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Yusuf Hamied Department of Chemistry

 
Portrait of arf25

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

Chemical physics of protein folding.
PG Wolynes, WA Eaton, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(2012)
109,
17770
Stability of p53 homologs.
T Brandt, JL Kaar, AR Fersht, DB Veprintsev
– PloS one
(2012)
7,
e47889
Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2.
SM Vogel, MR Bauer, AC Joerger, R Wilcken, T Brandt, DB Veprintsev, TJ Rutherford, AR Fersht, FM Boeckler
– Proc Natl Acad Sci U S A
(2012)
109,
16906
Sequence-dependent sliding kinetics of p53
JS Leith, A Tafvizi, F Huang, WE Uspal, PS Doyle, AR Fersht, LA Mirny, AM van Oijen
– Proc Natl Acad Sci U S A
(2012)
109,
16552
Domain–domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy
M Bista, SM Freund, AR Fersht
– Proc Natl Acad Sci U S A
(2012)
109,
15752
In support of the BMRB.
JL Markley, H Akutsu, T Asakura, M Baldus, R Boelens, A Bonvin, R Kaptein, A Bax, I Bezsonova, MR Gryk, JC Hoch, DM Korzhnev, MW Maciejewski, D Case, WJ Chazin, TA Cross, S Dames, H Kessler, O Lange, T Madl, B Reif, M Sattler, D Eliezer, A Fersht, J Forman-Kay, LE Kay, J Fraser, J Gross, T Kortemme, A Sali, T Fujiwara, K Gardner, X Luo, J Rizo-Rey, M Rosen, RR Gil, C Ho, G Rule, AM Gronenborn, R Ishima, J Klein-Seetharaman, P Tang, P van der Wel, Y Xu, S Grzesiek, S Hiller, J Seelig, ED Laue, H Mott, D Nietlispach, I Barsukov, L-Y Lian, D Middleton, T Blumenschein, G Moore, I Campbell, J Schnell, IJ Vakonakis, A Watts, MR Conte, J Mason, M Pfuhl, MR Sanderson, J Craven, M Williamson, C Dominguez, G Roberts, U Günther, M Overduin, J Werner, P Williamson, C Blindauer, M Crump, P Driscoll, T Frenkiel, A Golovanov, S Matthews, J Parkinson, D Uhrin, M Williams, D Neuhaus, H Oschkinat, A Ramos, DE Shaw, C Steinbeck, M Vendruscolo, GW Vuister, KJ Walters, H Weinstein, K Wüthrich, S Yokoyama
– Nature Structural & Molecular Biology
(2012)
19,
854
First-order rate-determining aggregation mechanism of p53 and its implications
G Wang, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(2012)
109,
13590
Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition
R Wilcken, G Wang, FM Boeckler, AR Fersht
– Proc Natl Acad Sci U S A
(2012)
109,
13584
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 Edition
(2012)
52,
361
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
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