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 II. Factors that influence stability at an internal position
A Horovitz, JM Matthews, AR Fersht
Journal of Molecular Biology
(1992)
227
Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces.
L Serrano, J Sancho, M Hirshberg, AR Fersht
J Mol Biol
(1992)
227
GENETIC-ENGINEERING AND PHOTOSYNTHESIS
P CHENE, AG DAY, AR FERSHT
RECHERCHE
(1992)
23
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
Effect of active site residues in barnase on activity and stability.
EM Meiering, L Serrano, AR Fersht
J Mol Biol
(1992)
225
The folding of an enzyme
L Serrano, A Matouschek, AR Fersht
J Mol Biol
(1992)
224
The folding of an enzyme V. solH2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: Complementarity to and agreement with protein engineering studies
A Matouschek, L Serrano, EM Meiering, M Bycroft, AR Fersht
Journal of Molecular Biology
(1992)
224
The folding of an enzyme IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure
A Matouschek, L Serrano, AR Fersht
Journal of Molecular Biology
(1992)
224
The folding of an enzyme III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
L Serrano, A Matouschek, AR Fersht
Journal of Molecular Biology
(1992)
224
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
J Mol Biol
(1992)
224