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

Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering.
G Schreiber, AR Fersht
Biochemistry
(2002)
32
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism.
AR Fersht, JW Knill-Jones, H Bedouelle, G Winter
Biochemistry
(2002)
27
Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis.
SE Jackson, N elMasry, AR Fersht
Biochemistry
(2002)
32
DETERMINATION OF THE 3-DIMENSIONAL SOLUTION STRUCTURE OF BARNASE USING NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
M Bycroft, S Ludvigsen, AR Fersht, FM Poulsen
Biochemistry
(2002)
30
Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation.
J Clarke, AR Fersht
Biochemistry
(2002)
32
Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding.
SE Jackson, AR Fersht
Biochemistry
(2002)
30
Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR
EM Meiering, M Bycroft, AR Fersht
Biochemistry
(2002)
30
Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability.
J Sancho, L Serrano, AR Fersht
Biochemistry
(2002)
31
Role of phenylalanine-327 in the closure of loop 6 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum
AG Day, P Chène, AR Fersht
Biochemistry
(2002)
32
Establishing the misacylation/deacylation of the tRNA pathway for the editing mechanism of prokaryotic and eukaryotic valyl-tRNA synthetases
AR Fersht, C Dingwall
Biochemistry
(2002)
18