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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

Variants of subtilisin BPN' with altered specificity profiles
M Rheinnecker, J Eder, PS Pandey, AR Fersht
– Biochemistry
(2002)
33,
221
(doi: 10.1021/bi00167a029)
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)
Detection of an intermediate in the folding of the (beta alpha)8-barrel N-(5'-phosphoribosyl)anthranilate isomerase from Escherichia coli.
A Jasanoff, B Davis, AR Fersht
– Biochemistry
(2002)
33,
6350
(doi: 10.1021/bi00186a039)
Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and half-of-the-sites reactivity in aminoacylation
R Jakes, AR Fersht
– Biochemistry
(2002)
14,
3344
(doi: 10.1021/bi00686a009)
Investigation of transition-state stabilization by residues histidine-45 and threonine-40 in the tyrosyl-tRNA synthetase
RJ Leatherbarrow, AR Fersht
– Biochemistry
(2002)
26,
8524
(doi: 10.1021/bi00400a005)
Mechanism of the -chymotrypsin-catalyzed hydrolysis of specific amide substrates.
AR Fersht
– J Am Chem Soc
(2002)
94,
293
(doi: 10.1021/ja00756a061)
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis
AR Fersht
– Biochemistry
(2002)
26,
8031
(doi: 10.1021/bi00399a001)
Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy.
M Bycroft, S Ludvigsen, AR Fersht, FM Poulsen
– Biochemistry
(2002)
30,
8697
(doi: 10.1021/bi00099a030)
Engineered Disulfide Bonds as Probes of the Folding Pathway of Barnase: Increasing the Stability of Proteins against the Rate of Denaturation
J Clarke, AR Fersht
– Biochemistry
(2002)
32,
4322
(doi: 10.1021/bi00067a022)
Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the alpha-ammonium group binding site of tyrosyl-tRNA synthetase.
DM Lowe, G Winter, AR Fersht
– Biochemistry
(2002)
26,
6038
(doi: 10.1021/bi00393a014)
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