Research outline - Macromolecular Structure Laboratory

Within: Bosch Institute, Discipline of Pathology

On this page:

Overview of research program

The research programme in this laboratory has two strands:

  1. Determination of the molecular structure and function of proteins, focusing primarily on contractile proteins. Dynamic structural changes within proteins are investigated using the spectroscopic techniques of fluorescence, circular dichroic and electron paramagnetic resonance (EPR) spectroscopy. This laboratory collaborates on projects to determine the structure of proteins at atomic resolution using both X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. Molecular biology techniques are used to genetically engineer and express muscle proteins we are interested in, to enable new spectroscopic probe sites to be incorporated into relevant proteins and to facilitate NMR and crystallographic studies.
  2. Understanding cardiovascular disease at a molecular and cellular level. Protein biochemical and structural techniques are applied to understanding the protein defects that occur in disease processes such as familial hypertrophic cardiomyopathy and cardiac ischaemia. Additionally, this laboratory has developed tissue culture and other experimental models of atherosclerosis, which are used to examine molecular and cellular changes during atherosgensis. Commercial applications of our discoveries in cardiac ischaemia and atherosclerosis are being exploited.

Major funding sources

A temporal profile of signalling via phosphorylation during myocardial ischemia / reperfusion injury
NHMRC Project Grants $355,050 over 3 years

Selected publications

  • Wu, H., Craft, M., Wang, P., Wyburn, K., Chen, G., Ma, J., Hambly, B., Chadban, S. IL-18 Contributes to Renal Damage after Ischemia-Reperfusion. Journal of the American Society of Nephrology : JASN. 2008; 19:2331-41.
  • Ko, H., Hambly, B., Eris, J., Levidiotis, V., Wyburn, K., Wu, H., Chadban, S., Yin, J. Dentritic cell derived IL-18 production is inhibited by rapamycin and sanglifehrin A, but not cyclosporine A. Transplant immunology. 2008; 20:99-105.
  • Hambly, B., Oakley, C., Fajer, P. Protein Comparative Sequence Analysis and Computer Modeling. In: Clinical Bioinformatics. New Jersey, USA: Humana Press Inc. 2008. p. 245-256.
  • Hambly, B., Oakley, C., Fajer, P. Protein comparative sequence analysis and computer modeling. Methods in molecular medicine. 2008; 141:245-256.
  • Tavakoli, N., Hambly, B., Sullivan, D., Bao, S. Forkhead box protein 3: Essential immune regulatory role. The international journal of biochemistry & cell biology. 2008; 40:2369-73.
  • Stefani, M., Tsubakihara, M., Allen, P., Macdonald, P., dos Remedios, C. Actin and its binding proteins in heart failure. In: Actin-binding proteins and disease. United Kingdom: Springer 2008. p. 318-334.

Major collaborations

  • China. (Department of Plastic Surgery, Shanghai Third People’s Hospital, School of Medicine, Shanghai Jiaotong University) Collaborative research with Prof Yong Fang.The project addresses immunological mechanisms in atherosclerosis and wound healing.
  • United States. (Florida State University) Adjunct Assoc Professor, Biology (Molec Biophysics), Florida State Univ, Tallahassee. Collaborative research with Profs Peter Fajer and Tim Logan. The project addresses heart muscle structural biology questions.