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

Folding and binding
E Shakhnovich, A Fersht
Current Opinion in Structural Biology
(1998)
8
A reply to Englander and Woodward
J Clarke, LS Itzhaki, AR Fersht
Trends in Biochemical Sciences
(1998)
23
Thermodynamic stability of wild-type and mutant p53 core domain
AN Bullock, J Henckel, BS DeDecker, CM Johnson, PV Nikolova, MR Proctor, DP Lane, AR Fersht
Proc Natl Acad Sci U S A
(1997)
94
Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathway
CJ Bond, KB Wong, J Clarke, AR Fersht, V Daggett
Proceedings of the National Academy of Sciences of the United States of America
(1997)
94
Strain in the transition state of folding and in the native state of proteins
A Ladurner, L Itzhaki, A Fersht
Protein Engineering
(1997)
10
Folding of barnase in the presence of the molecular chaperone SecB.
G Stenberg, AR Fersht
Journal of Molecular Biology
(1997)
274
Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 211Edited by J. Karn
AG Ladurner, LS Itzhaki, G de Prat Gay, AR Fersht
Journal of molecular biology
(1997)
273
Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
AG Ladurner, AR Fersht
J Mol Biol
(1997)
273
Circular dichroism of denatured barstar suggests residual structure
B Nölting, R Golbik, AS Soler-González, AR Fersht
Biochemistry
(1997)
36
Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature
LS Itzhaki, JL Neira, AR Fersht
J Mol Biol
(1997)
270