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

Transient folding intermediates characterized by protein engineering.
A Matouschek, JT Kellis, L Serrano, M Bycroft, AR Fersht
Nature
(1990)
346
Protein engineering and the study of structure—function relationships in receptors
WH Ward, D Timms, AR Fersht
Trends in pharmacological sciences
(1990)
11
Folding pathway enigma
AR FERSHT, JT KELLIS, ATEL MATOUSCHEK, L SERRANO
Nature
(1990)
343
Capping and α-helix stability
L Serrano, AR Fersht
Nature
(1989)
342
Mapping the transition state and pathway of protein folding by protein engineering
A Matouschek, JT Kellis, L Serrano, AR Fersht
Nature
(1989)
340
Can a simple function for the dielectric response model electrostatic effects in globular proteins?
AR Fersht, MJ Sternberg
"Protein Engineering, Design and Selection"
(1989)
2
Stabilization of protein structure by interaction of α-helix dipole with a charged side chain
D Sali, M Bycroft, AR Fersht
Nature
(1988)
335
TYROSYL-TRANSFER RNA-SYNTHETASE ACTS AS AN ASYMMETRIC DIMER IN CHARGING TRANSFER-RNA - A RATIONALE FOR HALF-OF-THE-SITES ACTIVITY
WHJ WARD, AR FERSHT
BIOCHEMISTRY
(1988)
27
Contribution of hydrophobic interactions to protein stability
JT Kellis, K Nyberg, D Sali, AR Fersht
Nature
(1988)
333
DISSECTION OF ENZYME STRUCTURE AND ACTIVITY
AR FERSHT
BIOL CHEM H-S
(1988)
369