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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

Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates11Edited by J. Karn
AG Ladurner, AR Fersht
– Journal of Molecular Biology
(1997)
273,
330
Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2.
AG Ladurner, LS Itzhaki, G de Prat Gay, AR Fersht
– Journal of molecular biology
(1997)
273,
317
Circular dichroism of denatured barstar suggests residual structure
B Nölting, R Golbik, AS Soler-González, AR Fersht
– Biochemistry
(1997)
36,
9899
Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis
JL Neira, LS Itzhaki, DE Otzen, B Davis, AR Fersht
– Journal of molecular biology
(1997)
270,
99
The role of Glu73 of barnase in catalysis and the binding of barstar
G Schreiber, C Frisch, AR Fersht
– J Mol Biol
(1997)
270,
111
Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature11Edited by J. Karn
LS Itzhaki, JL Neira, AR Fersht
– J Mol Biol
(1997)
270,
89
Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
S Perrett, R Zahn, G Stenberg, AR Fersht
– Journal of Molecular Biology
(1997)
269,
892
The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 211Edited by J. Karn
YJ Tan, M Oliveberg, DE Otzen, AR Fersht
– J Mol Biol
(1997)
269,
611
Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase.
MM Sánchez del Pino, AR Fersht
– Biochemistry
(1997)
36,
5560
NMR N-15 relaxation and structural studies reveal slow conformational exchange in Barstar C40/82A
KB Wong, AR Fersht, SM Freund
– Journal of Molecular Biology
(1997)
268,
494
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