Stop press: Why not read the Imperial News Story on our latest paper?
I am a Research Fellow in the section of Molecular Medicine at the National Heart & Lung Institute at Imperial College. My research lies at the boundary between the biological and physical sciences and I use kinetics, spectroscopy and other biophysical techniques to answer biological questions and to improve human health.
Biophysics and the quantitative measurement of proteins are central to my research. The major project in my lab at the moment investigates the physical behaviour of protein kinases as they are activated and inhibited. I have built a collaborative partnership which includes drug discovery units in both the UK and US. This places us in a good position not only to make new discoveries, but also enables us to feed back these discoveries into kinase inhibitor programmes as quickly and smoothly as possible.
Initially I studied protein folding, completing my PhD under Professor Sir Alan Fersht at the MRC Centre for Protein Engineering in Cambridge. From Cambridge, I moved to the section of Structural Biology at the Institute of Cancer Research in London to work on protein kinases under Professor Richard Bayliss. At ICR I learnt about the drug discovery process, enzyme kinetics, structural biology and current questions in the field of protein kinase regulation. I became fascinated by the information that could be extracted from simple measurements and devised a new kinetic test to determine the mechanism of kinase autophosphorylation using assays routinely used in drug discovery programmes. I also characterised a novel drug-binding kinase conformation (Aurora-A bound to the inhibitor MLN8054), and used kinetic and structural data to propose a new model of kinase activation. A derivative of MLN8054, MLN8237 (alisertib), has now reached Phase III clinical trials.
In preparation for my work at Imperial, I studied physical spectroscopies with Professor Mark Wallace, Professor Peter Hore and Professor Christiane Timmel in the Department of Chemistry at the University of Oxford. This multidisciplinary partnership is researching cryptochrome proteins - thought to be involved in animal navigation - and our work focused on measuring the response of proteins to magnetic fields. While at Oxford, I held a Fulford Junior Research Fellowship at Somerville College.
I welcome enquiries from motivated students interested in joining the laboratory for short projects. Funding deadlines for summer projects are usually in the first few months of the year.
et al., 2017, Dynamic Equilibrium of the Aurora A Kinase Activation Loop Revealed by Single-Molecule Spectroscopy, Angewandte Chemie - International Edition, Vol:56, ISSN:1433-7851, Pages:11409-11414
et al., 2017, Kinetic Analysis Reveals the Identity of Aβ-Metal Complex Responsible for the Initial Aggregation of Aβ in the Synapse., Acs Chem Neurosci, Vol:8, Pages:1970-1979
Dodson CA, 2017, Production of Protein Kinases in E. coli., Methods Mol Biol, Vol:1586, Pages:251-264
et al., 2016, Chemical amplification of magnetic field effects relevant to avian magnetoreception, Nature Chemistry, Vol:8, ISSN:1755-4330, Pages:384-391
et al., 2015, Fluorescence-detected magnetic field effects on radical pair reactions from femtolitre volumes., Chemical Communications, Vol:51, ISSN:1364-548X, Pages:8023-8026
Dodson CA, Bayliss R, 2012, Activation of Aurora-A Kinase by Protein Partner Binding and Phosphorylation Are Independent and Synergistic, Journal of Biological Chemistry, Vol:287, ISSN:0021-9258, Pages:1150-1157
et al., 2013, A Kinetic Test Characterizes Kinase Intramolecular and Intermolecular Autophosphorylation Mechanisms, Science Signaling, Vol:6, ISSN:1945-0877