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

Helix stability in barstar peptides
AS Soler-González, AR Fersht
The FEBS Journal
(2004)
249
Carl-Ivar!Branden - 1934-2004 - Obituary
S Zhang, A Rich, JL Sussman, AR Fersht
Nature Structural & Molecular Biology
(2004)
11
Φ-Value analysis and the nature of protein-folding transition states
AR Fersht, S Sato
Proc Natl Acad Sci U S A
(2004)
101
Designing a metal-binding site in the scaffold of Escherichia coli KDO8PS.
Z Oliynyk, L Briseño-Roa, T Janowitz, P Sondergeld, AR Fersht
Protein Engineering Design and Selection
(2004)
17
Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation.
P Jemth, S Gianni, R Day, B Li, CM Johnson, V Daggett, AR Fersht
Proceedings of the National Academy of Sciences
(2004)
101
Testing protein-folding simulations by experiment: B domain of protein A
S Sato, TL Religa, V Daggett, AR Fersht
Proceedings of the National Academy of Sciences
(2004)
101
The crystal structure of human CD1b with a bound bacterial glycolipid
T Batuwangala, D Shepherd, SD Gadola, KJC Gibson, NR Zaccai, AR Fersht, GS Besra, V Cerundolo, EY Jones
Journal of Immunology
(2004)
172
Structural Distortion of p53 by the Mutation R249S and its Rescue by a Designed Peptide: Implications for “Mutant Conformation”
A Friedler, BS DeDecker, SMV Freund, C Blair, S Rüdiger, AR Fersht
J Mol Biol
(2004)
336
Binding of p53-derived Ligands to MDM2 Induces a Variety of Long Range Conformational Changes
O Schon, A Friedler, S Freund, AR Fersht
J Mol Biol
(2004)
336
Analysis of Enzyme Structure and Activity by Protein Engineering
AR Fersht, J Shi, AJ Wilkinson, DM Blow, P Carter, MMY Waye, GP Winter
Angewandte Chemie International Edition in English
(2003)
23