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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

The Transition State for Folding of a Peripheral Subunit-binding Domain Contains Robust and Ionic-strength Dependent Characteristics
N Ferguson, TD Sharpe, CM Johnson, AR Fersht
– Journal of Molecular Biology
(2005)
356,
1237
(doi: 10.1016/j.jmb.2005.12.016)
Analogues with Fluorescent Leaving Groups for Screening and Selection of Enzymes That Efficiently Hydrolyze Organophosphorus Nerve Agents
L Briseño-Roa, J Hill, S Notman, D Sellers, AP Smith, CM Timperley, J Wetherell, NH Williams, GR Williams, AR Fersht, AD Griffiths
– Journal of medicinal chemistry
(2005)
49,
246
(doi: 10.1021/jm050518j)
Ultra-fast Barrier-limited Folding in the Peripheral Subunit-binding Domain Family
N Ferguson, TD Sharpe, PJ Schartau, S Sato, MD Allen, CM Johnson, TJ Rutherford, AR Fersht
– Journal of molecular biology
(2005)
353,
427
(doi: 10.1016/j.jmb.2005.08.031)
Solution structure of a protein denatured state and folding intermediate
TL Religa, JS Markson, U Mayor, SMV Freund, AR Fersht
– Nature
(2005)
437,
1053
(doi: 10.1038/nature04054)
Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.
X Salvatella, CM Dobson, AR Fersht, M Vendruscolo
– Proc Natl Acad Sci U S A
(2005)
102,
12389
(doi: 10.1073/pnas.0408226102)
Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding
GWN White, S Gianni, JG Grossmann, P Jemth, AR Fersht, V Daggett
– J Mol Biol
(2005)
350,
757
(doi: 10.1016/j.jmb.2005.05.005)
The crystal structure of human CD1d with and without alpha-galactosylceramide
M Koch, VS Stronge, D Shepherd, SD Gadola, B Mathew, G Ritter, AR Fersht, GS Besra, RR Schmidt, EY Jones, V Cerundolo
– Nature immunology
(2005)
6,
819
(doi: 10.1038/ni1225)
The structure of the major transition state for folding of an FF domain from experiment and simulation
P Jemth, R Day, S Gianni, F Khan, M Allen, V Daggett, AR Fersht
– Journal of molecular biology
(2005)
350,
363
(doi: 10.1016/j.jmb.2005.04.067)
Comparative binding of p53 to its promoter and DNA recognition elements
RL Weinberg, DB Veprintsev, M Bycroft, AR Fersht
– Journal of molecular biology
(2005)
348,
589
(doi: 10.1016/j.jmb.2005.03.014)
Simulation and experiment at high temperatures: Ultrafast folding of a thermophilic protein by nucleation-condensation
N Ferguson, R Day, CM Johnson, MD Allen, V Daggett, AR Fersht
– J Mol Biol
(2005)
347,
855
(doi: 10.1016/j.jmb.2004.12.061)
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