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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

Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.
MM Altamirano, JM Blackburn, C Aguayo, AR Fersht
– Nature
(2000)
403,
617
(doi: 10.1038/35001001)
Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold (Retracted article. See vol 417, pg 468, 2002)
MM Altamirano, JM Blackburn, C Aguayo, AR Fersht
– Nature
(2000)
403,
617
(doi: 10.1038/35001001)
Mechanism of rescue of common p53 cancer mutations by second‐site suppressor mutations
PV Nikolova, KB Wong, B DeDecker, J Henckel, AR Fersht
– The EMBO Journal
(2000)
19,
370
(doi: 10.1093/emboj/19.3.370)
Interdomain interactions within the gene 3 protein of filamentous phage.
J Chatellier, O Hartley, AD Griffiths, AR Fersht, G Winter, L Riechmann
– FEBS Lett
(2000)
463,
371
(doi: 10.1016/s0014-5793(99)01658-0)
Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis–Finnish type
RL Isaacson, AG Weeds, AR Fersht
– Proc Natl Acad Sci U S A
(1999)
96,
11247
(doi: 10.1073/pnas.96.20.11247)
Formation of short-lived protein aggregates directly from the coil in two-state folding.
M Silow, YJ Tan, AR Fersht, M Oliveberg
– Biochemistry
(1999)
38,
13006
(doi: 10.1021/bi9909997)
Identification of substrate binding site of GroEL minichaperone in solution 1 1 Edited by J. Karn
N Tanaka, AR Fersht
– Journal of Molecular Biology
(1999)
292,
173
(doi: 10.1006/jmbi.1999.3041)
NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution 1 1Edited by J. Karn
N Kobayashi, SM Freund, J Chatellier, R Zahn, AR Fersht
– Journal of Molecular Biology
(1999)
292,
181
(doi: 10.1006/jmbi.1999.3042)
GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices1 1Edited by J. Karn
J Chatellier, AM Buckle, AR Fersht
– Journal of Molecular Biology
(1999)
292,
163
(doi: 10.1006/jmbi.1999.3040)
The FHA domain is a modular phosphopeptide recognition motif.
D Durocher, J Henckel, AR Fersht, SP Jackson
– Molecular Cell
(1999)
4,
387
(doi: 10.1016/s1097-2765(00)80340-8)
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