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

Structural insights in the folding of small single-domain proteins.
S Gianni, U Mayor, AR Fersht
The Italian journal of biochemistry
(2003)
52
The denatured state of Engrailed Homeodomain under denaturing and native conditions.
U Mayor, JG Grossmann, NW Foster, SMV Freund, AR Fersht
Journal of Molecular Biology
(2003)
333
Unifying features in protein-folding mechanisms
S Gianni, NR Guydosh, F Khan, TD Caldas, U Mayor, GWN White, ML DeMarco, V Daggett, AR Fersht
Proc Natl Acad Sci U S A
(2003)
100
Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide.
N Issaeva, A Friedler, P Bozko, KG Wiman, AR Fersht, G Selivanova
Proc Natl Acad Sci U S A
(2003)
100
The Kinetic Pathway of Folding of Barnase
F Khan, JI Chuang, S Gianni, AR Fersht
Journal of Molecular Biology
(2003)
333
Crystal structure of a superstable mutant of human p53 core domain - Insights into the mechanism of rescuing oncogenic mutations
AC Joerger, MD Allen, AR Fersht
The Journal of biological chemistry
(2003)
279
Crystal Structures of Engrailed Homeodomain Mutants: Implications for stability and dynamics
EJ Stollar, U Mayor, SC Lovell, L Federici, SMV Freund, AR Fersht, BF Luisi
The Journal of biological chemistry
(2003)
278
Rapid amyloid fiber formation from the fast-folding WW domain FBP28.
N Ferguson, J Berriman, M Petrovich, TD Sharpe, JT Finch, AR Fersht
Proc Natl Acad Sci U S A
(2003)
100
Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity.
AC Joerger, S Mayer, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2003)
100
Kinetic instability of p53 core domain mutants: implications for rescue by small molecules.
A Friedler, DB Veprintsev, LO Hansson, AR Fersht
The Journal of biological chemistry
(2003)
278