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

Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis
JL Neira, LS Itzhaki, DE Otzen, B Davis, AR Fersht
Journal of molecular biology
(1997)
270
The role of Glu73 of barnase in catalysis and the binding of barstar.
G Schreiber, C Frisch, AR Fersht
Journal of molecular biology
(1997)
270
Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
S Perrett, R Zahn, G Stenberg, AR Fersht
Journal of molecular biology
(1997)
269
The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2.
YJ Tan, M Oliveberg, DE Otzen, AR Fersht
J Mol Biol
(1997)
269
Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase.
MM Sánchez del Pino, AR Fersht
Biochemistry
(1997)
36
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
KB Wong, AR Fersht, SM Freund
Journal of Molecular Biology
(1997)
268
Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks11Edited by J. Karn
CM Johnson, M Oliveberg, J Clarke, AR Fersht
Journal of Molecular Biology
(1997)
268
Following co-operative formation of secondary and tertiary structure in a single protein module
JL Neira, LS Itzhaki, AG Ladurner, B Davis, G de Prat Gay, AR Fersht
Journal of molecular biology
(1997)
268
A structural model for GroEL-polypeptide recognition
AM Buckle, R Zahn, AR Fersht
Proc Natl Acad Sci U S A
(1997)
94
Refolding chromatography with immobilized mini-chaperones.
MM Altamirano, R Golbik, R Zahn, AM Buckle, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(1997)
94