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

DISULFIDE MUTANTS OF BARNASE .1. CHANGES IN STABILITY AND STRUCTURE ASSESSED BY BIOPHYSICAL METHODS AND X-RAY CRYSTALLOGRAPHY
J Clarke, K Henrick, AR Fersht
Journal of Molecular Biology
(1995)
253
Disulfide mutants of barnase. II: Changes in structure and local stability identified by hydrogen exchange.
J Clarke, AM Hounslow, AR Fersht
Journal of molecular biology
(1995)
253
Negative activation enthalpies in the kinetics of protein folding.
M Oliveberg, YJ Tan, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(1995)
92
The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.
FJ Corrales, AR Fersht
Proceedings of the National Academy of Sciences
(1995)
92
Preface
CM Dobson, AR Fersht
Philosophical Transactions of the Royal Society B Biological Sciences
(1995)
348
Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution.
AR Fersht
Philos Trans R Soc Lond B Biol Sci
(1995)
348
Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles
G Schreiber, AR Fersht
J Mol Biol
(1995)
248
Folding of a nascent polypeptide chain in vitro: Cooperative formation of structure in a protein module
G De Prat Gay, J Ruiz-Sanz, JL Neira, LS Itzhaki, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(1995)
92
TOWARD SOLVING THE FOLDING PATHWAY OF BARNASE - THE BACKBONE C-13, N-15 AND H-1-NMR ASSIGNMENTS OF ITS PH-DENATURED AND UREA-DENATURED STATES
VL ARCUS, S VUILLEUMIER, SMV FREUND, M BYCROFT, AR FERSHT
J CELL BIOCHEM
(1995)
Crystallographic analysis of Phe→Leu substitution in the hydrophobic core of barnase
YW Chen, AR Fersht, K Henrick
Acta crystallographica. Section D, Biological crystallography
(1995)
51