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

Measurement of barnase refolding rate constants under denaturing conditions.
JM Sanz, AR Fersht
FEBS Lett
(2001)
344
Hydrolysis of small peptide substrates parallels binding of chymotrypsin inhibitor 2 for mutants of subtilisin BPN'
J Eder, M Rheinnecker, AR Fersht
FEBS letters
(2001)
335
Protein folding and stability: the pathway of folding of barnase
AR Fersht
FEBS Letters
(2001)
325
Modification of the amino acid specificity of tyrosyl‐tRNA synthetase by protein engineering
G de Prat Gay, HW Duckworth, AR Fersht
FEBS Letters
(2001)
318
Ultrafast folding of WW domains without structured aromatic clusters in the denatured state
N Ferguson, CM Johnson, M Macias, H Oschkinat, A Fersht
Proceedings of the National Academy of Sciences
(2001)
98
Using flexible loop mimetics to extend Φ-value analysis to secondary structure interactions
N Ferguson, JR Pires, F Toepert, CM Johnson, YP Pan, R Volkmer-Engert, J Schneider-Mergener, V Daggett, H Oschkinat, A Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2001)
98
Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen‐deuterium exchange
DN Jones, M Bycroft, MJ Lubienski, AR Fersht
FEBS Letters
(2001)
331
The catalytic activity of the inactive conformation of delta-chymotrypsin.
AR Fersht
FEBS letters
(2001)
29
Stability and solvation of Thr/Ser to Ala and Gly mutations at the N‐cap of α‐helices
YW Chen, AR Fersht
FEBS Lett
(2001)
347
Rescuing the function of mutant p53
AN Bullock, AR Fersht
Nature reviews. Cancer
(2001)
1