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

Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2.
G de Prat Gay, CM Johnson, AR Fersht
Protein engineering
(1994)
7
Editorial overview
AR Fersht, KA Dill
Current Opinion in Structural Biology
(1994)
4
Contribution of Buried Hydrogen Bonds to Protein Stability The Crystal Structures of Two Barnase Mutants
YW Chen, AR Fersht, K Henrick
J Mol Biol
(1993)
234
Crystal Structural Analysis of Mutations in the Hydrophobic Cores of Barnase
AM Buckle, K Henrick, AR Fersht
J Mol Biol
(1993)
234
Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways
J Clarke, AM Hounslow, M Bycroft, AR Fersht
Proc Natl Acad Sci U S A
(1993)
90
Refolding of barnase mutants and pro‐barnase in the presence and absence of GroEL.
TE Gray, J Eder, M Bycroft, AG Day, AR Fersht
The EMBO journal
(1993)
12
THE REFOLDING OF CIS-PEPTIDYLPROLYL AND TRANS-PEPTIDYLPROLYL ISOMERS OF BARSTAR
G SCHREIBER, AR FERSHT
BIOCHEMISTRY
(1993)
32
Protein stability: experimental data from protein engineering
AR Fersht, SE Jackson, L Serrano
Philosophical Transactions of the Royal Society of London. Series A: Physical and Engineering Sciences
(1993)
345
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