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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

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)
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)
Side-chain determinants of beta-sheet stability.
DE Otzen, AR Fersht
– Biochemistry
(2002)
34,
5718
(doi: 10.1021/bi00017a003)
Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
J Clarke, AR Fersht
– Biochemistry
(2002)
32,
4322
(doi: 10.1021/bi00067a022)
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism
AR Fersht, JW Knill-Jones, H Bedouelle, G Winter
– Biochemistry
(2002)
27,
1581
(doi: 10.1021/bi00405a028)
pKA Values of Carboxyl Groups in the Native and Denatured States of Barnase: The pKA Values of the Denatured State Are on Average 0.4 Units Lower Than Those of Model Compounds
M Oliveberg, VL Arcus, AR Fersht
– Biochemistry
(2002)
34,
9424
(doi: 10.1021/bi00029a018)
Protein Stability as a Function of Denaturant Concentration: The Thermal Stability of Barnase in the Presence of Urea
CM Johnson, AR Fersht
– Biochemistry
(2002)
34,
6795
(doi: 10.1021/bi00020a026)
ASSIGNMENT OF HISTIDINE RESONANCES IN THE H-1-NMR (500 MHZ) SPECTRUM OF SUBTILISIN BPN' USING SITE-DIRECTED MUTAGENESIS
M Bycroft, AR Fersht
– Biochemistry
(2002)
27,
7390
(doi: 10.1021/bi00419a033)
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