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Cover Picture: Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water (Angew. Chem. Int. Ed. 27/2008)
Article first published online: 16 JUN 2008
DOI: 10.1002/anie.200890127
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Kim, H.-Y., Cho, M.-K., Riedel, D., Fernandez, Claudio O. and Zweckstetter, M. (2008), Cover Picture: Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water (Angew. Chem. Int. Ed. 27/2008). Angew. Chem. Int. Ed., 47: 4939. doi: 10.1002/anie.200890127
Publication History
- Issue published online: 16 JUN 2008
- Article first published online: 16 JUN 2008
Keywords:
- α-synuclein;
- amyloid fibrils;
- electron microscopy;
- NMR spectroscopy;
- proteins
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.