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

Ultraslow oligomerization equilibria of p53 and its implications.
E Natan, D Hirschberg, N Morgner, CV Robinson, AR Fersht
Proc Natl Acad Sci U S A
(2009)
106
Effects of Stability on the Biological Function of p53*
KH Khoo, S Mayer, AR Fersht
J Biol Chem
(2009)
284
Adaptive Evolution of p53 Thermodynamic Stability
KH Khoo, A Andreeva, AR Fersht
J Mol Biol
(2009)
393
The accessory subunit of mitochondrial DNA polymerase gamma determines the DNA content of mitochondrial nucleoids in human cultured cells.
M Di Re, H Sembongi, J He, A Reyes, T Yasukawa, P Martinsson, LJ Bailey, S Goffart, JD Boyd-Kirkup, TS Wong, AR Fersht, JN Spelbrink, IJ Holt
Nucleic Acids Res
(2009)
37
Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics.
S Rajagopalan, A Andreeva, DP Teufel, SM Freund, AR Fersht
Journal of Biological Chemistry
(2009)
284
Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core.
KH Khoo, AC Joerger, SMV Freund, AR Fersht
Protein Engineering Design and Selection
(2009)
22
The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family.
H Neuweiler, TD Sharpe, TJ Rutherford, CM Johnson, MD Allen, N Ferguson, AR Fersht
J Mol Biol
(2009)
390
PRIMA-1 reactivates mutant p53 by covalent binding to the core domain.
JMR Lambert, P Gorzov, DB Veprintsev, M Söderqvist, D Segerbäck, J Bergman, AR Fersht, P Hainaut, KG Wiman, VJN Bykov
Cancer Cell
(2009)
15
Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2.
DP Teufel, M Bycroft, AR Fersht
Oncogene
(2009)
28
Downhill versus Barrier-Limited Folding of BBL 1: Energetic and Structural Perturbation Effects upon Protonation of a Histidine of Unusually Low pKa
E Arbely, TJ Rutherford, TD Sharpe, N Ferguson, AR Fersht
Journal of Molecular Biology
(2009)
387