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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

CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90
S Rudiger, SMV Freund, DB Veprintsev, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(2002)
99,
11085
Two sequence motifs from HIF-1α bind to the DNA-binding site of p53
LO Hansson, A Friedler, S Freund, S Rudiger, AR Fersht
– Proceedings of the National Academy of Sciences
(2002)
99,
10305
Recognition of DNA by p53 Core Domain and Location of Intermolecular Contacts of Cooperative Binding
TM Rippin, SMV Freund, DB Veprintsev, AR Fersht
– Journal of molecular biology
(2002)
319,
351
Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold (Retraction of vol 403, pg 617, 2000)
MM Altamirano, JM Blackburn, C Aguayo, AR Fersht
– NATURE
(2002)
417,
468
Correction: retraction: Directed evolution of new catalytic activity using the α/β-barrel scaffold
MM Altamirano, JM Blackburn, C Aguayo, AR Fersht
– Nature
(2002)
417,
468
Mechanism of the -chymotrypsin-catalyzed hydrolysis of specific amide substrates.
AR Fersht
– Journal of the American Chemical Society
(2002)
94,
293
pH dependence of chymotrypsin catalysis. Appendix: substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method.
AR Fersht, M Renard
– Biochemistry
(2002)
13,
1416
Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases.
AR Fersht, JS Ashford, CJ Bruton, R Jakes, GL Koch, BS Hartley
– Biochemistry
(2002)
14,
1
Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases.
AR Fersht, JS Shindler, WC Tsui
– Biochemistry
(2002)
19,
5520
Structural Studies on Peptides Corresponding to Mutants of the Major .alpha.-Helix of Barnase
AD Kippen, VL Arcus, AR Fersht
– Biochemistry
(2002)
33,
10013
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