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

Folding of Circular and Permuted Chymotrypsin Inhibitor 2:  Retention of the Folding Nucleus
DE Otzen, AR Fersht
Biochemistry
(1998)
37
Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathway (vol 94, pg 13409, 1997)
CJ Bond, KB Wong, J Clarke, AR Fersht, V Daggett
P NATL ACAD SCI USA
(1998)
95
A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease.
DD Axe, NW Foster, AR Fersht
Biochemistry
(1998)
37
Research: Protein structure - Sieves in sequence
AR Fersht
SCIENCE
(1998)
280
The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding 1 1Edited by W. Baumeister
M Oliveberg, YJ Tan, M Silow, AR Fersht
Journal of molecular biology
(1998)
277
Movement of the Intermediate and Rate Determining Transition State of Barnase on the Energy Landscape with Changing Temperature
PA Dalby, M Oliveberg, AR Fersht
Biochemistry
(1998)
37
Folding intermediates of wild-type and mutants of barnase. I. Use of phi-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium
PA Dalby, M Oliveberg, AR Fersht
J Mol Biol
(1998)
276
Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate.
PA Dalby, J Clarke, CM Johnson, AR Fersht
J Mol Biol
(1998)
276
Real‐time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2
TR Killick, SM Freund, AR Fersht
FEBS Lett
(1998)
423
Thermodynamic stability and folding of GroEL minichaperones 1 1Edited by P. E. Wright
R Golbik, R Zahn, SE Harding, AR Fersht
Journal of molecular biology
(1998)
276