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
Journal of molecular biology
(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 N-15, C-13(alpha) and C-13-methyl relaxation dispersion and H-1/(2) H-exchange NMR Spectroscopy
DM Korzhnev, TL Religa, P Lundström, AR Fersht, LE Kay
Journal of molecular biology
(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
Proc Natl Acad Sci U S A
(2007)
104
Solution structure of ASPP2 n-terminal domain (N-ASPP2) reveals a ubiquitin-like fold
H Tidow, A Andreeva, TJ Rutherford, AR Fersht
Journal of molecular biology
(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
Structural biology: 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 - Editorial overview
AR Fersht, V Daggett
Current Opinion in Structural Biology
(2007)
17