Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different

Amyloid polymorphism of twisted and straight β-endorphin fibrils was studied by negative-stain transmission electron microscopy, scanning transmission electron microscopy, and solid-state nuclear magnetic resonance spectroscopy. Whereas fibrils assembled in the presence of salt formed flat, striated...

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Veröffentlicht in:	The journal of physical chemistry. B 2017-03, Vol.121 (8), p.1783-1792
Hauptverfasser:	Seuring, Carolin, Verasdonck, Joeri, Ringler, Philippe, Cadalbert, Riccardo, Stahlberg, Henning, Böckmann, Anja, Meier, Beat H, Riek, Roland
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyloid - chemistry Amyloid - ultrastructure Analytical chemistry Atomic structure beta-Endorphin - chemistry Chemical Sciences Fingerprints Flats (landforms) Humans Microscopy, Electron, Scanning Transmission Molecular structure Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Polymorphism Protein Multimerization Protein Structure, Secondary Ribbons Sodium Chloride - chemistry Spectra
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