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

Determination of the folding transition states of barnase by using ΦI-value-restrained simulations validated by double mutant ΦIJ-values
X Salvatella, CM Dobson, AR Fersht, M Vendruscolo
Proceedings of the National Academy of Sciences of the United States of America
(2005)
102
Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding
GWN White, S Gianni, JG Grossmann, P Jemth, AR Fersht, V Daggett
Journal of Molecular Biology
(2005)
350
The crystal structure of human CD1d with and without alpha-galactosylceramide.
M Koch, VS Stronge, D Shepherd, SD Gadola, B Mathew, G Ritter, AR Fersht, GS Besra, RR Schmidt, EY Jones, V Cerundolo
Nature immunology
(2005)
6
The structure of the major transition state for folding of an FF domain from experiment and simulation
P Jemth, R Day, S Gianni, F Khan, M Allen, V Daggett, AR Fersht
Journal of Molecular Biology
(2005)
350
Comparative binding of p53 to its promoter and DNA recognition elements
RL Weinberg, DB Veprintsev, M Bycroft, AR Fersht
J Mol Biol
(2005)
348
Simulation and experiment at high temperatures: Ultrafast folding of a thermophilic protein by nucleation-condensation
N Ferguson, R Day, CM Johnson, MD Allen, V Daggett, AR Fersht
Journal of Molecular Biology
(2005)
347
Modulation of binding of DNA to the C-terminal domain of p53 by acetylation.
A Friedler, DB Veprintsev, SMV Freund, KI von Glos, AR Fersht
Structure (London, England : 1993)
(2005)
13
Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor.
MR Fernandez-Fernandez, DB Veprintsev, AR Fersht
Proceedings of the National Academy of Sciences
(2005)
102
INSERTION IN BARNASE OF A LOOP SEQUENCE FROM RIBONUCLEASE-T1 - INVESTIGATING SEQUENCE AND STRUCTURE ALIGNMENTS BY PROTEIN ENGINEERING
S Vuilleumier, AR Fersht
European journal of biochemistry
(2005)
221
Structures of p53 Cancer Mutants and Mechanism of Rescue by Second-site Suppressor Mutations*
AC Joerger, HC Ang, DB Veprintsev, CM Blair, AR Fersht
J Biol Chem
(2005)
280