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

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
The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase.
AR Fersht
FEBS Letters
(2001)
325
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 of the United States of America
(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
Proc Natl Acad Sci U S A
(2001)
98
Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar
MJ Lubienski, M Bycroft, DN Jones, AR Fersht
FEBS Letters
(2001)
332
The catalytic activity of the inactive conformation of δ‐chymotrypsin
AR Fersht
FEBS letters
(2001)
29
Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of alpha-helices.
YW Chen, AR Fersht
FEBS letters
(2001)
347
Rescuing the function of mutant p53
AN Bullock, AR Fersht
Nature Reviews Cancer
(2001)
1