The School has a long and successful tradition of research in the development and application of biophysical methods, including Magnetic Circular Dichroism, EPR, direct voltammetric methods, NMR and protein X-ray crystallography, to solve problems of protein structure and functions.
Research is currently led by the following members of Faculty:
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Prof Peter Belton
- Use of cereal proteins to make biodegradable plastics and as drug delivery systems.
- Applications of spectroscopy and other physical characterisation to food and drug delivery systems
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Dr Tharin Blumenschein
- Nuclear magnetic resonance of proteins
- Protein dynamics, interactions, and function
- Intrinsically disordered proteins
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Prof Julea N Butt
- voltammetric and spectroelectrochemical studies of redox-active metalloproteins.
- enzymes of anaerobic microbial respiration that participate in the nitrogen, sulphur and iron cycles.
- developing strategies to study Q/QH2 oxidoreductases in electrode supported bilayers.
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Dr Myles Cheesman
- EPR (electron paramagnetic resonance) and MCD (magnetic circular dichroism) spectroscopy of transition-metal centres in proteins.
- Multi-heme enzymes involved in bacterial denitrification.
- MOTTLE (MCD monitored optically transparent thin layer electrodes)
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Dr Andrew M Hemmings
- X-ray structural and mechanistic studies of enzymes
- Metal-protein recognition and the mechanisms of metal homeostasis in bacteria
- Bioinformatics & protein structure prediction, particularly of cofactor-rich proteins
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Dr Nick E Le Brun
- metal ion trafficking and storage in bacterial cells
- Iron-sulfur- and heme-binding transcriptional regulators
- thioredoxin-like proteins involved in disulfide bond management
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Dr Fraser MacMillan
- Application and development of EPR (ESR) including multi-frequency, pulsed and double resonance techniques
- Structure/function/dynamics relationships in biomacromolecules, especially in membrane and metallo-proteins
- Protein - ligand interactions, electron transfer and biological transport processes
- Spin Labelling, EPR and distance measurements
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Prof Geoffrey R Moore
- Natively unfolded proteins
- Intermolecular interactions involving proteins
- Biomolecular NMR spectroscopy
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Dr Vasily Oganesyan
- Theoretical and Computational methods for advanced spectroscopy
- Electronic structure calculations
- Molecular Dynamics simulations
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Prof Chris Pickett
- Artificial Hydrogenases
- Photoelectrocatalytic devices for hydrogen generation, carbon dioxide fixation and alkane functionalisation
- Electropolymer materials
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Prof Andrew J Thomson
- Iron sulfur clusters as regulators of bacterial genes in response to environmental factors such as redox stress, oxygen and nitric oxide
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