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

The complete folding pathway of a protein from nanoseconds to microseconds
U Mayor, NR Guydosh, CM Johnson, JG Grossmann, S Sato, GS Jas, SMV Freund, DOV Alonso, V Daggett, AR Fersht
Nature
(2003)
421
Early events in protein folding.
N Ferguson, AR Fersht
Current opinion in structural biology
(2003)
13
Sequential unfolding of ankyrin repeats in tumor suppressor p16
KS Tang, AR Fersht, LS Itzhaki
Structure (London, England : 1993)
(2003)
11
Is there a unifying mechanism for protein folding?
V Daggett, AR Fersht
Trends in Biochemical Sciences
(2003)
28
Molecular Mechanism of the Interaction between MDM2 and p53
O Schon, A Friedler, M Bycroft, SMV Freund, AR Fersht
Journal of Molecular Biology
(2002)
323
On the simulation of protein folding by short time scale molecular dynamics and distributed computing.
AR Fersht
Proc Natl Acad Sci U S A
(2002)
99
CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90.
S Rudiger, SMV Freund, DB Veprintsev, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2002)
99
Two sequence motifs from HIF-1α bind to the DNA-binding site of p53
LO Hansson, A Friedler, S Freund, S Rudiger, AR Fersht
Proceedings of the National Academy of Sciences
(2002)
99
Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding.
TM Rippin, SMV Freund, DB Veprintsev, AR Fersht
J Mol Biol
(2002)
319
Directed evolution of new catalytic activity using the α/β-barrel scaffold (Retraction of vol 403, pg 617, 2000)
MM Altamirano, JM Blackburn, C Aguayo, AR Fersht
NATURE
(2002)
417