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.

Publications

The FHA domain is a modular phosphopeptide recognition motif
D Durocher, J Henckel, AR Fersht, SP Jackson
Molecular Cell
(1999)
4
Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2.
AG Ladurner, AR Fersht
Nature Structural Biology
(1999)
6
Minimal and optimal mechanisms for GroE-mediated protein folding.
AP Ben-Zvi, J Chatellier, AR Fersht, P Goloubinoff
Proc Natl Acad Sci U S A
(1998)
95
Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability.
PV Nikolova, J Henckel, DP Lane, AR Fersht
Proceedings of the National Academy of Sciences
(1998)
95
Combined Molecular Dynamics and Φ-Value Analysis of Structure−Reactivity Relationships in the Transition State and Unfolding Pathway of Barnase: Structural Basis of Hammond and Anti-Hammond Effects
V Daggett, A Li, AR Fersht
Journal of the American Chemical Society
(1998)
120
In vivo activities of GroEL minichaperones.
J Chatellier, F Hill, PA Lund, AR Fersht
Proceedings of the National Academy of Sciences
(1998)
95
Synergy between simulation and experiment in describing the energy landscape of protein folding.
AG Ladurner, LS Itzhaki, V Daggett, AR Fersht
Proc Natl Acad Sci U S A
(1998)
95
Protein folding: Think globally, (inter)act locally
AR Fersht, EI Shakhnovich
Current biology : CB
(1998)
8
Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar.
M Vijayakumar, KY Wong, G Schreiber, AR Fersht, A Szabo, HX Zhou
J Mol Biol
(1998)
278
Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain.
MG Mateu, AR Fersht
The EMBO journal
(1998)
17