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

Searching for multiple folding pathways of a nearly symmetrical protein: Temperature dependent Phi-Value analysis of the B domain of protein A
S Sato, AR Fersht
J Mol Biol
(2007)
372
Correlation of Levels of Folded Recombinant p53 in Escherichia coli with Thermodynamic Stability in Vitro
S Mayer, S Rüdiger, HC Ang, AC Joerger, AR Fersht
Journal of Molecular Biology
(2007)
372
The Folding Pathway of an FF domain: Characterization of an On-pathway Intermediate State Under Folding Conditions by 15N, 13Cα and 13C-methyl Relaxation Dispersion and 1H/2H-exchange NMR Spectroscopy
DM Korzhnev, TL Religa, P Lundström, AR Fersht, LE Kay
J Mol Biol
(2007)
372
The helix-turn-helix motif as an ultrafast independently folding domain:: The pathway of folding of Engrailed homeodomain
TL Religa, CM Johnson, DM Vu, SH Brewer, RB Dyer, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2007)
104
Solution structure of ASPP2 n-terminal domain (N-ASPP2) reveals a ubiquitin-like fold
H Tidow, A Andreeva, TJ Rutherford, AR Fersht
J Mol Biol
(2007)
371
Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53.
DP Teufel, SM Freund, M Bycroft, AR Fersht
Proceedings of the National Academy of Sciences
(2007)
104
Structure-function-rescue: the diverse nature of common p53 cancer mutants.
AC Joerger, AR Fersht
Oncogene
(2007)
26
Conformational entropy of alanine versus glycine in protein denatured states
KA Scott, DOV Alonso, S Sato, AR Fersht, V Daggett
Proc Natl Acad Sci U S A
(2007)
104
Analysis of 'downhill' protein folding
N Ferguson, TD Sharpe, CM Johnson, PJ Schartau, AR Fersht
Nature
(2007)
445
Folding and binding: implementing the game plan
AR Fersht, V Daggett
Current Opinion in Structural Biology
(2007)
17