Dr Steve Prince (BSc, PhD) - research
Membrane Protein Structural Biology
Up to 30% of the genome of any given organism codes for integral membrane proteins, and over 50% of pharmacological targets are membrane proteins. Recent developments in the use of protein over-expression systems are overcoming the restrictions imposed by membrane protein scarcity. This has opened up structural biology techniques for these sparse proteins. Recombinant technology can therefore be exploited to address membrane protein structure and function, revealing information on important classes of proteins such as Ion Channels, ABC transporters and the Outer Membrane Proteins of pathogenic bacteria.
Membrane proteins are difficult to purify and handle due to their inherent insolubility in aqueous solutions. High-resolution structures of membrane proteins can be obtained if a detergent stabilized protein complex can be crystallized. If crystallization is not possible lower resolution techniques such as Electron Microscopy or Small Angle Scattering can be deployed.
Current projects focus on:
- Prokaryotic Ion channels and ABC transporters (including participation in the Membrane Protein Structure Initiative - a UK wide consortium of eight laboratories investigating the structural details of membrane transport).
- The interaction of scaffold proteins and ion channels in neurons.
- Eukaryotic ABC transporters.
- Proteins from the outer membranes of pathogenic bacteria.
- Neutron crystallography and scattering studies on membrane proteins.