As an undergraduate I read physics at Oriel College, University of Oxford, specialising in biophysics and condensed matter physics in my final year. I graduated from this master’s course in 2011 and immediately started my first year at the Doctoral Training Centre, on the Life Sciences Interface program. When I started my postgraduate course here I switched to Linacre College. After the first year of training at the DTC I started a DPhil studying toxic pore-forming proteins at the single-molecule level, in the group of Mark Wallace in the chemistry department. I am now going into the final year of my DPhil and DTC course. When I'm not studying I play badminton for the university and the county.
8-week MPhys project (Jan 2011): using DNA as a molecular energy transporter - a nanoscale photonic wire, in the group of Achilles Kapanidis
10-week DTC short project (May 2012): designing an optical tweezer set-up to be used in conjunction with a fluorescence microscope, in the group of Mark Leake
10-week DTC short project (July 2012): assembly of toxic pore-forming proteins at the single-molecule level (continued to DPhil), in the group of Mark Wallace
DPhil project (Oct 2012 - present): see below
Single-molecule fluorescence imaging of cholesterol-dependent cytolysin assembly on droplet interface bilayers.
Cholesterol-dependent cytolysins (CDCs) are proteins that form large pores in cholesterol-containing target membranes. They contribute to such infectious diseases as meningitis, pneumonia, listeriosis and tetanus, and are therefore of high importance in the biomedical sciences. CDCs are typically secreted as single molecules but assemble to form large rings of many subunits when bound to a target membrane. Structural and biochemical investigations have supplied a great amount of detail regarding the mechanism and function of these proteins, but a dynamic picture of pore assembly remains elusive. In order to gain further insight into the CDC mechanism, we are using droplet interface bilayers (DIBs) as cell membrane mimics to observe the dynamic assembly of CDCs at the single-molecule level. We label the protein molecules with a fluorescent dye and use total internal reflection fluorescence microscopy to observe their behaviour on DIBs; such information will allow us to discriminate between possible assembly pathways. This work brings together aspects of chemical biology, molecular biology and biophysics, at the interface between the physical and life sciences. Ultimately, this work could be applied in medical research to create more specialised drugs and vaccines, to aid the fight against the associated bacterial diseases.
British Biophysical Society Meeting 2014 (presented poster)