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; basis of molecular recognition; and structure-activity relationships of proteins involved in cancer and disease.
Selected Publications
The solution structure of p53 core domain: structural basis for its instability J. M. P. Cañadillas, H. Tidow, S. M. V. Freund, T. J. Rutherford, H. C. Ang and A. R. Fersht" Proc. Natl. Acad. Sci. USA. 102, 2115-2119 (2006)
Core domain interactions in full length p53 in solution D. B. Veprintsev, S. M.V. Freund, A. Andreeva, S. E. Rutledge, H. Tidow, J. M. P. Cañadillas, C. M. Blair, and A. R. Fersht Proc. Natl. Acad. Sci. USA. 102, 2109-2114 (2006)
Φ-analysis of the folding of the B domain of Protein A using multiple optical probes S. Sato, T. L. Religa, and A. R. Fersht J. Mol. Biol. 360, 850-864 (2006)
A. C. Joerger H-C Ang, D. B. Veprintsev, C. M. Blair, and Alan R. Fersht Structures of p53 Cancer Mutants and Mechanism of Rescue by Second-Site Suppressor Mutations J. Biol. Chem. 280, 8051-8059 (2005)
Solution structure of a protein denatured state/folding intermediate T. L. Religa, J. S. Markson, U. Mayor, S. M. V. Freund and A.R. Fersht Nature 437, 1053-1056 (2005)