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

Initiation sites of protein folding by NMR analysis.
SM Freund, KB Wong, AR Fersht
Proceedings of the National Academy of Sciences
(1996)
93
Mechanism of the molecular chaperone GroEL.
AR Fersht
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1996)
212
Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity.
R Zahn, S Perrett, AR Fersht
J Mol Biol
(1996)
261
An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway.
J Clarke, AR Fersht
Folding and Design
(1996)
1
Kinetic significance of GroEL(14)center dot(GroES(7))(2) complexes in molecular chaperone activity
FJ Corrales, AR Fersht
Folding and Design
(1996)
1
Mechanism of the molecular chaperone GroEL.
AR Fersht
BIOCHEMISTRY
(1996)
35
Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.
KB Wong, SM Freund, AR Fersht
Journal of molecular biology
(1996)
259
An NMR study on the beta-hairpin region of barnase.
JL Neira, AR Fersht
Folding and Design
(1996)
1
Towards the complete structural characterization of a protein folding pathway: The structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor .2. Direct evidence for a nucleation-condensation mechanism
JL Neira, B Davis, AG Ladurner, AM Buckle, GDP Gay, AR Fersht
Fold Des
(1996)
1
A new approach to the study of transient protein conformations: The formation of a semiburied salt link in the folding pathway of barnase
M Oliveberg, AR Fersht
Biochemistry
(1996)
35