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 Letters
(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 of the United States of America
(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
GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices1 1Edited by J. Karn
J Chatellier, AM Buckle, AR Fersht
J Mol Biol
(1999)
292
Identification of substrate binding site of GroEL minichaperone in solution 1 1 Edited by J. Karn
N Tanaka, AR Fersht
Journal of Molecular Biology
(1999)
292
NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.
N Kobayashi, SM Freund, J Chatellier, R Zahn, AR Fersht
Journal of Molecular Biology
(1999)
292
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
The solution structure of oxidized Escherichia coli cytochrome b562
F Arnesano, L Banci, I Bertini, J Faraone-Mennella, A Rosato, PD Barker, AR Fersht
Biochemistry
(1999)
38