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

Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis
AR Fersht
Biochemistry
(2002)
27
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
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 three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy
M Bycroft, S Ludvigsen, AR Fersht, FM Poulsen
Biochemistry
(2002)
30
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
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
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
Engineering a novel specificity in subtilisin BPN'
M Rheinnecker, G Baker, J Eder, AR Fersht
Biochemistry
(2002)
32