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

Reaction of modified and unmodified tRNATyr substrates with tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
JM Avis, AG Day, GA Garcia, AR Fersht
Biochemistry
(2002)
32
Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
G Schreiber, AR Fersht
Biochemistry
(2002)
32
Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases
AR Fersht, JS Ashford, CJ Bruton, R Jakes, GL Koch, BS Hartley
Biochemistry
(2002)
14
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
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
The valyl-tRNA synthetase from Bacillus stearothermophilus has considerable sequence homology with the isoleucyl-tRNA synthetase from Escherichia coli
TJ Borgford, NJ Brand, TE Gray, AR Fersht
Biochemistry
(2002)
26
Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains.
S Vuilleumier, J Sancho, R Loewenthal, AR Fersht
Biochemistry
(2002)
32
STRUCTURE AND DYNAMICS OF BARNASE COMPLEXED WITH 3'-GMP STUDIED BY NMR-SPECTROSCOPY
EM Meiering, M Bycroft, MJ Lubienski, AR Fersht
Biochemistry
(2002)
32
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy.
MJ Lubienski, M Bycroft, SM Freund, AR Fersht
Biochemistry
(2002)
33
Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2.
SE Jackson, M Moracci, N elMasry, CM Johnson, AR Fersht
Biochemistry
(2002)
32