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

Characterization of the p53-rescue drug CP-31398 in vitro and in living cells
TM Rippin, VJN Bykov, SMV Freund, G Selivanova, KG Wiman, AR Fersht
Oncogene
(2002)
21
Characterization of the p53-rescue drug CP-31398 in vitro and in living cells.
TM Rippin, VJN Bykov, SMV Freund, G Selivanova, KG Wiman, AR Fersht
Oncogene
(2002)
21
Max Ferdinand Perutz OM FRS - Obituary
AR Fersht
NAT STRUCT BIOL
(2002)
9
A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.
CK Vaughan, P Harryson, AM Buckle, AR Fersht
Acta crystallographica. Section D, Biological crystallography
(2002)
58
Protein Folding and Unfolding at Atomic Resolution
AR Fersht, V Daggett
Cell
(2002)
108
Cooperativity in ATP hydrolysis by GroEL is increased by GroES
TE Gray, AR Fersht
FEBS letters
(2002)
292
Folding of the yeast prion protein Ure2: Kinetic evidence for folding and unfolding intermediates
D Galani, AR Fersht, S Perrett
Journal of Molecular Biology
(2002)
315
A peptide that binds and stabilizes p53 core domain:: Chaperone strategy for rescue of oncogenic mutants
A Friedler, LO Hansson, DB Veprintsev, SMV Freund, TM Rippin, PV Nikolova, MR Proctor, S Rüdiger, AR Fersht
Proc Natl Acad Sci U S A
(2002)
99
Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type.
SL Kazmirski, RL Isaacson, C An, A Buckle, CM Johnson, V Daggett, AR Fersht
Nature structural biology
(2002)
9
New Look and New Outlook
WA Hendrickson, C-I Brändén, AR Fersht
Structure
(2002)
10