Home /
People /
Chemistry /
Frances Separovic

Frances Separovic

The Separovic laboratory is studying the structure-function relationships of macro-molecular assemblies and biological systems at the molecular level using primarily nuclear magnetic resonance spectroscopy (NMR).

Our primary research interest is the determination of the structure and dynamics of the components of biological membranes in situ using solid-state NMR techniques. We have determined the molecular structure of the antibiotic gramicidin A and the bee toxin melittin within phospholipid membranes, and the techniques used to study these polypeptides are being extended to other integral membrane proteins. Together with our collaborators, we are providing insight into the biophysical chemistry and structure-function relationships of membrane-active peptides and proteins relevant to disease states and treatments. Projects include studies of membrane-active peptides, toxins, amyloid Aβ, antibiotics and ionic liquids.

Techniques and specialities in the lab include: Biophysical chemistry and NMR of model membrane systems, including powder samples, hydrated dispersions and aligned samples; both static and magic angle spinning (MAS) solid-state NMR techniques.

Frances Separovic Bio

Professor Frances Separovic is a Biophysical Chemist who specializes in NMR spectroscopy. After 23 years working at CSIRO, including a year at National Institutes of Health (USA), Frances joined the University of Melbourne in 1996. She has developed solid-state NMR techniques to determine the structure and dynamics of membrane components in situ, specializing in peptide antibiotics and toxins within phospholipid membranes. Frances was President of the Australian Society for Biophysics (1999-2001) and Director of Australian New Zealand Magnetic Resonance Society (1996-2000). She has successfully organized over 25 national or international scientific conferences and published more than 130 refereed papers in international journals.