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I first developed an interest in structural molecular biology during my undergraduate degree at the University of Sheffield. To pursue this interest, I studied for a PhD in X-ray crystallography at the Astbury Centre for Structural Molecular Biology, University of Leeds under the supervision of Prof. Simon Phillips. I then worked as a postdoctoral research fellow under the supervision of Prof. Steve Homans and Prof. Steve Baldwin. By studying how a range of small molecules bind to the hydrophobic pocket of a small protein, we were able to demonstrate that hydrophobic ligand-protein interactions can be enthalpy driven with a significant contribution from London dispersion forces.
In 2006, I started a postdoctoral position at the University of York work under the supervision of Prof. Jennifer Potts on fibronectin-binding proteins from pathogenic bacteria, elucidating mechanisms of the beta-zipper interaction.
I joined the Department of Biological Sciences at the University of Huddersfield in September 2008.
My current research interests are directed at the causative agent of Lyme Disease- Borrelia burgdorferi. The main projects are:
I teach on the following modules: Structural and Functional Genomics, Applied Molecular Genetics, Biochemistry 2, Physiology 3, Immunology and Infection
My research is based on the pathogenic bacteria Borrelia garinii and Borrelia burgdorferi, both causative agents of Lyme Disease in humans. These spiral shaped (spirochaete) bacteria are obligate parasites with a complex life cycle, alternating between the gut of blood-feeding ticks and mammalian hosts. Borrelia burgdorferi is the predominant cause of Lyme disease in the U.S., while Borrelia garinii is the most common species found in Europe. I aim to further our understanding of these unique organisms at the molecular level. This will shed light on related bacteria of the spirochete phylum and could potentially lead to new therapeutic agents.
Kpodo, F., Agbenorhevi, J., Alba, K., Bingham, R., Oduro, I., Morris, G. and Kontogiorgos, V. (2017) ‘Pectin isolation and characterization from six okra genotypes’ Food Hydrocolloids , 72, pp. 323-330. ISSN 0268-005X
Alba, K., Bingham, R. and Kontogiorgos, V. (2017) ‘Mesoscopic structure of pectin in solution’ Biopolymers . ISSN 0006-3525
Dyer, A., Brown, G., Stejskal, L., Laity, P. and Bingham, R. (2015) ‘The Borrelia afzelii outer membrane protein BAPKO_0422 binds human Factor-H and is predicted to form a membrane-spanning beta-barrel’ Bioscience Reports , 35 (4), p. e00240. ISSN 0144-8463
Akif, M., Masuyer, G., Bingham, R., Sturrock, E., Isaac, R. and Acharya, K. (2012) ‘Structural basis of peptide recognition by the angiotensin-1 converting enzyme homologue AnCE from Drosophila melanogaster.’ The FEBS journal , 279 (24), pp. 4525-4534. ISSN 1742-4658
Gruszka, D., Wojdyla, J., Bingham, R., Turkenburg, J., Manfield, I., Steward, A., Leech, A., Geoghegan, J., Foster, T., Clarke, J. and Potts, J. (2012) ‘Staphylococcal biofilm-forming protein has a contiguous rod-like structure’ Proceeding of the National Academy of Sciences , 109 (17), p. E1011-E1018. ISSN 1091-6490
Norris, N., Bingham, R., Harris, G., Speakman, A., Jones, R., Leech, A., Turkenburg, J. and Potts, J. (2011) ‘Structural and functional analysis of the tandem ?-zipper interaction of a streptococcal protein with human fibronectin’ The Journal of biological chemistry , 286 (44), pp. 38311-38320. ISSN 1083-351X
Atkin, K., Brentnall, A., Harris, G., Bingham, R., Erat, M., Millard, C., Schwarz-Linek, U., Staunton, D., Vakonakis, I., Campbell, I. and Potts, J. (2010) ‘The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.’ The Journal of biological chemistry , 285 (47), pp. 36977-83. ISSN 1083-351X
Bingham, R. and Potts, J. (2010) ‘Fibronectin structure: a new piece of the puzzle emerges’ Structure , 18 (6), pp. 660-661.
