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
Proceedings of the National Academy of Sciences of the United States of America
(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
Proc Natl Acad Sci U S A
(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
J Mol Biol
(1997)
274
Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2.
AG Ladurner, LS Itzhaki, G de Prat Gay, AR Fersht
J Mol Biol
(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
Journal of molecular biology
(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 temperature11Edited by J. Karn
LS Itzhaki, JL Neira, AR Fersht
J Mol Biol
(1997)
270