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

Contribution of 3' leads to 5' exonuclease activity of DNA polymerase III holoenzyme from Escherichia coli to specificity.
AR Fersht, JW Knill-Jones
J Mol Biol
(1983)
165
Fidelity of replication of bacteriophage phi X174 DNA in vitro and in vivo.
AR Fersht, JW Knill-Jones
J Mol Biol
(1983)
165
Kinetics of base misinsertion by DNA polymerase I of Escherichia coli
AR Fersht, JP Shi, WC Tsui
Journal of molecular biology
(1983)
165
ACCURACY OF DNA POLYMERASE-ALPHA IN COPYING NATURAL DNA
F GROSSE, G KRAUSS, JW KNILLJONES, AR FERSHT
H-S Z PHYSIOL CHEM
(1983)
364
Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding
G Winter, AR Fersht, AJ Wilkinson, M Zoller, M Smith
Nature
(1982)
299
Kinetic basis of spontaneous mutation. Misinsertion frequencies, proofreading specificities and cost of proofreading by DNA polymerases of Escherichia coli.
AR Fersht, JW Knill-Jones, WC Tsui
Journal of molecular biology
(1982)
156
Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli.
WC Tsui, AR Fersht
Nucleic Acids Res
(1981)
9
Review Lecture Enzymic editing mechanisms and the genetic code
AR Fersht
Proceedings of the Royal Society B
(1981)
212
Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases
H Jakubowski, AR Fersht
Nucleic Acids Res
(1981)
9
DNA polymerase accuracy and spontaneous mutation rates: frequencies of purine.purine, purine.pyrimidine, and pyrimidine.pyrimidine mismatches during DNA replication.
AR Fersht, JW Knill-Jones
Proc Natl Acad Sci U S A
(1981)
78