A 4-year PhD studentship is available, to start from October 2016.
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, with an emphasis on understanding the mechanism of folding through kinetic and thermodynamic studies. We 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 with a focus on membrane transport proteins. Techniques range from cell cultures, protein expression, biochemistry and molecular biology to biophysical, chemical and nanoscience methods.
Only successful candidates will be contacted.
Harris, N.J., Findlay, H.E., Simms, J., Liu, X., Booth, P.J. (2014) Relative domain folding and stability of a membrane transport protein. J. Mol. Biol. 426: 1812-1825
Charalambous K., Booth, P.J., Woscholski, R., Seddon, J.M., Templer, R.H., Law, R.V., Barter, L.M. and Ces, O. (2012) Engineering de-novo membrane mediated protein-protein communication networks J Am Chem Soc. 134, 5746-5749.
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.
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
Research Programme Start date : 1st October 2016
4 Year Programme with RCUK Rates for Stipend (£16,142 p/a) and Fees included - UK/EU applicants only.
Check the general KCL entry requirements and other information about applying:
Candidates should apply for a PhD in the usual way through King’s myApplication system, https://apply.kcl.ac.uk/
Please ensure that you quote the project title and supervisor on the application form and the following reference 16-CHEM-01
Informal inquiries about this position can be addressed directly to Professor Paula Booth [email protected]
Any questions regards to the application process or online application system should be directed to : Admissions team +44 (0) 20 7848 7000