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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

Pathways of protein folding
AR Fersht
– PROG BIOPHYS MOL BIO
(1996)
65,
SA401
Folding & design: Introduction to a new journal
AR Fersht, FE Cohen
– FOLD DES
(1996)
1,
U7
Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism.
JL Neira, B Davis, AG Ladurner, AM Buckle, GDP Gay, AR Fersht
– Structure
(1996)
1,
189
An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway.
J Clarke, AR Fersht
– Structure
(1996)
1,
243
Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activity.
FJ Corrales, AR Fersht
– Structure
(1996)
1,
265
Perturbed pKA-values in the denatured states of proteins.
YJ Tan, M Oliveberg, B Davis, AR Fersht
– Journal of molecular biology
(1995)
254,
980
CONFORMATIONAL PATHWAY OF THE POLYPEPTIDE-CHAIN OF CHYMOTRYPSIN INHIBITOR-2 GROWING FROM ITS N-TERMINUS IN-VITRO - PARALLELS WITH THE PROTEIN-FOLDING PATHWAY
G de Prat Gay, J Ruiz-Sanz, JL Neira, FJ Corrales, DE Otzen, AG Ladurner, AR Fersht
– Journal of Molecular Biology
(1995)
254,
968
Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.
LS Itzhaki, JL Neira, J Ruiz-Sanz, G de Prat Gay, AR Fersht
– Journal of Molecular Biology
(1995)
254,
289
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
LS Itzhaki, DE Otzen, AR Fersht
– Journal of molecular biology
(1995)
254,
260
A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding
VL Arcus, S Vuilleumier, SM Freund, M Bycroft, AR Fersht
– Journal of Molecular Biology
(1995)
254,
305
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