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Yusuf Hamied Department of Chemistry

 

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

Protein-protein recognition: Crystal structural analysis of a barnase-barstar complex at 2.0-.ANG. resolution
AM Buckle, G Schreiber, AR Fersht
– Biochemistry
(2002)
33,
8878
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism
AR Fersht, JW Knill-Jones, H Bedouelle, G Winter
– Biochemistry
(2002)
27,
1581
Movement of the position of the transition state in protein folding
A Matouschek, DE Otzen, LS Itzhaki, SE Jackson, AR Fersht
– Biochemistry
(2002)
34,
13656
Backbone Dynamics of Chymotrypsin Inhibitor 2: Effect of Breaking the Active Site Bond and Its Implications for the Mechanism of Inhibition of Serine Proteases
GL Shaw, B Davis, J Keeler, AR Fersht
– Biochemistry
(2002)
34,
2225
Stability and folding of the protein complexes of barnase.
JL Neira, E Vázquez, AR Fersht
– Eur J Biochem
(2002)
267,
2859
Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques.
MF Perutz, BJ Pope, D Owen, EE Wanker, E Scherzinger
– Proceedings of the National Academy of Sciences of the United States of America
(2002)
99,
5596
Characterization of the p53-rescue drug CP-31398 in vitro and in living cells.
TM Rippin, VJN Bykov, SMV Freund, G Selivanova, KG Wiman, AR Fersht
– Oncogene
(2002)
21,
2119
Characterization of the p53-rescue drug CP-31398 in vitro and in living cells
TM Rippin, VJN Bykov, SMV Freund, G Selivanova, KG Wiman, AR Fersht
– Oncogene
(2002)
21,
2119
Max Ferdinand Perutz OM FRS
AR Fersht
– Nat Struct Biol
(2002)
9,
245
Max Ferdinand Perutz OM FRS - Obituary
AR Fersht
– NATURE STRUCTURAL BIOLOGY
(2002)
9,
245
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