Multiscale Simulations of Biological Membrane Systems

The overall theme of work in the Sansom group is to employ computational techniques to explore the structure and function of membrane proteins and related systems. Membrane proteins play keys role in cell biology e.g. as ion channels, drug receptors, and solute transporters. Indeed, it has been estimated that ~25% of genes code for membrane proteins, and that ca. 50% of potential new drug targets are membrane proteins. In particular the group is interested in ion channels, membrane transport proteins, and bacterial outer membrane proteins.

The group’s research forms a core component of the Structural Bioinformatics and Computational Biochemistry Unit (http://sbcb.bioch.ox.ac.uk). This embraces all areas of computational studies of membrane proteins and related systems, ranging from molecular simulations of channels and transporters, to computational bionanoscience, and membrane protein folding and stability. The group is also interested in multi-level simulations of membrane proteins in the context of addressing the 'gap' between molecular and systems descriptions of membranes.

Dr. Sansom group has major grant support in a number of areas, including ion channel structure/function studies, bacterial outer membrane protein simulations, computational bionanoscience, and e-science methodologies for molecular simulations. In summary, the group aims to:

1. Undertake computational studies of membrane proteins and membrane systems
2. Focus on key aspects of membrane biology: channels, receptors, transporters, and signalling
3. Advance understanding of membrane protein biophysics: structure, stability, and folding
4. Embrace multiple computational approaches: structural bioinformatics, molecular modelling & simulation, computational systems biology, and e-science & HPC
5. Address a range of applications: atomic resolution physiology of excitable cell membranes, computational bionanoscience, and systems biology of membrane transport & signaling

Source: http://www.bioch.ox.ac.uk/aspsite/index.asp?pageid=599