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

Assignment of histidine resonances in the 1H NMR (500 MHz) spectrum of subtilisin BPN' using site-directed mutagenesis.
M Bycroft, AR Fersht
Biochemistry
(2002)
27
Energetics of complementary side-chain packing in a protein hydrophobic core.
JT Kellis, K Nyberg, AR Fersht
Biochemistry
(2002)
28
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
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
SE Jackson, AR Fersht
Biochemistry
(2002)
30
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
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
Barnase has subsites that give rise to large rate enhancements.
AG Day, D Parsonage, S Ebel, T Brown, AR Fersht
Biochemistry
(2002)
31
Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxyribonucleic acid derivative
MS Silver, AR Fersht
Biochemistry
(2002)
22
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism
AR Fersht, JW Knill-Jones, H Bedouelle, G Winter
Biochemistry
(2002)
27
SUBSITE BINDING IN AN RNASE - STRUCTURE OF A BARNASE TETRANUCLEOTIDE COMPLEX AT 1.76-ANGSTROM RESOLUTION
AM Buckle, AR Fersht
Biochemistry
(2002)
33