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

SUBUNIT INTERACTIONS IN METHIONYL-TRANSFER-RNA SYNTHETASE OF BACILLUS-STEAROTHERMOPHILUS
RS MULVEY, AR FERSHT
BIOCHEMISTRY-US
(1976)
15
MECHANISM OF AMINOACYLATION OF TRANSFER-RNA - PROOF OF AMINOACYL ADENYLATE PATHWAY FOR ISOLEUCYL-TRANSFER-RNA AND TYROSYL-T-RNA SYNTHETASES FROM ESCHERICHIA-COLI-K12
AR FERSHT, MM KAETHNER
BIOCHEMISTRY
(1976)
15
DEMONSTRATION OF 2 REACTION PATHWAYS FOR AMINOACYLATION OF TRANSFER-RNA - APPLICATION OF PULSED QUENCHED FLOW TECHNIQUE
AR FERSHT, R JAKES
BIOCHEMISTRY-US
(1975)
14
Catalysis, binding and enzyme-substrate complementarity.
AR Fersht
Proceedings of the Royal Society of London. Series B, Biological sciences
(1974)
187
The charge relay system in chymotrypsin and chymotrypsinogen
AR Fersht, J Sperling
J Mol Biol
(1973)
74
Conformational equilibria in α- and δ-chymotrypsin The energetics and importance of the salt bridge
AR Fersht
Journal of molecular biology
(1972)
64
Conformational equilibria in α- and δ-chymotrypsin
AR Fersht
Journal of Molecular Biology
(1972)
64
Conformational Equilibria and the Salt Bridge in Chymotrypsin
AR Fersht
Cold Spring Harb Symp Quant Biol
(1972)
36
Intramolecular catalysis
AJ Kirby, AR Fersht
(1971)
Equilibrium and rate constants for the interconversion of two conformations of α-chymotrypsin The existence of a catalytically inactive conformation at neutral pH
AR Fersht, Y Requena
Journal of molecular biology
(1971)
60