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

Energetics of complementary side-chain packing in a protein hydrophobic core.
JT Kellis, K Nyberg, AR Fersht
Biochemistry
(2002)
28
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 proton NMR (500 MHz) spectrum of subtilisin BPN' using site-directed mutagenesis
M Bycroft, AR Fersht
Biochemistry
(2002)
27
Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin
J Fastrez, AR Fersht
Biochemistry
(2002)
12
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
Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis.
AR Fersht
Biochemistry
(2002)
27
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
Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions
AR Fersht, C Dingwall
Biochemistry
(2002)
18
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