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

Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements.
DM Lowe, AR Fersht, AJ Wilkinson, P Carter, G Winter
Biochemistry
(2002)
24
An editing mechanism for the methionyl-tRNA synthetase in the selection of amino acids in protein synthesis
AR Fersht, C Dingwall
Biochemistry
(2002)
18
Direct observation of complexes of ssb and recA proteins with a fluorescent single-stranded deoxyribonucleic acid derivative.
SM Cotterill, AR Fersht
Biochemistry
(2002)
22
SITE-DIRECTED MUTAGENESIS AS A PROBE OF ENZYME STRUCTURE AND CATALYSIS - TYROSYL-TRANSFER RNA-SYNTHETASE CYSTEINE-35 TO GLYCINE-35 MUTATION
AJ Wilkinson, AR Fersht, DM Blow, G Winter
Biochemistry
(2002)
22
recA Filaments in solution
SM Cotterill, AR Fersht
Biochemistry
(2002)
22
Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxyribonucleic acid derivative
MS Silver, AR Fersht
Biochemistry
(2002)
22
Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative
MS Silver, AR Fersht
Biochemistry
(2002)
21
RECA PROTEIN FROM ESCHERICHIA-COLI - A VERY RAPID AND SIMPLE PURIFICATION PROCEDURE - BINDING OF ADENOSINE 5'-TRIPHOSPHATE AND ADENOSINE 5'-DIPHOSPHATE BY THE HOMOGENEOUS PROTEIN
SM Cotterill, AC Satterthwait, AR Fersht
Biochemistry
(2002)
21
Contribution of Residues in the Reactive Site Loop of Chymotrypsin Inhibitor 2 to Protein Stability and Activity
SE Jackson, AR Fersht
Biochemistry
(2002)
33
Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes.
AR Fersht
Biochemistry
(2002)
14