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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

Pathway and Stability of Protein Folding
AR Fersht
– Biochem Soc Trans
(1994)
22,
267
(doi: 10.1042/bst0220267)
Pathway and Stability of Protein Folding
AR FERSHT
– Biochemical Society Transactions
(1994)
22,
267
(doi: 10.1042/bst0220267)
Editorial overview
AR FERSHT, KA DILL
– Current Opinion in Structural Biology
(1994)
4,
67
(doi: 10.1016/S0959-440X(94)90061-2)
Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue.
Y Harpaz, N Elmasry, AR Fersht, K Henrick
– Proc Natl Acad Sci U S A
(1994)
91,
311
(doi: 10.1073/pnas.91.1.311)
CONTRIBUTION OF A PROLINE RESIDUE AND A SALT BRIDGE TO THE STABILITY OF A TYPE-I REVERSE TURN IN CHYMOTRYPSIN INHIBITOR-2
G de Prat Gay, CM Johnson, AR Fersht
– Protein Eng
(1994)
7,
103
(doi: 10.1093/protein/7.1.103)
Contribution of Buried Hydrogen Bonds to Protein Stability The Crystal Structures of Two Barnase Mutants
YW Chen, AR Fersht, K Henrick
– Journal of Molecular Biology
(1993)
234,
1158
(doi: 10.1006/jmbi.1993.1667)
Crystal structural analysis of mutations in the hydrophobic cores of barnase.
AM Buckle, K Henrick, AR Fersht
– Journal of Molecular Biology
(1993)
234,
847
(doi: 10.1006/jmbi.1993.1630)
Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.
J Clarke, AM Hounslow, M Bycroft, AR Fersht
– Proceedings of the National Academy of Sciences of the United States of America
(1993)
90,
9837
(doi: 10.1073/pnas.90.21.9837)
Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.
TE Gray, J Eder, M Bycroft, AG Day, AR Fersht
– The EMBO journal
(1993)
12,
4145
(doi: 10.1002/j.1460-2075.1993.tb06098.x)
THE REFOLDING OF CIS-PEPTIDYLPROLYL AND TRANS-PEPTIDYLPROLYL ISOMERS OF BARSTAR
G SCHREIBER, AR FERSHT
– BIOCHEMISTRY-US
(1993)
32,
11195
(doi: 10.1021/bi00092a032)
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