Dr Paul Gooley
Position: Senior Lecturer, Department of Biochemistry and Molecular Biology, University of Melbourne
Affiliation: Department of Biochemistry and Molecular Biology, University of Melbourne
Phone: +61 (03) 8344 5935
NMR spectroscopy has developed into a powerful tool for determining the structure and dynamics of small proteins. Developments in triple resonance methods, sample manipulations, spectral analysis tools and assignment strategies have simplified and ensured unambiguous assignment of complex spectra. NMR experiments can provide data for determining structure fold, protein backbone and side chain dynamics, electrostatics and surface topology, and determine changes to both the conformation and dynamics of the protein on complexing with ligands (eg other proteins and protein domains, lipids, enzyme regulators, hormones and drugs). Importantly, simple titrations with physiologically important, but weak binding ligands can show what regions are important and direct protein engineering and inhibitor programs.
A number of projects are underway including structural and dynamic investigations of plant antimicrobial proteins, endosome and golgi trafficking proteins, metalloenzymes that confer bacterial invasiveness and proteins involved in regulation of transcription. All programs can provide experience in molecular biology, protein engineering, protein expression, fermentation, NMR methodology, structure calculation methods, dynamic analyses and computer modeling.
The department is equipped with three spectrometers (400, 500 and 600 MHz), SGI workstations and a network of PC workstations using Linux, a 2 liter fermenter, and several FPLC and Akta chromatography systems for protein purification.