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Yusuf Hamied Department of Chemistry

 

Professor Sir Alan Fersht FRS

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

First-order rate-determining aggregation mechanism of p53 and its implications
G Wang, AR Fersht
– Proceedings of the National Academy of Sciences
(2012)
109,
13590
(doi: 10.1073/pnas.1211557109)
Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase
K Pagel, E Natan, Z Hall, AR Fersht, CV Robinson
– Angewandte Chemie (International ed. in English)
(2012)
52,
361
(doi: 10.1002/anie.201203047)
Halogen-enriched fragment libraries as leads for drug rescue of mutant p53.
R Wilcken, X Liu, MO Zimmermann, TJ Rutherford, AR Fersht, AC Joerger, FM Boeckler
– J Am Chem Soc
(2012)
134,
6810
(doi: 10.1021/ja301056a)
Long-Range Modulation of Chain Motions within the Intrinsically Disordered Transactivation Domain of Tumor Suppressor p53
JK Lum, H Neuweiler, AR Fersht
– Journal of the American Chemical Society
(2012)
134,
1617
(doi: 10.1021/ja2078619)
Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: An NMR relaxation dispersion study
DM Korzhnev, RM Vernon, TL Religa, AL Hansen, D Baker, AR Fersht, LE Kay
– Journal of the American Chemical Society
(2011)
133,
10974
(doi: 10.1021/ja203686t)
Combination of Markov State Models and Kinetic Networks for the Analysis of Molecular Dynamics Simulations of Peptide Folding
IH Radford, AR Fersht, G Settanni
– The journal of physical chemistry. B
(2011)
115,
7459
(doi: 10.1021/jp112158w)
Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration
E Arbely, E Natan, T Brandt, MD Allen, DB Veprintsev, CV Robinson, JW Chin, AC Joerger, AR Fersht
– Proceedings of the National Academy of Sciences
(2011)
108,
8251
(doi: 10.1073/pnas.1105028108)
Electrocatalytic monitoring of metal binding and mutation-induced conformational changes in p53 at picomole level
E Paleček, V Ostatná, H Černocká, AC Joerger, AR Fersht
– Journal of the American Chemical Society
(2011)
133,
7190
(doi: 10.1021/ja201006s)
Interaction of the p53 DNA-binding domain with its N-terminal extension modulates the stability of the p53 tetramer
E Natan, C Baloglu, K Pagel, SMV Freund, N Morgner, CV Robinson, AR Fersht, AC Joerger
– Journal of molecular biology
(2011)
409,
358
(doi: 10.1016/j.jmb.2011.03.047)
Malleability of folding intermediates in the homeodomain superfamily.
W Banachewicz, TL Religa, RD Schaeffer, V Daggett, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(2011)
108,
5596
(doi: 10.1073/pnas.1101752108)
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