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

Minimal and optimal mechanisms for GroE-mediated protein folding (vol 95, pg 15275, 1998)
AP Ben-Zvi, J Chatellier, AR Fersht, P Goloubinoff
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(1999)
96
Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization.
MG Mateu, AR Fersht
Proc Natl Acad Sci U S A
(1999)
96
Acquisition of native-like interactions in C-terminal fragments of barnase.
JL Neira, AR Fersht
Journal of Molecular Biology
(1999)
287
Structural response to mutation at a protein-protein interface 1 1Edited by R. Huber
CK Vaughan, AM Buckle, AR Fersht
Journal of molecular biology
(1999)
286
An irregular β-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase
DD Axe, NW Foster, AR Fersht
J Mol Biol
(1999)
286
Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53
MG Mateu, MM Sánchez Del Pino, AR Fersht
Nat Struct Biol
(1999)
6
Oxidative refolding chromatography: folding of the scorpion toxin Cn5
MM Altamirano, C García, LD Possani, AR Fersht
Nat Biotechnol
(1999)
17
Stability and folding of the tumour suppressor protein p16.
KS Tang, BJ Guralnick, WK Wang, AR Fersht, LS Itzhaki
J Mol Biol
(1999)
285
Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments.
JL Neira, AR Fersht
J Mol Biol
(1999)
285
The FHA domain is a modular phosphopeptide recognition motif
D Durocher, J Henckel, AR Fersht, SP Jackson
Molecular Cell
(1999)
4