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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

Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease.
J Carmichael, J Chatellier, A Woolfson, C Milstein, AR Fersht, DC Rubinsztein
– Proceedings of the National Academy of Sciences of the United States of America
(2000)
97,
9701
Protein folding transition states: elicitation of Hammond effects by 2,2,2-trifluoroethanol.
CP Yiu, MG Mateu, AR Fersht
– Chembiochem : a European journal of chemical biology
(2000)
1,
49
Stabilization of GroEL minichaperones by core and surface mutations
Q Wang, AM Buckle, AR Fersht
– Journal of Molecular Biology
(2000)
298,
917
Fast-folding proteins.
AR Fersht
– ABSTR PAP AM CHEM S
(2000)
219,
U283
Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding
KB Wong, J Clarke, CJ Bond, JL Neira, SM Freund, AR Fersht, V Daggett
– Journal of Molecular Biology
(2000)
296,
1257
Characterization of in vitro oxidized barstar
C Frisch, G Schreiber, AR Fersht
– FEBS letters
(2000)
370,
273
Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy
AN Bullock, J Henckel, AR Fersht
– Oncogene
(2000)
19,
1245
Untitled
JM Lehn, AR Fersht
– EUROPEAN JOURNAL OF INORGANIC CHEMISTRY
(2000)
A80
Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase.
M Ibba, CM Johnson, H Hennecke, AR Fersht
– FEBS letters
(2000)
358,
293
Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.
AR Fersht
– Proc Natl Acad Sci U S A
(2000)
97,
1525
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