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

Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis.
DE Mossakowska, K Nyberg, AR Fersht
Biochemistry
(2002)
28
Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesis.
FT Lau, AR Fersht
Biochemistry
(2002)
28
DETERMINATION OF THE 3-DIMENSIONAL SOLUTION STRUCTURE OF BARNASE USING NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
M Bycroft, S Ludvigsen, AR Fersht, FM Poulsen
Biochemistry
(2002)
30
Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
G Schreiber, AR Fersht
Biochemistry
(2002)
32
Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR.
EM Meiering, M Bycroft, AR Fersht
Biochemistry
(2002)
30
Variants of subtilisin BPN' with altered specificity profiles.
M Rheinnecker, J Eder, PS Pandey, AR Fersht
Biochemistry
(2002)
33
recA Filaments in solution
SM Cotterill, AR Fersht
Biochemistry
(2002)
22
ASSIGNMENT OF HISTIDINE RESONANCES IN THE H-1-NMR (500 MHZ) SPECTRUM OF SUBTILISIN BPN' USING SITE-DIRECTED MUTAGENESIS
M Bycroft, AR Fersht
Biochemistry
(2002)
27
Quantitative Determination of Helical Propensities from Trifluoroethanol Titration Curves
A Jasanoff, AR Fersht
Biochemistry
(2002)
33
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