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

Natural variation of tyrosyl-tRNA synthetase and comparison with engineered mutants.
MD Jones, DM Lowe, T Borgford, AR Fersht
Biochemistry
(2002)
25
Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase
TN Wells, AR Fersht
Biochemistry
(2002)
25
Fine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase
AR Fersht, AJ Wilkinson, P Carter, G Winter
Biochemistry
(2002)
24
Reversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface
DH Jones, AJ McMillan, AR Fersht, G Winter
Biochemistry
(2002)
24
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
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-tRNA 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
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