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

Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar
MJ Lubienski, M Bycroft, DNM Jones, AR Fersht
FEBS Letters
(1993)
332
Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen-deuterium exchange
DNM Jones, M Bycroft, MJ Lubienski, AR Fersht
FEBS Letters
(1993)
331
Folding of Subtilisin BPN': Role of the Pro-sequence
J Eder, M Rheinnecker, AR Fersht
J Mol Biol
(1993)
233
Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability.
L Serrano, AG Day, AR Fersht
Journal of Molecular Biology
(1993)
233
Refolding of barnase in the presence of GroE.
TE Gray, AR Fersht
J Mol Biol
(1993)
232
Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding.
A Matouschek, AR Fersht
Proceedings of the National Academy of Sciences
(1993)
90
Long-Range Surface Charge-Charge Interactions in Proteins Comparison of Experimental Results with Calculations from a Theoretical Method
R Loewenthal, J Sancho, T Reinikainen, AR Fersht
J Mol Biol
(1993)
232
Principles of protein stability derived from protein engineering experiments
AR Fersht, L Serrano
Current Opinion in Structural Biology
(1993)
3
THE CONTRIBUTION OF INTRA-LOOP HYDROGEN-BONDS TO PROTEIN STABILITY REVEALED BY 2 MUTANT CRYSTAL-STRUCTURES OF BARNASE
YW CHEN, K HENRICK, AR FERSHT
PROTEIN ENGINEERING
(1993)
6
General discussion
M Charton, KA Brown, GE Schulz, A Warshel, J Kraut, E Pombo-Villar, AR Fersht, M Karplus, IH Williams, KA Rubinson, D Eisenberg, AD Buckingham, IH Hillier, O Smart, RJ Deeth, RK Owusu, RHM Hatley, F Franks, AC Albrecht, LD Barron, ML Sinnott, LR Fisher, DR Brown, R Lewis, R King, M Perutz, AR Leach
Faraday Discussions
(1992)
93