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

ALPHA-HELIX STABILITY IN PROTEINS .1. 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
Journal of molecular biology
(1992)
227
Alpha-helix stability in proteins. II. Factors that influence stability at an internal position.
A Horovitz, JM Matthews, AR Fersht
J Mol Biol
(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
J Mol Biol
(1992)
225
MUTATION OF ASPARAGINE-111 OF RUBISCO FROM RHODOSPIRILLUM-RUBRUM ALTERS THE CARBOXYLASE OXYGENASE SPECIFICITY
P Chène, AG Day, AR Fersht
J Mol Biol
(1992)
225
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
J Mol Biol
(1992)
224
The folding of an enzyme
L Serrano, A Matouschek, AR Fersht
Journal of molecular biology
(1992)
224
THE FOLDING OF AN ENZYME .5. H/H-2 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
J Mol Biol
(1992)
224
THE FOLDING OF AN ENZYME .4. STRUCTURE OF AN INTERMEDIATE IN THE REFOLDING OF BARNASE ANALYZED 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
J Mol Biol
(1992)
224