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Yusuf Hamied Department of Chemistry

 

Professor Sir Alan Fersht FRS

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

Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the sites activity
WH Ward, AR Fersht
– Biochemistry
(2002)
27,
5525
(doi: 10.1021/bi00415a021)
Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains
S Vuilleumier, J Sancho, R Loewenthal, AR Fersht
– Biochemistry
(2002)
32,
10303
(doi: 10.1021/bi00090a005)
Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesis
FT Lau, AR Fersht
– Biochemistry
(2002)
28,
6841
(doi: 10.1021/bi00443a010)
Folding of subtilisin BPN': characterization of a folding intermediate.
J Eder, M Rheinnecker, AR Fersht
– Biochemistry
(2002)
32,
18
(doi: 10.1021/bi00052a004)
Stability and folding of the protein complexes of barnase
JL Neira, E Vázquez, AR Fersht
– Eur J Biochem
(2002)
267,
2859
(doi: 10.1046/j.1432-1327.2000.01290.x)
Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques.
MF Perutz, BJ Pope, D Owen, EE Wanker, E Scherzinger
– Proceedings of the National Academy of Sciences of the United States of America
(2002)
99,
5596
(doi: 10.1073/pnas.042681599)
Characterization of the p53-rescue drug CP-31398 in vitro and in living cells.
TM Rippin, VJN Bykov, SMV Freund, G Selivanova, KG Wiman, AR Fersht
– Oncogene
(2002)
21,
2119
(doi: 10.1038/sj.onc.1205362)
Characterization of the p53-rescue drug CP-31398 in vitro and in living cells
TM Rippin, VJN Bykov, SMV Freund, G Selivanova, KG Wiman, AR Fersht
– Oncogene
(2002)
21,
2119
(doi: 10.1038/sj/onc/1205362)
Max Ferdinand Perutz OM FRS - Obituary
AR Fersht
– NAT STRUCT BIOL
(2002)
9,
245
(doi: 10.1038/nsb0402-245)
Max Ferdinand Perutz OM FRS
AR Fersht
– Nature structural biology
(2002)
9,
245
(doi: 10.1038/nsb0402-245)
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