Our major research programme concerns the folding, stability and activity of proteins. We apply a broad multi-disciplinary approach that combines methods and ideas of molecular biology and physical-organic chemistry. We use techniques including protein engineering, DNA cloning, sequencing and mutagenesis, cell culture, gene and peptide synthesis, spectroscopy, rapid reaction techniques, multi-dimensional NMR (we have a 500, 600, 700 and an 800 MHz spectrometers) and x-ray protein crystallography.
Current major projects include: protein folding, misfolding and disease; drug discovery; and structure-activity relationships of proteins involved in cancer and disease.
Although now emeritus, I am still fully active in research with long term funding, including an MRC Programme Grant.
A transient and low populated protein folding intermediate at atomic resolution D. M. Korzhnev, T. L. Religa, W. Banachewicz, A. R. Fersht, Lewis E. Kay Science, 329, 1312-6 (2010).
Towards the Rational Design of p53 Stabilizing Drugs: Probing the Surface of the Oncogenic Y220C Mutant N. Basse, J. L. Kaar, G. Settanni, A. C. Joerger, T. J. Rutherford and A. R. Fersht Chem. Biol. 17, 46-56 (2010)
Mapping the physical and functional interactions between the tumour suppressors p53 and BRCA2 S. Rajagopalan, A, Andreeva, T. J. Rutherford and A. R. Fersht Proc Natl. Acad Sci. USA 107, 8587-8592 (2010).
Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer F. Huang, S. Rajagopalan, G. Settanni, R. J. Marsh, D. A. Armoogum, N. Nicolaou, A. J. Bain, E, Lerner, E. Haas L. Ying and A. R. Fersht Proc Natl. Acad Sci. USA 106, 20758-63 (2009).
Targeted rescue of a destabilized mutant of p53 by an in-silico screened drug F. M. Boeckler, A. C. Joerger, G. Jaggi, T. J. Rutherford, D. B. Veprintsev and A. R. Fersht Proc Natl. Acad Sci. USA. 105, 10360-5 (2008).