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Physical basis of amyloid fibril polymorphism.
Nat. Commun. 9:699 (2018)
Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangement of a structurally conserved building block. A comparison with the theoretically possible constellations reveals the experimentally observed spectrum of fibril morphologies to be governed by opposing sets of forces that primarily arise from the beta-sheet twist, as well as peptide-peptide interactions within the fibril cross-section. Our results provide a framework for rationalizing and predicting the structure and polymorphism of cross-beta fibrils, and suggest that a small number of physical parameters control the observed fibril architectures.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Solid-state Nmr; Cryo-em; In-vivo; Beta; A-beta(1-40); Aggregation; Backbone; Sequence; Reveals; Disease
ISSN (print) / ISBN
2041-1723
e-ISSN
2041-1723
Journal
Nature Communications
Quellenangaben
Volume: 9,
Issue: 1,
Article Number: 699
Publisher
Nature Publishing Group
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)