Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study

Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study

The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer and molecular scales. Various fibril growth conditions have been identified to cause polymorphism, but the intrinsic amino acid sequence basis for this polymorphism has been unclear. Several singl...

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Main Authors: Nick, Mimi (Author), Jo, Hyunil (Author), Lemmin, Thomas (Author), Prusiner, Stanley B. (Author), DeGrado, William F. (Author), Stöhr, Jan (Author), Elkins, Matthew Ryan (Contributor), Wang, Tuo (Contributor), Hong, Mei (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Chemical Engineering (Contributor)
Format: Article
Language:English
Published: American Chemical Society (ACS), 2018-01-29T15:38:47Z.
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