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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

Nature and Consequences of GroEL-Protein Interactions
LS Itzhaki, DE Otzen, AR Fersht
– Biochemistry
(2002)
34,
14581
(doi: 10.1021/bi00044a037)
Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis.
SE Jackson, N elMasry, AR Fersht
– Biochemistry
(2002)
32,
11270
(doi: 10.1021/bi00093a002)
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)
Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow technique
AR Fersht, R Jakes
– Biochemistry
(2002)
14,
3350
(doi: 10.1021/bi00686a010)
Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes
AR Fersht
– Biochemistry
(2002)
14,
5
(doi: 10.1021/bi00672a002)
Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase
FT Lau, AR Fersht, HW Hellinga, PR Evans
– Biochemistry
(2002)
26,
4143
(doi: 10.1021/bi00387a060)
Intramolecular nucleophilic catalysis in the hydrolysis of substituted aspirin acids.
AR Fersht, AJ Kirby
– J Am Chem Soc
(2002)
90,
5826
(doi: 10.1021/ja01023a029)
Establishing the misacylation/deacylation of the tRNA pathway for the editing mechanism of prokaryotic and eukaryotic valyl-tRNA synthetases
AR Fersht, C Dingwall
– Biochemistry
(2002)
18,
1238
(doi: 10.1021/bi00574a019)
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)
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
SE Jackson, AR Fersht
– Biochemistry
(2002)
30,
10428
(doi: 10.1021/bi00107a010)
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