Ling, Z., Suits, M., Bingham, R., Bruce, N., Davies, G., Fairbanks, A., Moir, J. and Taylor, E. (2009) ‘The X-ray Crystal Structure of an Arthrobacter protophormiae Endo-?-N-Acetylglucosaminidase Reveals a (?/?)8 Catalytic Domain, Two Ancillary Domains and Active Site Residues Key for Transglycosylation Activity’ Journal of Molecular Biology , 389 (1), pp. 1-9. ISSN 00222836
Bingham, R., Rudino-Pinera, E., Meenan, N., Schwarz-Linek, U., Turkenburg, J., Hook, M., Garman, E. and Potts, J. (2008) ‘Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains’ Proceedings of the National Academy of Sciences , 105 (34), pp. 12254-12258. ISSN 00278424
Barratt, E., Bronowska, A., Vondr��ek, J., ?ern�, J., Bingham, R., Phillips, S. and Homans, S. (2006) ‘Thermodynamic Penalty Arising from Burial of a Ligand Polar Group Within a Hydrophobic Pocket of a Protein Receptor’ Journal of Molecular Biology , 362 (5), pp. 994-1003. ISSN 00222836
Bingham, R., Dive, V., Phillips, S., Shirras, A. and Isaac, R. (2006) ‘Structural diversity of angiotensin-converting enzyme. Insights from structure-activity comparisons of two Drosophila enzymes’ FEBS Journal , 273 (2), pp. 362-373. ISSN 1742-464X
Malham, R., Johnstone, S., Bingham, R., Barratt, E., Phillips, S., Laughton, C. and Homans, S. (2005) ‘Strong Solute?Solute Dispersive Interactions in a Protein?Ligand Complex’ Journal of the American Chemical Society , 127 (48), pp. 17061-17067. ISSN 1520-5126
Barratt, E., Bingham, R., Warner, D., Laughton, C., Phillips, S. and Homans, S. (2005) ‘Van der Waals Interactions Dominate Ligand?Protein Association in a Protein Binding Site Occluded from Solvent Water’ Journal of the American Chemical Society , 127 (33), pp. 11827-11834. ISSN 0002-7863
Thomas, J., Rylett, C., Carham, A., Bland, N., Bingham, R., Shirras, A., Turner, A. and Isaac, R. (2005) ‘Drosophila melanogaster NEP2 is a new soluble member of the neprilysin family of endopeptidases with implications for reproduction and renal function’ Biochemical Journal , 386 (2), pp. 357-366. ISSN 0264-6021
Bingham, R., Findlay, J., Hsieh, S., Kalverda, A., Kjellberg, A., Perazzolo, C., Phillips, S., Seshadri, K., Trinh, C., Turnbull, W., Bodenhausen, G. and Homans, S. (2004) ‘Thermodynamics of Binding of 2-Methoxy-3-isopropylpyrazine and 2-Methoxy-3-isobutylpyrazine to the Major Urinary Protein’ Journal of the American Chemical Society , 126 (6), pp. 1675-1681. ISSN 1520-5126
Lyme disease, the most common vector borne disease in the northern hemisphere, is the result of infection by the spirochete Borrelia burgdorferi. As an obligate parasite, alternating between tick and mammalian vectors, Borrelia have evolved complex strategies to survive extended periods of time in the mammalian host. These strategies initially involve binding to host regulators of the immune response such as Factor H, but then continue to involve invasion of vascular walls crossing the blood brain barrier to establish prolonged infection of nerve tissue.
Current research is focussed on the identification and characterisation of surface proteins responsible for binding to host proteins. We are particularly interested in potential factor H binding proteins from B. garinii, B afzelii and B. burgdorferi.
Research students who have either government sponsorship or scholarships are welcome to apply for PhD positions.