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
pKA Values of Carboxyl Groups in the Native and Denatured States of Barnase: The pKA 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 Ftammond Behavior for the Gross Structure of the Transition State and Anti-Hammond Behavior for Structural Elements for Unfolding/Folding of Bamase
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