NMR studies of protein structure, function, folding and dynamics
Solution-state nuclear magnetic resonance (NMR) spectroscopy provides atomic-level information on biological macromolecules such as proteins and nucleic acids in their native-like environment. My group uses NMR in diverse ways including determining protein structures in solution, probing backbone dynamics of proteins on a range of timescales, characterising partially-folded molten globule states of proteins, and studying protein-protein interactions. We use NMR spectrometers located in the Department of Biochemistry (Rex Richards Building) which operate at 1H frequencies of 500 to 950 MHz. Our research is highly collaborative and we work closely with other groups in Biochemistry and the Medical Sciences Division to apply NMR spectroscopy to a range of interesting biological problems. Recent projects have focussed on: 1) understanding the specificity and reactivity of the bacterial transmembrane oxidoreductase DsbD, 2) studying the structure and dynamics EGF-like domains in proteins including fibrillin-1, LTBP and Notch-1, 3) using NMR to study the structure, dynamics and interactions of proteins involved in bacterial chemotaxis, 4) characterising the determinants of the structure and stability of the molten globule states of proteins including α-lactalbumin.