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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

Assignment of histidine resonances in the 1H NMR (500 MHz) spectrum of subtilisin BPN' using site-directed mutagenesis.
M Bycroft, AR Fersht
– Biochemistry
(2002)
27,
7390
(doi: 10.1021/bi00419a033)
Folding of Chymotrypsin Inhibitor 2.1. Evidence for a Two-State Transition
SE Jackson, AR Fersht
– Biochemistry
(2002)
30,
10428
(doi: 10.1021/bi00107a010)
Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin
MF Perutz, AR Fersht, SR Simon, GC Roberts
– Biochemistry
(2002)
13,
2174
(doi: 10.1021/bi00707a027)
Rationally designing the accumulation of a folding intermediate of barnase by protein engineering
JM Sanz, AR Fersht
– Biochemistry
(2002)
32,
13584
(doi: 10.1021/bi00212a026)
Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetase.
EA First, AR Fersht
– Biochemistry
(2002)
32,
13644
(doi: 10.1021/bi00212a032)
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)
Engineering a novel specificity in subtilisin BPN'
M Rheinnecker, G Baker, J Eder, AR Fersht
– Biochemistry
(2002)
32,
1199
(doi: 10.1021/bi00056a001)
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)
Exploring the Energy Surface of Protein Folding by Structure-Reactivity Relationships and Engineered Proteins: Observation of Ftammond Behavior for the Gross Structure of the Transition State and Anti-Hammond Behavior for Structural Elements for Unfolding/Folding of Bamase
JM Matthews, AR Fersht
– Biochemistry
(2002)
34,
6805
(doi: 10.1021/bi00020a027)
Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity.
SE Jackson, AR Fersht
– Biochemistry
(2002)
33,
13880
(doi: 10.1021/bi00250a042)
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