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

[Folding mechanism and folding rate].
T Ikura, AR Fersht
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme
(2001)
46
Experimental assignment of the structure of the transition state for the association of barnase and barstar.
C Frisch, AR Fersht, G Schreiber
Journal of molecular biology
(2001)
308
Structure of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha.
WK Wang, M Bycroft, NW Foster, AM Buckle, AR Fersht, YW Chen
Acta Crystallographica Section D Biological Crystallography
(2001)
57
Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution.
SL Kazmirski, KB Wong, SM Freund, YJ Tan, AR Fersht, V Daggett
Proceedings of the National Academy of Sciences of the United States of America
(2001)
98
Ligand-independent assembly of recombinant human CD1 by using oxidative refolding chromatography
MM Altamirano, A Woolfson, A Donda, A Shamshiev, L Briseño-Roa, NW Foster, DB Veprintsev, G De Libero, AR Fersht, C Milstein
Proceedings of the National Academy of Sciences
(2001)
98
The Binding of Bis-ANS to the Isolated GroEL Apical Domain Fragment Induces the Formation of a Folding Intermediate with Increased Hydrophobic Surface Not Observed in Tetradecameric GroEL
AL Smoot, M Panda, BT Brazil, AM Buckle, AR Fersht, PM Horowitz
Biochemistry
(2001)
40
Preface
CM Dobson, R John Ellis, AR Fersht
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(2001)
356
Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation (vol 97, pg 13518, 2000)
U Mayor, CM Johnson, V Daggett, AR Fersht
P NATL ACAD SCI USA
(2001)
98
Structure on the move
WA Hendrickson, C-I Brändén, AR Fersht
Structure
(2001)
9
From Minichaperone to GroEL 2: Importance of Avidity of the Multisite Ring Structure
J Chatellier, F Hill, AR Fersht
Journal of Molecular Biology
(2000)
304