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

Refolding chromatography with immobilized mini-chaperones.
MM Altamirano, R Golbik, R Zahn, AM Buckle, AR Fersht
Proc Natl Acad Sci U S A
(1997)
94
Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli.
V Gopalan, R Golbik, G Schreiber, AR Fersht, S Altman
Journal of molecular biology
(1997)
267
Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation11Edited by J. Karn
C Frisch, G Schreiber, CM Johnson, AR Fersht
Journal of Molecular Biology
(1997)
267
Role of Isoleucine-164 at the Active Site of Rubisco fromRhodospirillum rubrum
P Chène, AG Day, AR Fersht
Biochem Biophys Res Commun
(1997)
232
The folding pathway of a protein at high resolution from microseconds to seconds.
B Nölting, R Golbik, JL Neira, AS Soler-Gonzalez, G Schreiber, AR Fersht
Proceedings of the National Academy of Sciences
(1997)
94
Nucleation mechanisms in protein folding
AR Fersht
Curr Opin Struct Biol
(1997)
7
Hydrogen exchange at equilibrium: a short cut for analysing protein-folding pathways?
J Clarke, LS Itzhaki, AR Fersht
Trends in biochemical sciences
(1997)
22
Strain in the folding nucleus of chymotrypsin inhibitor 2
AG Ladurner, LS Itzhaki, AR Fersht
Structure
(1997)
2
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
R Zahn, AM Buckle, S Perrett, CM Johnson, FJ Corrales, R Golbik, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(1996)
93
Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways.
YJ Tan, M Oliveberg, AR Fersht
J Mol Biol
(1996)
264