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

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
INFLUENCE OF GLOBIN STRUCTURE ON STATE OF HEME .2. ALLOSTERIC TRANSITIONS IN METHEMOGLOBIN
MF Perutz, AR Fersht, SR Simon, GC Roberts
Biochemistry
(2002)
13
Recombinant chymotrypsin inhibitor 2: expression, kinetic analysis of inhibition with alpha-chymotrypsin and wild-type and mutant subtilisin BPN', and protein engineering to investigate inhibitory specificity and mechanism.
C Longstaff, AF Campbell, AR Fersht
Biochemistry
(2002)
29
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
Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetase
CK Ho, AR Fersht
Biochemistry
(2002)
25
Natural variation of tyrosyl-tRNA synthetase and comparison with engineered mutants
MD Jones, DM Lowe, T Borgford, AR Fersht
Biochemistry
(2002)
25