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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

Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase.
EA First, AR Fersht
– Biochemistry
(2002)
32,
13658
(doi: 10.1021/bi00212a034)
recA Filaments in solution
SM COTTERILL, AR FERSHT
– Biochemistry
(2002)
22,
3525
(doi: 10.1021/bi00283a034)
Structure and dynamics of barnase complexed with 3'-GMP studied by NMR spectroscopy.
EM Meiering, M Bycroft, MJ Lubienski, AR Fersht
– Biochemistry
(2002)
32,
10975
(doi: 10.1021/bi00092a006)
Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis.
DE Mossakowska, K Nyberg, AR Fersht
– Biochemistry
(2002)
28,
3843
(doi: 10.1021/bi00435a033)
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis
AR Fersht
– Biochemistry
(2002)
26,
8031
(doi: 10.1021/bi00399a001)
Acyl-transfer reactions of amides and esters with alcohols and thiols. A reference system for the serine and cysteine proteinases. Concerning the N protonation of amides and amide-imidate equilibria.
AR Fersht
– J Am Chem Soc
(2002)
93,
3504
(doi: 10.1021/ja00743a035)
Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase.
FT Lau, AR Fersht, HW Hellinga, PR Evans
– Biochemistry
(2002)
26,
4143
(doi: 10.1021/bi00387a060)
Energetics of complementary side chain packing in a protein hydrophobic core
JT Kellis, K Nyberg, AR Fersht
– Biochemistry
(2002)
28,
4914
(doi: 10.1021/bi00437a058)
Use of binding energy in catalysis: optimization of rate in a multistep reaction.
JM Avis, AR Fersht
– Biochemistry
(2002)
32,
5321
(doi: 10.1021/bi00071a006)
Metal ion dependence of phosphorothioate ATP analogues in the Bacillus stearothermophilus tyrosyl-tRNA synthetase reaction.
GA Garcia, RJ Leatherbarrow, F Eckstein, AR Fersht
– Biochemistry
(2002)
29,
1643
(doi: 10.1021/bi00458a041)
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