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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

Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks11Edited by J. Karn
CM Johnson, M Oliveberg, J Clarke, AR Fersht
– Journal of molecular biology
(1997)
268,
198
Following co-operative formation of secondary and tertiary structure in a single protein module11Edited by J. Karn
JL Neira, LS Itzhaki, AG Ladurner, B Davis, G de Prat Gay, AR Fersht
– Journal of Molecular Biology
(1997)
268,
185
A structural model for GroEL-polypeptide recognition.
AM Buckle, R Zahn, AR Fersht
– Proc Natl Acad Sci U S A
(1997)
94,
3571
Refolding chromatography with immobilized mini-chaperones
MM Altamirano, R Golbik, R Zahn, AM Buckle, AR Fersht
– Proc Natl Acad Sci U S A
(1997)
94,
3576
Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli11Edited by K. Nagai
V Gopalan, R Golbik, G Schreiber, AR Fersht, S Altman
– Journal of Molecular Biology
(1997)
267,
765
Thermodynamics of the interaction of barnase and barstar: Changes in free energy versus changes in enthalpy on mutation
C Frisch, G Schreiber, CM Johnson, AR Fersht
– J Mol Biol
(1997)
267,
696
Role of Isoleucine-164 at the Active Site of Rubisco fromRhodospirillum rubrum
P Chène, AG Day, AR Fersht
– Biochem Biophys Res Commun
(1997)
232,
482
The folding pathway of a protein at high resolution from microseconds to seconds
B Nölting, R Golbik, JL Neira, AS Soler-Gonzalez, G Schreiber, AR Fersht
– Proceedings of the National Academy of Sciences
(1997)
94,
826
Nucleation mechanisms in protein folding
AR Fersht
– Current Opinion in Structural Biology
(1997)
7,
3
Preface
CM DOBSON, AR FERSHT
– Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(1997)
348,
3
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