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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

Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'
SE Jackson, AR Fersht
– Biochemistry
(2002)
32,
13909
(doi: 10.1021/bi00213a021)
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)
Fine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase.
AR Fersht, AJ Wilkinson, P Carter, G Winter
– Biochemistry
(2002)
24,
5858
(doi: 10.1021/bi00342a025)
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)
Quantitative Determination of Helical Propensities from Trifluoroethanol Titration Curves
A Jasanoff, AR Fersht
– Biochemistry
(2002)
33,
2129
(doi: 10.1021/bi00174a020)
Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains
S Vuilleumier, J Sancho, R Loewenthal, AR Fersht
– Biochemistry
(2002)
32,
10303
(doi: 10.1021/bi00090a005)
Movement of the position of the transition state in protein folding
A Matouschek, DE Otzen, LS Itzhaki, SE Jackson, AR Fersht
– Biochemistry
(2002)
34,
13656
(doi: 10.1021/bi00041a047)
Correlations between kinetic and x-ray analyses of engineered enzymes: crystal structures of mutants Cys.fwdarw.Gly-35 and Tyr.fwdarw.Phe-34 of tyrosyl-tRNA synthetase
MD Fothergill, AR Fersht
– Biochemistry
(2002)
30,
5157
(doi: 10.1021/bi00235a007)
Folding of barnase in parts.
AD Kippen, J Sancho, AR Fersht
– Biochemistry
(2002)
33,
3778
(doi: 10.1021/bi00178a039)
Histidine residues at the N- and C-termini of .alpha.-helixes: perturbed pKas and protein stability
J Sancho, L Serrano, AR Fersht
– Biochemistry
(2002)
31,
2253
(doi: 10.1021/bi00123a006)
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