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

Submillisecond events in protein folding.
B Nölting, R Golbik, AR Fersht
Proceedings of the National Academy of Sciences
(1995)
92
Disulfide mutants of barnase. I: 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
J Mol Biol
(1995)
253
Negative activation enthalpies in the kinetics of protein folding.
M Oliveberg, YJ Tan, AR Fersht
Proc Natl Acad Sci U S A
(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 of the United States of America
(1995)
92
Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution
AR Fersht
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
(1995)
348
Preface
CM Dobson, AR Fersht
Philosophical Transactions of the Royal Society B Biological Sciences
(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)