- Platform Technologies
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: the relaxin family of receptors which are GPCRs, their interactions with their respective hormones and their curious mechaisms of activatio; the specificity and affinity for oligosaccharides by the carbohydrate binding modules, and their signficance in regulation of the enzyme AMP protein activated kinas, protein import receptors of mitochondria and how they bind and pass preproteins through the membrane; apolipoprotein CII in the amyloid state from lipid and lipid free environments. They are also interested in applying NMR methods to metabolomics, focused on the role and impact of the gut microflora in health and in syndromes such as chronic fatigue. In addition they are interested in studying the effect of prebiotics, probiotics on the exometabolome of the microbiota.
Techniques in the lab include: NMR spectroscopy (proteins, ligand interactions, dynamics, small metabolites), Isothermal Titration Calorimetry (ligand binding); Mass Spectrometry (hydrogen deuterium exchange of proteins and protein complexes), Fluorescence (ligand binding), protein expression (bacterial and cell free) and protein purification.
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).