase (ZntA) and accompanying protein-ion interaction statistics.

Snapshot from a simulation monitoring proton-coupled dynamics in LacY (Andersson et al. 2012)