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

Folding of subtilisin BPN': characterization of a folding intermediate
J Eder, M Rheinnecker, AR Fersht
Biochemistry
(2002)
32
Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions.
AR Fersht, C Dingwall
Biochemistry
(2002)
18
Nature and consequences of GroEL-protein interactions.
LS Itzhaki, DE Otzen, AR Fersht
Biochemistry
(2002)
34
Mutation of lysine 233 to alanine introduces positive cooperativity into tyrosyl-tRNA synthetase.
EA First, AR Fersht
Biochemistry
(2002)
32
Movement of the position of the transition state in protein folding
A Matouschek, DE Otzen, LS Itzhaki, SE Jackson, AR Fersht
Biochemistry
(2002)
34
The valyl-tRNA synthetase from Bacillus stearothermophilus has considerable sequence homology with the isoleucyl-tRNA synthetase from Escherichia coli
TJ Borgford, NJ Brand, TE Gray, AR Fersht
Biochemistry
(2002)
26
Structural factors contributing to the hydrophobic effect: the partly exposed hydrophobic minicore in chymotrypsin inhibitor 2.
DE Otzen, M Rheinnecker, AR Fersht
Biochemistry
(2002)
34
PK(A) VALUES OF CARBOXYL GROUPS IN THE NATIVE AND DENATURED STATES OF BARNASE - THE PK(A) VALUES OF THE DENATURED STATE ARE ON AVERAGE 0.4 UNITS LOWER THAN THOSE OF MODEL COMPOUNDS
M Oliveberg, VL Arcus, AR Fersht
Biochemistry
(2002)
34
An editing mechanism for the methionyl-tRNA synthetase in the selection of amino acids in protein synthesis
AR Fersht, C Dingwall
Biochemistry
(2002)
18
Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.
S Perrett, J Clarke, AM Hounslow, AR Fersht
Biochemistry
(2002)
34