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

Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations
PV Nikolova, KB Wong, B DeDecker, J Henckel, AR Fersht
The EMBO Journal
(2000)
19
Interdomain interactions within the gene 3 protein of filamentous phage.
J Chatellier, O Hartley, AD Griffiths, AR Fersht, G Winter, L Riechmann
FEBS Lett
(2000)
463
Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis-Finnish type
RL Isaacson, AG Weeds, AR Fersht
Proceedings of the National Academy of Sciences
(1999)
96
Formation of short-lived protein aggregates directly from the coil in two-state folding.
M Silow, YJ Tan, AR Fersht, M Oliveberg
Biochemistry
(1999)
38
NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution 1 1 Edited by J. Karn
N Kobayashi, SM Freund, J Chatellier, R Zahn, AR Fersht
Journal of molecular biology
(1999)
292
Identification of substrate binding site of GroEL minichaperone in solution 1 1 Edited by J. Karn
N Tanaka, AR Fersht
J Mol Biol
(1999)
292
GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices
J Chatellier, AM Buckle, AR Fersht
Journal of Molecular Biology
(1999)
292
The FHA domain is a modular phosphopeptide recognition motif.
D Durocher, J Henckel, AR Fersht, SP Jackson
Molecular Cell
(1999)
4
Hot-spot mutants of p53 core domain evince characteristic local structural changes
KB Wong, BS DeDecker, SM Freund, MR Proctor, M Bycroft, AR Fersht
Proceedings of the National Academy of Sciences
(1999)
96
Equilibrium folding properties of the yeast prion protein determinant Ure2.
S Perrett, SJ Freeman, PJ Butler, AR Fersht
Journal of molecular biology
(1999)
290