Professor Christina Redfield's research involves the application of state-of-the-art nuclear magnetic resonance (NMR) spectroscopy methods to study the structure, function, dynamics and folding of proteins. NMR is unique in being able to provide detailed information at the residue-specific level for proteins in solution.
Some of the current projects in Redfield's research group include: (1) Studies of the partially-folded molten globule state of alpha-lactalbumin. Characterisation of this state provides insights into the intermediates formed during protein folding. (2) NMR is being used to study the active-site properties and interactions of the redox protein DsbD, which is essential for disulfide bond formation and isomerisation and for cytochrome c maturation systems in bacteria. The Department of Biochemistry has a world-class NMR facility with spectrometers operating at 500, 600, 750 and 950 MHz.