Personal profile

Biography

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.

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

Key Research Interests

The UEA-Wolfson Molecular Structure Centre

The UEA Molecular Structure Centre was founded in 1996 by researchers from the Schools of Biological and Chemical Sciences to ‘promote the determination and analysis of molecular structures at atomic resolution within the Norwich Research Park’ using solution-state NMR, solid-state NMR and X-ray crystallographic methods. Changes in research programmes at UEA together with changes in experimental methodologies, particularly the increased use of synchrotron X-ray sources in crystallography, led to a change in emphasis of the UEA Molecular Structure Centre, which is now focussed on solution-state NMR. Its name too has changed, to the UEA-Wolfson Molecular Structure Centre in recognition of the generous support of the Wolfson Foundation for the Centre. The aim of the Centre remains the same, however.

The Centre is equipped with Varian 300, 400, 500 and 600 MHz NMR spectrometers. These are equipped between them for inverse-detect 13C/15N NMR, deuterium decoupling for 2H/13C/15N samples, an inverse triple-resonance 8 mm probe for low-solubility samples, and direct-detect probes for 1H and 15N-31P studies. In 2007 an 800 MHz Bruker Avance IIa NMR spectrometer will be installed in the Centre.

Both internal UEA users and external researchers wishing to use the facilities of the Centre should contact either its Director, Prof. Geoff Moore, or the NMR manager, Mr Colin MacDonald.

Areas of Expertise

Relationships between the structures of proteins and their chemical properties and biochemical functions; uptake, storage and mobilisation of iron in biology; protein structure determination by NMR.

Expertise related to UN Sustainable Development Goals

In 2015, UN member states agreed to 17 global Sustainable Development Goals (SDGs) to end poverty, protect the planet and ensure prosperity for all. This person’s work contributes towards the following SDG(s):

  • SDG 3 - Good Health and Well-being

Collaborations and top research areas from the last five years

Recent external collaboration on country/territory level. Dive into details by clicking on the dots or