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

α-Helix stability in proteins
L Serrano, J Sancho, M Hirshberg, AR Fersht
Journal of molecular biology
(1992)
227
α-Helix stability in proteins II. Factors that influence stability at an internal position
A Horovitz, JM Matthews, AR Fersht
Journal of molecular biology
(1992)
227
GENETIC-ENGINEERING AND PHOTOSYNTHESIS
P CHENE, AG DAY, AR FERSHT
RECHERCHE
(1992)
23
Effect of active site residues in barnase on activity and stability.
EM Meiering, L Serrano, AR Fersht
Journal of molecular biology
(1992)
225
Mutation of asparagine 111 of rubisco from Rhodospirillum rubrum alters the carboxylase/oxygenase specificity.
P Chène, AG Day, AR Fersht
Journal of Molecular Biology
(1992)
225
The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.
L Serrano, JT Kellis, P Cann, A Matouschek, AR Fersht
Journal of molecular biology
(1992)
224
Co-operative interactions during protein folding
A Horovitz, AR Fersht
Journal of Molecular Biology
(1992)
224
Dissection of an enzyme by protein engineering The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity
J Sancho, AR Fersht
Journal of molecular biology
(1992)
224
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
J Sancho, JL Neira, AR Fersht
Journal of molecular biology
(1992)
224
Histidine-aromatic interactions in barnase
R Loewenthal, J Sancho, AR Fersht
J Mol Biol
(1992)
224