Research Network for Metals in Medicine

 

 

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

Postal Address:
The Russell Grimwade School
of Biochemistry and Molecular Biology
The University of Melbourne
Melbourne, Vic 3010
AUSTRALIA

Phone: +61 (03) 8344 5935
Email: prg@unimelb.edu.au
Webpage: http://grimwade.biochem.unimelb.edu.au/bch/research/pgooley_rp.htm


Research Profile

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.


Selected Publications

  1. Swarbrick, J. D., Bashtannyk, T., Maksel, D., Zhang, X.-R., Blackburn, G. M., Gayler, K. R. & Gooley, P. R. “The Three-Dimensional Structure of the Nudix Enzyme Diadenosine Tetraphosphate Hydrolase from Lupinus angustifolius L.” J. Mol. Biol. (2000), in press.
  2. Swarbrick, J. D., Bashtannyk, T., Maksel, D., Pau, R. N., Gayler, K. R. & Gooley, P. R. “Letter to the Editor: 1H, 13C, and 15N backbone assignment and secondary structure of the 19 kDa diadenosine 5’ 5’’’-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L.” J. Biomolecular NMR (2000) 16, 269-270.
  3. Gooley, P.R., Keniry, M.A., Dimitrov, R., Marsh, D.E., Keizer, D.W., Gayler, K.R. & Grant, B.R. “The NMR solution structure and characterization of pH dependent chemical shifts of the b-elicitin, cryptogein” Journal of Biomolecular NMR (1998) 12, 523-534.
  4. Gooley, P.R., O’Connell, J.F., Marcy, A.I., Cuca, G.C., Hagmann, W.K., Caldwell, C.G., Axel, M.G. & Becker, J.W. “Comparison of the Structure of Human Recombinant Short Form Stromelysin by Multidimensional Heteronuclear NMR and X-ray Crystallography.” Journal of Biomolecular NMR (1996) 7, 8-28.
  5. Gooley, P.R., O’Connell, J.F., Marcy, A.I., Cuca, G.C., Salowe, S.P., Bush, B.L., Hermes, J.D., Hagmann, W.K., Esser, C.K. & Springer, J.P. & Johnson, B.A. “The NMR Structure of the Inhibited Catalytic Domain of Human Stromelysin-1” Nature Structural Biology (1994) 1, 111-118.

Facilities

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.