Volume 47, Issue 27 p. 4939

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

Hai-Young Kim

Hai-Young Kim

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

Min-Kyu Cho

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.

Dietmar Riedel Dr.

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.

Claudio O. Fernandez Dr.

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.

Markus Zweckstetter Dr.

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

DFG Research Center for the Molecular Physiology of the Brain, 37077 Goettingen (Germany)

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First published: 16 June 2008

Graphical Abstract

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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