Matthew Crump
Professor
Department of Chemistry
University of Bristol
United Kingdom
Biography
He completed his BSc (Hons) and PhD in Chemistry at the University of Bristol. His PhD (1995) was supervised by Professor Tom Simpson where He completed the first NMR structure of a protein (actinorhodin ACP) using 500 and 600 MHz homonuclear NNR spectra (never ever again). Actually He did then go on to this again at the University of Alberta, Canada where He completed post-doctoral studies with Professor brian Sykes. During His three years in Canada we solved numerous NMR structures of chemokines, coiled coils, peptides and bacterial surface proteins. In 1999 He established a 600 MHz biological NMR centre in the School of Biological Sciences in Southampton followed by a new biological NMR centre at Bristol in 2003. This facility has grown to encompass two 600 MHz spectrometers as well as associated low field spectrometers as part of the chemistry NMR facility (under Dr Craig Butts). His group works on a range of structural biology problems and to date has deposited over 30 novel protein structures.
Research Interest
His group's work has centred around the use of nuclear magnetic resonance spectroscopy to study protein structure and function. The most high profile of these are based in areas such as cancer, antibiotics and structure aided drug design that are of central importance to the well being of today's society. A major highlight of our recent work has been the solution NMR structure of the domain 11 from the Insulin Growth.
Publications
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Dong, X, Bailey, C, Williams, C, Crosby, J, Simpson, T, Willis, C & Crump, M, 2016, ‘Recognition of extended linear and cyclised polyketide mimics by a Type II acyl carrier protein’. Chemical Science, vol 7., pp. 1779-1785
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Shoemark, DK, Williams, C, Fahey, MS, Watson, JJ, Tyler, SJ, Scoltock, SJ, Ellis, R, Wickendon, E, Burton, AJ, Hemmings, JLL, Bailey, CD, Dawbarn, D, Jane, DE, Willis, CL, Sessions, RB, Allen, SJ & Crump, MP, 2015, ‘Design and nuclear magnetic resonance (NMR) structure determination of the second extracellular immunoglobulin tyrosine kinase A (TrkAIg2) domain construct for binding site elucidation in drug discovery’. Journal of Medicinal Chemistry, vol 58., pp. 767-777
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Carter, T, Mooibroek, T, Stewart, P, Crump, M, Galan, C & Davis, A, 2016, ‘Platform Synthetic Lectins for Divalent Carbohydrate Recognition in Water’. Angewandte Chemie International Edition, vol 55., pp. 9311?9315
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Frago, S, Nicholls, R, Strickland, M, Hughes, J, Williams, C, Garner, L, Surakhy, M, Maclean, R, Rezgui, DAR, Prince, S, Zaccheo, O, Ebner, D, Sanegre, S, Yu, S, Buffa, FM, Crump, M & Hassan, AB, 2016, ‘Functional evolution of IGF2:IGF2R domain 11 binding generates novel structural interactions and a specific IGF2 antagonist’. Proceedings of the National Academy of Sciences, vol 113., pp. E2765-E2775
