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

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
Quantitative determination of helical propensities from trifluoroethanol titration curves.
A Jasanoff, AR Fersht
Biochemistry
(2002)
33
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
Engineering a novel specificity in subtilisin BPN'
M Rheinnecker, G Baker, J Eder, AR Fersht
Biochemistry
(2002)
32
Folding of subtilisin BPN': characterization of a folding intermediate.
J Eder, M Rheinnecker, AR Fersht
Biochemistry
(2002)
32
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
Nature and consequences of GroEL-protein interactions.
LS Itzhaki, DE Otzen, AR Fersht
Biochemistry
(2002)
34
Movement of the position of the transition state in protein folding.
A Matouschek, DE Otzen, LS Itzhaki, SE Jackson, AR Fersht
Biochemistry
(2002)
34
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