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

Binding of natively unfolded HIF-1alpha ODD domain to p53.
N Sánchez-Puig, DB Veprintsev, AR Fersht
Molecular Cell
(2005)
17
PFD: a database for the investigation of protein folding kinetics and stability.
KF Fulton, GL Devlin, RA Jodun, L Silvestri, SP Bottomley, AR Fersht, AM Buckle
Nucleic Acids Res
(2005)
33
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b(562)
P Garcia, M Bruix, M Rico, S Ciofi-Baffoni, L Banci, MC Ramachandra Shastry, H Roder, T de Lumley Woodyear, CM Johnson, AR Fersht, PD Barker
Journal of molecular biology
(2004)
346
Binding of Rad51 and other peptide sequences to a promiscuous, highly electrostatic binding site in p53
A Friedler, DB Veprintsev, T Rutherford, KI von Glos, AR Fersht
The Journal of biological chemistry
(2004)
280
Phi value versus psi analysis
AR Fersht
Proceedings of the National Academy of Sciences
(2004)
101
One-state downhill versus conventional protein folding
N Ferguson, PJ Schartau, TD Sharpe, S Sato, AR Fersht
Journal of Molecular Biology
(2004)
344
Relationship of Leffler (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates (vol 101, pg 14338, 2004)
AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2004)
101
Relationship of Leffler (Bronsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates
AR Fersht
Proceedings of the National Academy of Sciences
(2004)
101
Regulation of DNA Binding of p53 by its C-terminal Domain
RL Weinberg, SMV Freund, DB Veprintsev, M Bycroft, AR Fersht
Journal of Molecular Biology
(2004)
342
Cooperative binding of tetrameric p53 to DNA.
RL Weinberg, DB Veprintsev, AR Fersht
Journal of Molecular Biology
(2004)
341