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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

Protein folding and stability: the pathway of folding of barnase
AR FERSHT
– FEBS Letters
(2001)
325,
5
(doi: 10.1016/0014-5793(93)81405-o)
Modification of the amino acid specificity of tyrosyl‐tRNA synthetase by protein engineering
G de Prat Gay, HW Duckworth, AR Fersht
– FEBS letters
(2001)
318,
167
(doi: 10.1016/0014-5793(93)80014-l)
Ultrafast folding of WW domains without structured aromatic clusters in the denatured state.
N Ferguson, CM Johnson, M Macias, H Oschkinat, A Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(2001)
98,
13002
(doi: 10.1073/pnas.221467198)
Using flexible loop mimetics to extend Phi-value analysis to secondary structure interactions
N Ferguson, JR Pires, F Toepert, CM Johnson, YP Pan, R Volkmer-Engert, J Schneider-Mergener, V Daggett, H Oschkinat, A Fersht
– Proc Natl Acad Sci U S A
(2001)
98,
13008
(doi: 10.1073/pnas.221467398)
Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen-deuterium exchange.
DN Jones, M Bycroft, MJ Lubienski, AR Fersht
– FEBS letters
(2001)
331,
165
(doi: 10.1016/0014-5793(93)80319-p)
Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar.
MJ Lubienski, M Bycroft, DN Jones, AR Fersht
– FEBS Letters
(2001)
332,
81
(doi: 10.1016/0014-5793(93)80489-h)
The catalytic activity of the inactive conformation of δ‐chymotrypsin
AR Fersht
– FEBS letters
(2001)
29,
283
(doi: 10.1016/0014-5793(73)80039-0)
Stability and solvation of Thr/Ser to Ala and Gly mutations at the N‐cap of α‐helices
YW Chen, AR Fersht
– FEBS Letters
(2001)
347,
304
(doi: 10.1016/0014-5793(94)00574-5)
Rescuing the function of mutant p53.
AN Bullock, AR Fersht
– Nature reviews. Cancer
(2001)
1,
68
(doi: 10.1038/35094077)
[Folding mechanism and folding rate].
T Ikura, AR Fersht
– Protein (Tokyo)
(2001)
46,
1553
(link to publication)
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