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

Nature and consequences of GroEL-protein interactions.
LS Itzhaki, DE Otzen, AR Fersht
Biochemistry
(2002)
34
Movement of the position of the transition state in protein folding.
A Matouschek, DE Otzen, LS Itzhaki, SE Jackson, AR Fersht
Biochemistry
(2002)
34
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
Rationally designing the accumulation of a folding intermediate of barnase by protein engineering
JM Sanz, AR Fersht
Biochemistry
(2002)
32
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
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
Relationship between Equilibrium Amide Proton Exchange Behavior and the Folding Pathway of Barnase
S Perrett, J Clarke, AM Hounslow, AR Fersht
Biochemistry
(2002)
34
Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase.
JM Matthews, AR Fersht
Biochemistry
(2002)
34
Mechanism of aminoacylation of transfer RNA. A pre-steady-state analysis of the reaction pathway catalyzed by the methionyl-tRNA synthetase of Bacillus stearothermophilus.
RS Mulvey, AR Fersht
Biochemistry
(2002)
17