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 and binding - Editorial overview
KA Dill, AR Fersht
CURR OPIN STRUC BIOL
(1996)
6
Folding & Design: introduction to a new journal.
AR Fersht, FE Cohen
Folding and Design
(1996)
1
Folding & design: Introduction to a new journal
AR Fersht, FE Cohen
FOLDING & DESIGN
(1996)
1
Pathways of protein folding
AR Fersht
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
(1996)
65
Perturbed pKA-values in the denatured states of proteins.
YJ Tan, M Oliveberg, B Davis, AR Fersht
Journal of Molecular Biology
(1995)
254
CONFORMATIONAL PATHWAY OF THE POLYPEPTIDE-CHAIN OF CHYMOTRYPSIN INHIBITOR-2 GROWING FROM ITS N-TERMINUS IN-VITRO - PARALLELS WITH THE PROTEIN-FOLDING PATHWAY
G de Prat Gay, J Ruiz-Sanz, JL Neira, FJ Corrales, DE Otzen, AG Ladurner, AR Fersht
Journal of Molecular Biology
(1995)
254
Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2
LS Itzhaki, JL Neira, J Ruiz-Sanz, G de Prat Gay, AR Fersht
Journal of molecular biology
(1995)
254
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
VL Arcus, S Vuilleumier, SM Freund, M Bycroft, AR Fersht
J Mol Biol
(1995)
254
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding.
LS Itzhaki, DE Otzen, AR Fersht
Journal of molecular biology
(1995)
254
Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.
AR Fersht
Proc Natl Acad Sci U S A
(1995)
92