About the Project
Very recently, the Dodson laboratory has developed a single molecule fluorescence assay that is capable of monitoring kinase interconversion in solution for the first time. This has enabled us to show that phosphorylated kinase is dynamic in solution and to determine new information about the way in which kinase inhibitors bind to their targets [1,2]. Our assay also opens the door to directly testing hypotheses about which kinase residues drive conformational change.
The successful candidate for this PhD will investigate the role of a highly conserved triplet of amino acids (the DFG motif) in the dynamics of a regulatory region known as the kinase activation loop. She/he will use our technology to determine the factors which control the rate of conformational interconversion and the role of dynamics in kinase catalysis.
This project is highly interdisciplinary and is part of a growing interest in conformational change in drug-target interactions. It is suitable for candidates with either a biological or physical science background.
2. Gilburt, J. A. H. et al. (2019). Chem Sci 10(14), 4069-4076
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