Paul Gooley
NMR spectroscopy: Protein structure and dynamics
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.
Importantly, simple titrations with physiologically relevant, but weak, binding ligands can show what regions are important and direct protein engineering and inhibitor programs.
Projects
- Structural and dynamic investigations of plant antimicrobial proteins
- Endosome and golgi trafficking proteins
- Metalloenzymes that confer bacterial invasiveness
- Proteins involved in regulation of transcription
- molecular biology
- protein engineering
- protein expression
- fermentation
- NMR methodology
- structure calculation methods
- dynamic analyses
- 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 litre fermenter, and several FPLC and Akta chromatography systems for protein purification.
Lab personnel
HeadAssociate Professor Paul GooleyResearch staffDr Michael Bieri (Postdoctoral fellow) Graduate studentsChristopher Armstrong Honours studentsPhillip Dodson |