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

Mechanism of chymotrypsin. Structure, reactivity, and nonproductive binding relationships.
J Fastrez, AR Fersht
Biochemistry
(2002)
12
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis
AR Fersht
Biochemistry
(2002)
26
Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases.
TJ Borgford, TE Gray, NJ Brand, AR Fersht
Biochemistry
(2002)
26
Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
L Serrano, A Horovitz, B Avron, M Bycroft, AR Fersht
Biochemistry
(2002)
29
Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the alpha-ammonium group binding site of tyrosyl-tRNA synthetase.
DM Lowe, G Winter, AR Fersht
Biochemistry
(2002)
26
Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.
AR Fersht, RJ Leatherbarrow, TN Wells
Biochemistry
(2002)
26
Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase
FT Lau, AR Fersht, HW Hellinga, PR Evans
Biochemistry
(2002)
26
Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase
WHJ Ward, DH Jones, AR Fersht
Biochemistry
(2002)
26
The valyl-tRNA synthetase from Bacillus stearothermophilus has considerable sequence homology with the isoleucyl-tRNA synthetase from Escherichia coli
TJ Borgford, NJ Brand, TE Gray, AR Fersht
Biochemistry
(2002)
26
Free energy of hydrolysis of tyrosyl adenylate and its binding to wild-type and engineered mutant tyrosyl-tRNA synthetases
TN Wells, CK Ho, AR Fersht
Biochemistry
(2002)
25