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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

Engineering a two-helix bundle protein for folding studies.
CA Dodson, N Ferguson, TJ Rutherford, CM Johnson, AR Fersht
– Protein Engineering Design and Selection
(2010)
23,
357
(doi: 10.1093/protein/gzp080)
Toward the rational design of p53-stabilizing drugs: probing the surface of the oncogenic Y220C mutant.
N Basse, JL Kaar, G Settanni, AC Joerger, TJ Rutherford, AR Fersht
– Chem Biol
(2010)
17,
46
(doi: 10.1016/j.chembiol.2009.12.011)
Reply to Campos et al.: Direct observation versus ambiguous kinetics and thermodynamics
F Huang, LM Ying, H Neuweiler, AR Fersht
– Proceedings of the National Academy of Sciences
(2009)
106,
e140
(doi: 10.1073/pnas.0913321107)
Awakening guardian angels: Drugging the P53 pathway
CJ Brown, S Lain, CS Verma, AR Fersht, DP Lane
– Nature reviews. Cancer
(2009)
9,
862
(doi: 10.1038/nrc2763)
Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer.
F Huang, S Rajagopalan, G Settanni, RJ Marsh, DA Armoogum, N Nicolaou, AJ Bain, E Lerner, E Haas, L Ying, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(2009)
106,
20758
(doi: 10.1073/pnas.0909644106)
Mechanistic differences in the transcriptional activation of p53 by 14-3-3 isoforms
S Rajagopalan, RS Sade, FM Townsley, AR Fersht
– Nucleic Acids Research
(2009)
38,
893
(doi: 10.1093/nar/gkp1041)
Direct observation of ultrafast folding and denatured state dynamics in single protein molecules
H Neuweiler, CM Johnson, AR Fersht
– Proceedings of the National Academy of Sciences
(2009)
106,
18569
(doi: 10.1073/pnas.0910860106)
Posttranslational Modifications Affect the Interaction of S100 Proteins with Tumor Suppressor p53
J van Dieck, DP Teufel, AM Jaulent, MR Fernandez-Fernandez, TJ Rutherford, A Wyslouch-Cieszynska, AR Fersht
– Journal of Molecular Biology
(2009)
394,
922
(doi: 10.1016/j.jmb.2009.10.002)
Structural evolution of p53, p63, and p73: Implication for heterotetramer formation
AC Joerger, S Rajagopalan, E Natan, DB Veprintsev, CV Robinson, AR Fersht
– Proceedings of the National Academy of Sciences
(2009)
106,
17705
(doi: 10.1073/pnas.0905867106)
Biophysical characterizations of human mitochondrial transcription factor A and its binding to tumor suppressor p53
TS Wong, S Rajagopalan, SM Freund, TJ Rutherford, A Andreeva, FM Townsley, M Petrovich, AR Fersht
– Nucleic Acids Res
(2009)
37,
6765
(doi: 10.1093/nar/gkp750)
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