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

Phi-analysis at the experimental limits: mechanism of beta-hairpin formation.
M Petrovich, AL Jonsson, N Ferguson, V Daggett, AR Fersht
J Mol Biol
(2006)
360
Effects of Common Cancer Mutations on Stability and DNA Binding of Full-length p53 Compared with Isolated Core Domains*
HC Ang, AC Joerger, S Mayer, AR Fersht
J Biol Chem
(2006)
281
Solution structure of p53 core domain: structural basis for its instability.
JMP Cañadillas, H Tidow, SMV Freund, TJ Rutherford, HC Ang, AR Fersht
Proceedings of the National Academy of Sciences
(2006)
103
Core domain interactions in full-length p53 in solution
DB Veprintsev, SMV Freund, A Andreeva, SE Rutledge, H Tidow, JMP Cañadillas, CM Blair, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2006)
103
The central region of HDM2 provides a second binding site for p53
GW Yu, S Rudiger, D Veprintsev, S Freund, MR Fernandez-Fernandez, AR Fersht
Proc Natl Acad Sci U S A
(2006)
103
Solution structure of the C4 zinc finger domain of HDM2.
GW Yu, MD Allen, A Andreeva, AR Fersht, M Bycroft
Protein science : a publication of the Protein Society
(2005)
15
The Transition State for Folding of a Peripheral Subunit-binding Domain Contains Robust and Ionic-strength Dependent Characteristics
N Ferguson, TD Sharpe, CM Johnson, AR Fersht
Journal of molecular biology
(2005)
356
Analogues with Fluorescent Leaving Groups for Screening and Selection of Enzymes That Efficiently Hydrolyze Organophosphorus Nerve Agents
L Briseño-Roa, J Hill, S Notman, D Sellers, AP Smith, CM Timperley, J Wetherell, NH Williams, GR Williams, AR Fersht, AD Griffiths
J Med Chem
(2005)
49
Ultra-fast Barrier-limited Folding in the Peripheral Subunit-binding Domain Family
N Ferguson, TD Sharpe, PJ Schartau, S Sato, MD Allen, CM Johnson, TJ Rutherford, AR Fersht
Journal of Molecular Biology
(2005)
353
Solution structure of a protein denatured state and folding intermediate
TL Religa, JS Markson, U Mayor, SMV Freund, AR Fersht
Nature
(2005)
437