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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

Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate
PA Dalby, J Clarke, CM Johnson, AR Fersht
– J Mol Biol
(1998)
276,
647
Folding intermediates of wild-type and mutants of barnase.: I.: Use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium
PA Dalby, M Oliveberg, AR Fersht
– J Mol Biol
(1998)
276,
625
Real‐time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2
TR Killick, SM Freund, AR Fersht
– FEBS Lett
(1998)
423,
110
Thermodynamic stability and folding of GroEL minichaperones11Edited by P. E. Wright
R Golbik, R Zahn, SE Harding, AR Fersht
– Journal of molecular biology
(1998)
276,
505
Folding and binding - overview
E Shakhnovich, AR Fersht
– Current Opinion in Structural Biology
(1998)
8,
65
A reply to Englander and Woodward
J Clarke, LS Itzhaki, AR Fersht
– Trends in Biochemical Sciences
(1998)
23,
379
Thermodynamic stability of wild-type and mutant p53 core domain
AN Bullock, J Henckel, BS DeDecker, CM Johnson, PV Nikolova, MR Proctor, DP Lane, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1997)
94,
14338
Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathway
CJ Bond, KB Wong, J Clarke, AR Fersht, V Daggett
– Proceedings of the National Academy of Sciences of the United States of America
(1997)
94,
13409
Strain in the transition state of folding and in the native state of proteins
A Ladurner, L Itzhaki, A Fersht
– Protein Engineering
(1997)
10,
29
Folding of barnase in the presence of the molecular chaperone SecB.
G Stenberg, AR Fersht
– J Mol Biol
(1997)
274,
268
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