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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

Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
YJ Tan, M Oliveberg, AR Fersht
– Journal of Molecular Biology
(1996)
264,
377
Initiation sites of protein folding by NMR analysis
SM Freund, KB Wong, AR Fersht
– Proc Natl Acad Sci U S A
(1996)
93,
10600
Mechanism of the molecular chaperone GroEL.
AR Fersht
– ABSTR PAP AM CHEM S
(1996)
212,
1
Conformational states bound by the molecular chaperones GroEL and SecB: A hidden unfolding (annealing) activity
R Zahn, S Perrett, AR Fersht
– Journal of Molecular Biology
(1996)
261,
43
Kinetic significance of GroEL14ยท(GroES7)2 complexes in molecular chaperone activity
FJ Corrales, AR Fersht
– Folding and Design
(1996)
1,
265
Mechanism of the molecular chaperone GroEL.
AR Fersht
– BIOCHEMISTRY-US
(1996)
35,
1
Cold denaturation of barstar: H-1, N-15 and C-13 NMR assignment and characterisation of residual structure
KB Wong, SM Freund, AR Fersht
– Journal of Molecular Biology
(1996)
259,
805
Active barnase variants with completely random hydrophobic cores.
DD Axe, NW Foster, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1996)
93,
5590
A new approach to the study of transient protein conformations: The formation of a semiburied salt link in the folding pathway of barnase
M Oliveberg, AR Fersht
– Biochemistry
(1996)
35,
6795
Importance of two buried salt bridges in the stability and folding pathway of barnase
AC Tissot, S Vuilleumier, AR Fersht
– Biochemistry
(1996)
35,
6786
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