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
Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases
AR Fersht, JS Shindler, WC Tsui
Biochemistry
(2002)
19
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
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
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
Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases.
AR Fersht, C Dingwall
Biochemistry
(2002)
18