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Cover Picture: Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water (Angew. Chem. Int. Ed. 27/2008)

Authors

  • Hai-Young Kim,

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
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  • Min-Kyu Cho,

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
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  • Dietmar Riedel Dr.,

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
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  • Claudio O. Fernandez Dr.,

    1. Instituto de Biología Molecular y Celular de Rosario, Universidad Nacional de Rosario, Suipacha 531, S2002 LRK Rosario (Argentina)
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  • Markus Zweckstetter Dr.

    1. Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany), Fax: (+49) 551-201-2202
    2. DFG Research Center for the Molecular Physiology of the Brain, 37077 Goettingen (Germany)
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Abstract

original image

Amyloid fibrils are filamentous aggregates of peptides and proteins with exceptional stability that are associated with several neurodegenerative diseases. M. Zweckstetter et al. demonstrate in their Communication on page 5046 ff. that amyloid fibrils formed by the protein α-synuclein, which is associated with Parkinson's disease, are rapidly denatured, that is, dissociated and lose the conformation of the constituent protein molecules, in supercooled water at −15 °C, conditions in which many globular proteins remain folded.

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