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

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
Mechanism of the -chymotrypsin-catalyzed hydrolysis of amides. pH dependence of k c and K m . Kinetic detection of an intermediate.
AR Fersht, Y Requena
J Am Chem Soc
(2002)
93
Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis.
AR Fersht
Biochemistry
(2002)
27
Metal ion dependence of phosphorothioate ATP analogues in the Bacillus stearothermophilus tyrosyl-tRNA synthetase reaction.
GA Garcia, RJ Leatherbarrow, F Eckstein, AR Fersht
Biochemistry
(2002)
29
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
Mechanism of aminoacylation of transfer RNA. A pre-steady-state analysis of the reaction pathway catalyzed by the methionyl-tRNA synthetase of Bacillus stearothermophilus.
RS Mulvey, AR Fersht
Biochemistry
(2002)
17
Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesis
FT Lau, AR Fersht
Biochemistry
(2002)
28
Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin.
MF Perutz, AR Fersht, SR Simon, GC Roberts
Biochemistry
(2002)
13
Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and half-of-the-sites reactivity in aminoacylation.
R Jakes, AR Fersht
Biochemistry
(2002)
14
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