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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

Stability and folding of the tumour suppressor protein p16 1 1Edited by J. Karn
KS Tang, BJ Guralnick, WK Wang, AR Fersht, LS Itzhaki
– Journal of molecular biology
(1999)
285,
1869
Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments
JL Neira, AR Fersht
– Journal of Molecular Biology
(1999)
285,
1309
Analysis of protein–protein interactions by mutagenesis: direct versus indirect effects
DE Otzen, AR Fersht
– Protein Eng
(1999)
12,
41
Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2.
AG Ladurner, AR Fersht
– Nat Struct Biol
(1999)
6,
28
(doi: 10.1038/4899)
The FHA domain is a modular phosphopeptide recognition motif
D Durocher, J Henckel, AR Fersht, SP Jackson
– Molecular Cell
(1999)
4,
387
Minimal and optimal mechanisms for GroE-mediated protein folding.
AP Ben-Zvi, J Chatellier, AR Fersht, P Goloubinoff
– Proceedings of the National Academy of Sciences
(1998)
95,
15275
Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability
PV Nikolova, J Henckel, DP Lane, AR Fersht
– Proc Natl Acad Sci U S A
(1998)
95,
14675
Combined Molecular Dynamics and Φ-Value Analysis of Structure−Reactivity Relationships in the Transition State and Unfolding Pathway of Barnase:  Structural Basis of Hammond and Anti-Hammond Effects
V Daggett, AJ Li, AR Fersht
– Journal of the American Chemical Society
(1998)
120,
12740
In vivo activities of GroEL minichaperones
J Chatellier, F Hill, PA Lund, AR Fersht
– Proc Natl Acad Sci U S A
(1998)
95,
9861
Synergy between simulation and experiment in describing the energy landscape of protein folding.
AG Ladurner, LS Itzhaki, V Daggett, AR Fersht
– Proc Natl Acad Sci U S A
(1998)
95,
8473
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