• Molecular chaperones (small heat-shock, casein, and 14-3-3 proteins)
• Protein unfolding 
• Amorphous and amyloid fibril protein aggregation
• Inhibition of protein aggregation
• Diseases of protein aggregation (cataract, Parkinson's, Alzheimer's, etc.)
• Protein NMR spectroscopy

John Carver undertook his undergraduate (Honours) degree in Chemistry at the University of Adelaide. In 1983, he was awarded his Ph.D. in Biological Chemistry from the Australian National University and subsequently undertook post-doctoral studies in Biochemistry at the Universities of Oxford and Adelaide. In 1988, John took up a position as Lecturer in Chemistry at the University of Wollongong where he subsequently became an Associate Professor. In early 2004, he returned to the University of Adelaide as Professor of Chemistry and Head of the School of Chemistry & Physics. In 2008, he became the Deputy Executive Dean of the Faculty of Sciences and, for all of 2009, he was also Head of the School of Molecular and Biomedical Science. From July 2013 to February 2019, John was Director of the Research School of Chemistry at the Australian National University. After this until the end of 2020, he was a Professor of Chemistry. Since January 2021, he has been an Emeritus Professor in the Research School of Chemistry.

Our general area of research activity is in protein structure, function, and interactions.

We use a variety of spectroscopic, biophysical, and protein chemical techniques to study molecular chaperone proteins and their mechanism of stabilising other proteins, for example those involved in diseases of protein aggregation (Alzheimer’s, Parkinson’s, cataract etc.). NMR spectroscopy is one of the techniques used to characterise these interactions.