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

Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis.
DE Mossakowska, K Nyberg, AR Fersht
Biochemistry
(2002)
28
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
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
Mechanism of chymotrypsin. Structure, reactivity, and nonproductive binding relationships.
J Fastrez, AR Fersht
Biochemistry
(2002)
12
Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis
AR Fersht
Biochemistry
(2002)
27
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
INVESTIGATION OF TRANSITION-STATE STABILIZATION BY RESIDUES HISTIDINE-45 AND THREONINE-40 IN THE TYROSYL-TRANSFER RNA-SYNTHETASE
RJ Leatherbarrow, AR Fersht
Biochemistry
(2002)
26
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis.
AR Fersht
Biochemistry
(2002)
26
Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases.
TJ Borgford, TE Gray, NJ Brand, AR Fersht
Biochemistry
(2002)
26
Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the alpha-ammonium group binding site of tyrosyl-tRNA synthetase.
DM Lowe, G Winter, AR Fersht
Biochemistry
(2002)
26