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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

recA Filaments in solution
SM COTTERILL, AR FERSHT
– Biochemistry
(2002)
22,
3525
(doi: 10.1021/bi00283a034)
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-helices: perturbed pKas and protein stability.
J Sancho, L Serrano, AR Fersht
– Biochemistry
(2002)
31,
2253
(doi: 10.1021/bi00123a006)
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)
INTERNAL THERMODYNAMICS OF POSITION 51 MUTANTS AND NATURAL VARIANTS OF TYROSYL-TRANSFER RNA-SYNTHETASE
CK Ho, AR Fersht
– Biochemistry
(2002)
25,
1891
(doi: 10.1021/bi00356a009)
Role of phenylalanine-327 in the closure of loop 6 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum.
AG Day, P Chène, AR Fersht
– Biochemistry
(2002)
32,
1940
(doi: 10.1021/bi00059a009)
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)
Subunit interactions in the methionyl-tRNA synthetase of Bacillus stearothermophilus.
RS Mulvey, AR Fersht
– Biochemistry
(2002)
15,
243
(doi: 10.1021/bi00647a001)
pH dependence of chymotrypsin catalysis. Appendix: substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method.
AR Fersht, M Renard
– Biochemistry
(2002)
13,
1416
(doi: 10.1021/bi00704a016)
Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases
AR Fersht, JS Shindler, WC Tsui
– Biochemistry
(2002)
19,
5520
(doi: 10.1021/bi00565a009)
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