skip to content
Home

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

Kinetic and thermodynamic properties of wild-type and engineered mutants of tyrosyl-tRNA synthetase analyzed by pyrophosphate-exchange kinetics
TN Wells, JW Knill-Jones, TE Gray, AR Fersht
– Biochemistry
(2002)
30,
5151
(doi: 10.1021/bi00235a006)
Acetylpyridinium ion intermediate in pyridine-catalyzed hydrolysis and acyl transfer reactions of acetic anhydride. Observation, kinetics, structure-reactivity correlations, and effects of concentrated salt solutions
AR FERSHT, WP JENCKS
– Journal of the American Chemical Society
(2002)
92,
5432
(doi: 10.1021/ja00721a023)
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)
Reaction of modified and unmodified tRNATyr substrates with tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
JM Avis, AG Day, GA Garcia, AR Fersht
– Biochemistry
(2002)
32,
5312
(doi: 10.1021/bi00071a005)
An editing mechanism for the methionyl-tRNA synthetase in the selection of amino acids in protein synthesis.
AR Fersht, C Dingwall
– Biochemistry
(2002)
18,
1250
(doi: 10.1021/bi00574a021)
Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis
AR Fersht
– Biochemistry
(2002)
27,
1577
(doi: 10.1021/bi00405a027)
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)
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)
Side-Chain Determinants of .beta.-Sheet Stability
DE Otzen, AR Fersht
– Biochemistry
(2002)
34,
5718
(doi: 10.1021/bi00017a003)
Free energies of hydrolysis of amides and peptides in aqueous solution at 25 degrees.
AR Fersht, Y Requena
– Journal of the American Chemical Society
(2002)
93,
3499
(doi: 10.1021/ja00743a034)
  • <
  • 26 of 66
  • >

    Study at Cambridge

    About the University

    Research at Cambridge