Michael Parker is an Associate Director of St Vincent's Institute of Medical Research in Melbourne where he is Head of the Biota Structural Biology Laboratory. He is a Senior Principal Research Fellow of the National Health and Medical Research Council and is a Professorial Fellow of Melbourne University. After obtaining his PhD in protein crystallography from Oxford University, Michael took up the post of staff scientist at the European Molecular Biology Laboratory in Germany. Whilst at EMBL he solved the first 3D atomic structure of a pore-forming protein toxin which provided a molecular understanding of how water-soluble proteins pass through biological membranes. This, and subsequent work on pore-forming toxins in Australia, has proven to be a seminal contribution to understanding this fundamental process in biology.
In 1991 Michael returned to Australia as a Wellcome Trust Senior Research Fellow to re-establish a protein crystallography laboratory at St Vincent's. The work of the laboratory is internationally recognised with the determination of more than fifty crystal structures including those of membrane-associating proteins, detoxifying enzymes and protein kinases. This work has provided insights into a number of diseases such as cancer, bacterial and viral infections, allergy and Alzheimer's disease. Recent highlights include the determination of the atomic structures of the ubiquitin ligase Siah, the pore-forming toxins gamma-hemolysin and intermedilysin, a fragment of AMP kinase, apo human growth hormone receptor, the copper-binding domain of amyloid precursor protein, a chloride intracellular channel and a hormone-bound antibody complex. Some of this work has been recognised with the awards to Michael of the 1994 Selwyn-Smith Medical Research Prize by the University of Melbourne, the 1996 Boehringer-Mannheim Medal of ASBMB, the 1999 Gottschalk Medal of the Australian Academy of Science and the Royal Society of New South Wales Walter Burfitt Prize in 2002.
The recent redevelopment of the Institute building has enabled an expansion of Michael's laboratory with new technologies including structure-based drug design (virtual screening), electrophysiology and cell-free expression. Michael continues his interest in membrane protein structure with the aims of understanding how biological signals are transmitted across biological membranes with the ultimate aim of developing new therapeutics, particularly against neurological diseases such as Alzheimer's disease and epilepsy, using structure-based drug design technology.