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NMR spectroscopy is a powerful tool for determining the structure and dynamics of small proteins. Developments in triple resonance methods, sample manipulations, methods of spectral analysis and assignment strategies have simplified, and ensured unambiguous assignment of complex spectra.
NMR experiments can provide data for determining:
- folding within the structure, dynamics of the protein backbone and side chains, electrostatics and surface topology; and
- changes to both the conformation and dynamics of the protein on complexing with ligands such as other proteins and protein domains, lipids, enzyme regulators, hormones and drugs.
The Gooley group is working on a number of projects including:
Structural and dynamic investigations of protein-protein, protein-peptide and protein-lipid interactions including: protein import receptors of mitochondria, apolipoprotein CII in the amyloid state, the relaxin receptor and its homologues, membrane and protein trafficking proteins of Leishmania (FYVE, SMP), carbohydrate binding modules, and insecticide-resistant GST proteins. An additional interest is applying NMR methods to metabolomics.
Techniques in the lab include: NMR spectroscopy as applied to biological problems with access to four NMR spectrometers (400, 500, 600 and 800 MHz) and a network of PC workstations using Linux. Fermentation and standard flask cell culture systems for protein expression and isotopic labelling. Large scale protein purification supported by several FPLC and Akta chromatography systems.
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Paul Gooley Bio
Associate Professor Paul Gooley directs a structural biology research group that focuses on the application of NMR spectroscopy to elucidate structure and protein interactions. He obtained his degrees at the University of New South Wales, and spent 10 years in the USA, including five at the pharmaceutical company Merck and Co. Over the last 10 years his group has conducted and published NMR structural and dynamical analyses on a number of protein domains and systems (5 to 35 kDa) that have biological functions in stress and infection (elicitin, diadenosine tetraphosphate hydrolase), in lipid transport (apolipoprotein CII), in protein and membrane trafficking (FYVE domain, Small Myristoylated Protein (flagellar biogenesis) and Tom20 of the mitochondrial import receptor), and receptor signalling (LDLa module of the relaxin receptor).
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Gooley Research Group
Postgraduate Students
- Mr Kieran Rimmer
- Ms Ann Koay (with David Stapleton)
Honours Students
- Mr Patrick Shilling
- Ms Alicia Ng
- Mr Chris Armstrong (with David Stapleton)
- Mr Shane Emanuelle (with David Stapleton)
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