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

Protein folding transition states: Elicitation of Hammond effects by 2,2,2-trifluoroethanol
CP Yiu, MG Mateu, AR Fersht
ChemBioChem
(2000)
1
Stabilization of GroEL minichaperones by core and surface mutations
Q Wang, AM Buckle, AR Fersht
Journal of Molecular Biology
(2000)
298
Fast-folding proteins.
AR Fersht
ABSTR PAP AM CHEM S
(2000)
219
Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding 1 1Edited by B. Honig
KB Wong, J Clarke, CJ Bond, JL Neira, SM Freund, AR Fersht, V Daggett
Journal of Molecular Biology
(2000)
296
Characterization of in vitro oxidized barstar.
C Frisch, G Schreiber, AR Fersht
FEBS Letters
(2000)
370
Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy.
AN Bullock, J Henckel, AR Fersht
Oncogene
(2000)
19
Untitled
JM Lehn, AR Fersht
EUR J INORG CHEM
(2000)
Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase.
M Ibba, CM Johnson, H Hennecke, AR Fersht
FEBS letters
(2000)
358
Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.
AR Fersht
Proceedings of the National Academy of Sciences
(2000)
97
Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.
MM Altamirano, JM Blackburn, C Aguayo, AR Fersht
Nature
(2000)
403