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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

Crystal Structures of Engrailed Homeodomain Mutants
EJ Stollar, U Mayor, SC Lovell, L Federici, SMV Freund, AR Fersht, BF Luisi
– Journal of Biological Chemistry
(2003)
278,
43699
Rapid amyloid fiber formation from the fast-folding WW domain FBP28
N Ferguson, J Berriman, M Petrovich, TD Sharpe, JT Finch, AR Fersht
– Proceedings of the National Academy of Sciences
(2003)
100,
9814
Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity.
AC Joerger, S Mayer, AR Fersht
– Proc Natl Acad Sci U S A
(2003)
100,
5694
Kinetic Instability of p53 Core Domain Mutants IMPLICATIONS FOR RESCUE BY SMALL MOLECULES*
A Friedler, DB Veprintsev, LO Hansson, AR Fersht
– The Journal of biological chemistry
(2003)
278,
24108
The complete folding pathway of a protein from nanoseconds to microseconds.
U Mayor, NR Guydosh, CM Johnson, JG Grossmann, S Sato, GS Jas, SMV Freund, DOV Alonso, V Daggett, AR Fersht
– Nature
(2003)
421,
863
Early events in protein folding.
N Ferguson, AR Fersht
– Current Opinion in Structural Biology
(2003)
13,
75
Is there a unifying mechanism for protein folding?
V Daggett, AR Fersht
– Trends in biochemical sciences
(2003)
28,
18
Sequential unfolding of ankyrin repeats in tumor suppressor p16.
KS Tang, AR Fersht, LS Itzhaki
– Structure
(2003)
11,
67
Molecular mechanism of the interaction between MDM2 and p53
O Schon, A Friedler, M Bycroft, SMV Freund, AR Fersht
– J Mol Biol
(2002)
323,
491
On the simulation of protein folding by short time scale molecular dynamics and distributed computing
AR Fersht
– Proceedings of the National Academy of Sciences
(2002)
99,
14122
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