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

Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea.
CM Johnson, AR Fersht
Biochemistry
(2002)
34
Side-chain determinants of beta-sheet stability.
DE Otzen, AR Fersht
Biochemistry
(2002)
34
Mechanism of chymotrypsin. Structure, reactivity, and nonproductive binding relationships.
J Fastrez, AR Fersht
Biochemistry
(2002)
12
A Calorimetric Study of the Thermal Stability of Barstar and Its Interaction with Barnase
JC Martínez, VV Filimonov, PL Mateo, G Schreiber, AR Fersht
Biochemistry
(2002)
34
Analysis of the Role of the KMSKS Loop in the Catalytic Mechanism of the Tyrosyl-tRNA Synthetase Using Multimutant Cycles
EA First, AR Fersht
Biochemistry
(2002)
34
Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin.
J Fastrez, AR Fersht
Biochemistry
(2002)
12
Backbone Dynamics of Chymotrypsin Inhibitor 2: Effect of Breaking the Active Site Bond and Its Implications for the Mechanism of Inhibition of Serine Proteases
GL Shaw, B Davis, J Keeler, AR Fersht
Biochemistry
(2002)
34
Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2)
J Ruiz-Sanz, G de Prat Gay, DE Otzen, AR Fersht
Biochemistry
(2002)
34
Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. Stereochemical interpretation
AR Fersht, DM Blow, J Fastrez
Biochemistry
(2002)
12
Analysis of the mechanism of assembly of cleaved barnase from two peptide fragments and its relevance to the folding pathway of uncleaved barnase.
AD Kippen, AR Fersht
Biochemistry
(2002)
34