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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

Characterizing transition states in protein folding: an essential step in the puzzle
AR Fersht
– Curr Opin Struct Biol
(1995)
5,
79
ASSOCIATION OF PROTEIN-FRAGMENTS THROUGH A 2ND-ORDER FOLDING REACTION - STRUCTURE OF THE ISOLATED FRAGMENTS AND EARLY EVENTS OF PROTEIN-FOLDING
GD GAV, J RUIZSANZ, B DAVIS, AR FERSHT
– PROTEIN ENGINEERING
(1995)
8,
19
Folding & Design: introduction to a new journal
AR Fersht, FE Cohen
– Folding & design
(1995)
1,
i
THE STRUCTURE OF THE TRANSITION-STATE FOR THE ASSOCIATION OF 2 FRAGMENTS OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 TO GENERATE NATIVE-LIKE PROTEIN - IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING
G de Prat Gay, J Ruiz-Sanz, B Davis, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1994)
91,
10943
STRUCTURE OF THE TRANSITION-STATE FOR THE FOLDING/UNFOLDING OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 AND ITS IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING
DE Otzen, LS Itzhaki, NF elMasry, SE Jackson, AR Fersht
– Proceedings of the National Academy of Sciences
(1994)
91,
10422
Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.
AR Fersht, LS Itzhaki, NF elMasry, JM Matthews, DE Otzen
– Proc Natl Acad Sci U S A
(1994)
91,
10426
Stability and function: two constraints in the evolution of barstar and other proteins
G Schreiber, AM Buckle, AR Fersht
– Structure (London, England : 1993)
(1994)
2,
945
Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state.
VL Arcus, S Vuilleumier, SM Freund, M Bycroft, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1994)
91,
9412
Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
A Matouschek, JM Matthews, CM Johnson, AR Fersht
– Protein Eng
(1994)
7,
1089
Mutational analysis of the N-capping box of the α-helix of chymotrypsin inhibitor 2
NF elMasry, AR Fersht
– Protein Eng
(1994)
7,
777
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