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Self-assembly is a hallmark of Biology. Our research is aimed at understanding the assembly of biological membranes and their constituent membrane proteins as well as exploiting this to create and control artificial modules for Synthetic Biology.
Integral membrane proteins account for about 30-40% of all cell proteins and function as transporters, receptors and signal transducers. They act as gateways to cells and comprise the vast majority of drug targets. We investigate the folding of these proteins to their functional state in a membrane, and use this knowledge to understand membrane biogenesis and misfolding that occurs in disease states. Moreover, we exploit the ability to self assemble transporters and receptors in Synthetic Biology, by constructing minimal artificial cellular compartments with defined roles that can be adapted for bio-inspired devices. An interdisciplinary approach is used at the interface of Biology and Chemistry to study a range of proteins including G protein coupled receptors, ABC and sugar transporters. Techniques range from cell cultures, protein expression, biochemistry and molecular biology to biophysical, chemical and nanoscience methods.
Webpage: http://www.bris.ac.uk/biochemistry/research/pjb.html
Funding Notes:
This studentship is funded by the ERC.
References:
1. Charalambous K, Booth PJ, Woscholski R, Seddon JM, Templer RH, Law RV, Barter LM, Ces O (2012) Engineering de-novo membrane mediated protein-protein communication networks J Am Chem Soc. 134: 5746-9
2. Curnow, P., Di Bartolo, N.D., Moreton, K.M., Ajoje, O.O., Saggese, N.P. and Booth, P.J. (2011) A stable folding core in the folding transition state of an alpha-helical integral membrane protein. Proc. Natl. Acad. Sci. USA 108:14133-14138
3. Findlay, H. E., Rutherford, N. G., Henderson, P. J. F., and Booth, P. J. (2010) The unfolding free energy of a two-domain transmembrane sugar transport protein Proc Natl Acad Sci U S A 107, 18451-18456
4. Barrera NP, Di Bartolo N, Booth PJ, Robinson CV: Micelles Protect Membrane Complexes from Solution to Vacuum. Science 2008, 321:243-246