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

Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering.
AJ Russell, PG Thomas, AR Fersht
J Mol Biol
(1987)
193
The hydrogen bond in molecular recognition
AR Fersht
Trends in Biochemical Sciences
(1987)
12
Concluding comment:–Fersht
AR Fersht
Protein Engineering Design and Selection
(1987)
1
Single-stranded M13 DNA: use as a cloning vector
MD Jones, NJ Brand, AR Fersht
Nucleic acids research
(1986)
14
Catalytic dissection of an enzyme active site
TNC WELLS, AR FERSHT
Biochemical Society Transactions
(1986)
14
Protein engineering.
RJ Leatherbarrow, AR Fersht
Protein engineering
(1986)
1
Binding energy and catalysis: a lesson from protein engineering of the tyrosyl-tRNA synthetase
AR Fersht, RJ Leatherbarrow, TNC Wells
Trends in Biochemical Sciences
(1986)
11
Protein engineering of homodimeric tyrosyl-tRNA synthetase to produce active heterodimers.
WH Ward, DH Jones, AR Fersht
Journal of Biological Chemistry
(1986)
261
Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships
AR Fersht, RJ Leatherbarrow, TNC Wells
Nature
(1986)
322
Commercial samples of subtilisin BPN′
AJ RUSSELL, AR FERSHT
Nature
(1986)
321