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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

Editing mechanisms in aminoacylation of tRNA: ATP consumption and the binding of aminoacyl-tRNA by elongation factor Tu.
RS Mulvey, AR Fersht
– Biochemistry
(2002)
16,
4731
(doi: 10.1021/bi00640a031)
ANALYSIS OF THE MECHANISM OF ASSEMBLY OF CLEAVED BARNASE FROM 2 PEPTIDE-FRAGMENTS AND ITS RELEVANCE TO THE FOLDING PATHWAY OF UNCLEAVED BARNASE
AD Kippen, AR Fersht
– Biochemistry
(2002)
34,
1464
(doi: 10.1021/bi00004a042)
Rationally designing the accumulation of a folding intermediate of barnase by protein engineering
JM Sanz, AR Fersht
– Biochemistry
(2002)
32,
13584
(doi: 10.1021/bi00212a026)
Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetase.
EA First, AR Fersht
– Biochemistry
(2002)
32,
13644
(doi: 10.1021/bi00212a032)
Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases
AR Fersht, JS Ashford, CJ Bruton, R Jakes, GL Koch, BS Hartley
– Biochemistry
(2002)
14,
1
(doi: 10.1021/bi00672a001)
SEQUENTIAL ASSIGNMENT OF THE H-1 NUCLEAR-MAGNETIC-RESONANCE SPECTRUM OF BARNASE
M Bycroft, RN Sheppard, FT Lau, AR Fersht
– Biochemistry
(2002)
29,
7425
(doi: 10.1021/bi00484a011)
Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence
R Loewenthal, J Sancho, AR Fersht
– Biochemistry
(2002)
30,
6775
(doi: 10.1021/bi00241a021)
Engineering a novel specificity in subtilisin BPN'.
M Rheinnecker, G Baker, J Eder, AR Fersht
– Biochemistry
(2002)
32,
1199
(doi: 10.1021/bi00056a001)
Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity.
SE Jackson, AR Fersht
– Biochemistry
(2002)
33,
13880
(doi: 10.1021/bi00250a042)
Folding of subtilisin BPN': characterization of a folding intermediate.
J Eder, M Rheinnecker, AR Fersht
– Biochemistry
(2002)
32,
18
(doi: 10.1021/bi00052a004)
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