Office: CAP 01.08 Email: g.moore@uea.ac.uk Tel: +44 (0) 1603-592697 School Position: Professor of Chemistry

Geoff Moore obtained a BSc. in Applied Chemistry from the Hatfield Polytechnic (now, University of Hertfordshire), a MSc. in Biochemistry from Imperial College London, and a D.Phil. on structure-function relationships in c-type cytochromes, supervised by Professor R.J.P.Williams F.R.S., from Oxford University. From 1980-1985 he studied in Oxford on a S.E.R.C. Advanced Fellowship and then moved as a Lecturer to UEA in 1986 where he became Professor of Chemistry in 1994.

During his time at Oxford and in the early part of his time at UEA Geoff continued to work on cytochromes and together with Professor Graham Pettigrew (Edinburgh) co-authored two books on cytochromes c. His major research at UEA has been within the Centre of Metalloprotein Spectroscopy and Biology or its off-shoot, the UEA-Wolfson Molecular Structure Centre. In recent years his research has focused on the use of NMR spectroscopy to characterise proteins, and specifically their structure determination, intermolecular interactions and conformational dynamics, and structure-function relationships in protein antibiotics and proteins involved in bacterial iron metabolism.

Geoff joined the UEA Learning, Teaching and Quality Directorate in 2000 and is currently the UEA Director of Taught Programmes with responsibility for undergraduate and taught postgraduate courses.

Selected publications

Protein-template-driven formation of polynuclear iron species. Malone, S.A., Lewin, A., Kilic, M.A., Svistunenko, D.A., Cooper, C.E., Wilson, M.T., Le Brun, N.E., Spiro, S. & Moore, G.R. (2004) J Am Chem Soc. 126, 496-504.  DOI:  10.1021/ja036483z

Clusters in an intrinsically disordered protein create a protein binding site: the TolB binding region of colicin E9. Tozawa, K., Macdonald, C.J., Penfold, C.N., James, R., Kleanthous, C., Clayden, N.J. & Moore, G.R. (2005) Biochemistry 44, 11496-11507.  DOI:  10.1021/bi0503596

Characterisation of the conformational properties of urea-unfolded Im7: implications for the early stages of protein folding. Le Duff, C.S, Whittaker, S.B-M., Radford, S.E. & Moore, G.R. (2006) J. Mol. Biol. in press.  DOI:  10.1016/j.jmb.2006.09.037

NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7. Whittaker, S.B-M., Spence, G.R., Grossmann, J.G., Radford, S.E. & Moore, G.R. (2006) J. Mol. Biol. in press.  DOI:  10.1016/j.jmb.2006.11.012