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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

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
Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates.
AG Ladurner, AR Fersht
– Journal of Molecular Biology
(1997)
273,
330
Circular Dichroism of Denatured Barstar Suggests Residual Structure,
B Nölting, R Golbik, AS Soler-González, AR Fersht
– Biochemistry
(1997)
36,
9899
The role of Glu73 of barnase in catalysis and the binding of barstar
G Schreiber, C Frisch, AR Fersht
– Journal of Molecular Biology
(1997)
270,
111
Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature
LS Itzhaki, JL Neira, AR Fersht
– Journal of molecular biology
(1997)
270,
89
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
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 2
YJ Tan, M Oliveberg, DE Otzen, AR Fersht
– Journal of molecular biology
(1997)
269,
611
Nonsequential Unfolding of the α/β Barrel Protein Indole-3-glycerol-phosphate Synthase †
MM Sánchez del Pino, AR Fersht
– Biochemistry
(1997)
36,
5560
NMR 15 N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A 1 1Edited by P. E. Wright
KB Wong, AR Fersht, SM Freund
– J Mol Biol
(1997)
268,
494
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