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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

Direct observation of barrier-limited folding of BBL by single-molecule fluorescence resonance energy transfer.
F Huang, L Ying, AR Fersht
– Proc Natl Acad Sci U S A
(2009)
106,
16239
Effects of Stability on the Biological Function of p53*
KH Khoo, S Mayer, AR Fersht
– J Biol Chem
(2009)
284,
30974
Adaptive evolution of p53 thermodynamic stability.
KH Khoo, A Andreeva, AR Fersht
– J Mol Biol
(2009)
393,
161
Ultraslow oligomerization equilibria of p53 and its implications.
E Natan, D Hirschberg, N Morgner, CV Robinson, AR Fersht
– Proceedings of the National Academy of Sciences
(2009)
106,
14327
The accessory subunit of mitochondrial DNA polymerase γ determines the DNA content of mitochondrial nucleoids in human cultured cells
M Di Re, H Sembongi, J He, A Reyes, T Yasukawa, P Martinsson, LJ Bailey, S Goffart, JD Boyd-Kirkup, TS Wong, AR Fersht, JN Spelbrink, IJ Holt
– Nucleic Acids Research
(2009)
37,
5701
Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics
S Rajagopalan, A Andreeva, DP Teufel, SM Freund, AR Fersht
– The Journal of biological chemistry
(2009)
284,
21728
Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core
KH Khoo, AC Joerger, SMV Freund, AR Fersht
– Protein Engineering Design and Selection
(2009)
22,
421
The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family.
H Neuweiler, TD Sharpe, TJ Rutherford, CM Johnson, MD Allen, N Ferguson, AR Fersht
– Journal of molecular biology
(2009)
390,
1060
PRIMA-1 reactivates mutant p53 by covalent binding to the core domain.
JMR Lambert, P Gorzov, DB Veprintsev, M Söderqvist, D Segerbäck, J Bergman, AR Fersht, P Hainaut, KG Wiman, VJN Bykov
– Cancer Cell
(2009)
15,
376
Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2.
DP Teufel, M Bycroft, AR Fersht
– Oncogene
(2009)
28,
2112
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