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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

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.
CK Vaughan, P Harryson, AM Buckle, AR Fersht
– Acta Crystallogr D Biol Crystallogr
(2002)
58,
591
(doi: 10.1107/s0907444902001567)
Protein folding and unfolding at atomic resolution
AR Fersht, V Daggett
– Cell
(2002)
108,
573
(doi: 10.1016/S0092-8674(02)00620-7)
Cooperativity in ATP hydrolysis by GroEL is increased by GroES.
TE Gray, AR Fersht
– FEBS Lett
(2002)
292,
254
(doi: 10.1016/0014-5793(91)80878-7)
Folding of the yeast prion protein Ure2: Kinetic evidence for folding and unfolding intermediates
D Galani, AR Fersht, S Perrett
– Journal of Molecular Biology
(2002)
315,
213
(doi: 10.1006/jmbi.2001.5234)
A peptide that binds and stabilizes p53 core domain:: Chaperone strategy for rescue of oncogenic mutants
A Friedler, LO Hansson, DB Veprintsev, SMV Freund, TM Rippin, PV Nikolova, MR Proctor, S Rüdiger, AR Fersht
– Proc Natl Acad Sci U S A
(2002)
99,
937
(doi: 10.1073/pnas.241629998)
Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type
SL Kazmirski, RL Isaacson, C An, A Buckle, CM Johnson, V Daggett, AR Fersht
– Nature Structural & Molecular Biology
(2002)
9,
112
(doi: 10.1038/nsb745)
New Look and New Outlook
WA Hendrickson, CI Branden, AR Fersht
– Structure
(2002)
10,
1
(doi: 10.1016/s0969-2126(01)00704-3)
Measurement of barnase refolding rate constants under denaturing conditions.
JM Sanz, AR Fersht
– FEBS Letters
(2001)
344,
216
(doi: 10.1016/0014-5793(94)00384-X)
Hydrolysis of small peptide substrates parallels binding of chymotrypsin inhibitor 2 for mutants of subtilisin BPN'.
J Eder, M Rheinnecker, AR Fersht
– FEBS Lett
(2001)
335,
349
(doi: 10.1016/0014-5793(93)80417-S)
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)
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