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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

Interfaces: two worlds unite.
J-M Lehn, AR Fersht
– Chembiochem : a European journal of chemical biology
(2008)
10,
4
Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p53
TS Wong, S Rajagopalan, FM Townsley, SM Freund, M Petrovich, D Loakes, AR Fersht
– Nucleic Acids Research
(2008)
37,
568
Structure of Human MDM4 N-Terminal Domain Bound to a Single-Domain Antibody
GW Yu, M Vaysburd, MD Allen, G Settanni, AR Fersht
– Journal of molecular biology
(2008)
385,
1578
Structural biology of the tumor suppressor p53.
AC Joerger, AR Fersht
– Annual Review of Biochemistry
(2008)
77,
557
14-3-3 activation of DNA binding of p53 by enhancing its association into tetramers
S Rajagopalan, AM Jaulent, M Wells, DB Veprintsev, AR Fersht
– Nucleic Acids Res
(2008)
36,
5983
PHYS 27-Experimental resolution of the early events in the folding of B domain of Protein A
DM Vu, SH Brewer, S Sato, AR Fersht, RB Dyer
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2008)
236,
Members of the S100 family bind p53 in two distinct ways.
MR Fernandez-Fernandez, TJ Rutherford, AR Fersht
– Protein Sci
(2008)
17,
1663
A Sequential Assignment Procedure for Proteins that have Intermediate Line Widths in MAS NMR Spectra: Amyloid Fibrils of Human CA150.WW2
J Becker, N Ferguson, J Flinders, B-J van Rossum, AR Fersht, H Oschkinat
– Chembiochem
(2008)
9,
1946
Targeted rescue of a destabilized mutant of p53 by an in silico screened drug
FM Boeckler, AC Joerger, G Jaggi, TJ Rutherford, DB Veprintsev, AR Fersht
– Proceedings of the National Academy of Sciences
(2008)
105,
10360
The novel p53 isoform “delta p53” is a misfolded protein and does not bind the p21 promoter site
MM García-Alai, H Tidow, E Natan, FM Townsley, DB Veprintsev, AR Fersht
– Protein Sci
(2008)
17,
1671
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