We have a fundamental interest in protein assembly, and why proteins have evolved to adopt a particular oligomeric form. We test our ideas using a combination of site-directed mutagenesis and biochemical and biophysical techniques.  Much of this work is done in collaboration with collaborators at the University Of Melbourne.
>>Selected Publications

Lysine is an essential amino acid. Inhibitors of the pathways of lysine biosynthesis are of interest as they may be toxic to plants and microorganisms, but not to animals.

Inhibitors of this pathway are potential herbicides and/or bactericides. We are investigating the molecular details of the reaction catalysed by dihydrodipicolinate synthase (DHDPS) and its mode of inhibition by lysine and other molecules, with a view to controlling the reaction and its regulation in vitro and in vivo.

We also collaborate with researchers in the University of Melbourne, designing and testing inhibitors of these enzymes.
>>Selected Publications

An understanding of protein assembly gives valuable insights into biomaterial design and how we might use proteins for bionanotechnological applications.  We are exploring this potential of proteins to form fibrillar aggregates, with particular emphasis being placed on the production of amyloid fibrils from a waste proteins.
This project is carried out in collaboration with Plant and Food and researchers at the University of Adelaide and the University of Melbourne.
>>Selected Publications