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

A New Approach to the Study of Transient Protein Conformations:  The Formation of a Semiburied Salt Link in the Folding Pathway of Barnase
M Oliveberg, AR Fersht
Biochemistry
(1996)
35
Importance of two buried salt bridges in the stability and folding pathway of barnase.
AC Tissot, S Vuilleumier, AR Fersht
Biochemistry
(1996)
35
Rapid, electrostatically assisted association of proteins
G Schreiber, AR Fersht
Nature Structural Biology
(1996)
3
Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.
FJ Corrales, AR Fersht
Proceedings of the National Academy of Sciences
(1996)
93
Structural and energetic responses to cavity-creating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
AM Buckle, P Cramer, AR Fersht
Biochemistry
(1996)
35
Structure of the Transition State for Folding of a Protein Derived from Experiment and Simulation
V Daggett, A Li, LS Itzhaki, DE Otzen, AR Fersht
J Mol Biol
(1996)
257
Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pH.
M Oliveberg, AR Fersht
Biochemistry
(1996)
35
Formation of electrostatic interactions on the protein-folding pathway
M Oliveberg, AR Fersht
Biochemistry
(1996)
35
Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB.
R Zahn, S Perrett, G Stenberg, AR Fersht
Science (New York, N.Y.)
(1996)
271
Folding and binding.
KA Dill, AR Fersht
Current Opinion in Structural Biology
(1996)
6