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
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-helices 1 1Edited by J. Karn
J Chatellier, AM Buckle, 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
J Mol Biol
(1999)
292
Identification of substrate binding site of GroEL minichaperone in solution
N Tanaka, AR Fersht
J Mol Biol
(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 of the United States of America
(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