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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

Reversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface
DH Jones, AJ McMillan, AR Fersht, G Winter
– Biochemistry
(2002)
24,
5852
(doi: 10.1021/bi00342a024)
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)
Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue.
G de Prat Gay, AR Fersht
– Biochemistry
(2002)
33,
7957
(doi: 10.1021/bi00191a024)
Anomalous pH dependence of kcat-KM in enzyme reactions. Rate constants for the association of chymotrypsin with substrates.
M Renard, AR Fersht
– Biochemistry
(2002)
12,
4713
(doi: 10.1021/bi00747a026)
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)
Folding of Chymotrypsin Inhibitor 2.1. Evidence for a Two-State Transition
SE Jackson, AR Fersht
– Biochemistry
(2002)
30,
10428
(doi: 10.1021/bi00107a010)
Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
SE Jackson, AR Fersht
– Biochemistry
(2002)
30,
10436
(doi: 10.1021/bi00107a011)
Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase.
AR Fersht
– Biochemistry
(2002)
16,
1025
(doi: 10.1021/bi00624a034)
Quantitative determination of helical propensities from trifluoroethanol titration curves.
A Jasanoff, AR Fersht
– Biochemistry
(2002)
33,
2129
(doi: 10.1021/bi00174a020)
Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering.
G Schreiber, AR Fersht
– Biochemistry
(2002)
32,
5145
(doi: 10.1021/bi00070a025)
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