Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aß(1-42) amyloid polymorph
Wälti, Marielle A.
- Journal Article
Rights / licenseCreative Commons Attribution 4.0 International
Alzheimer’s disease is associated with the aggregation into amyloid fibrils of Aβ(1–42) and Aβ(1–40) peptides. Interestingly, these fibrils often do not obtain one single structure but rather show different morphologies, so-called polymorphs. Here, we compare quenched hydrogen-deuterium (H/D) exchange of a disease-relevant Aβ(1–42) fibril for which the 3D structure has been determined by solid-state NMR with H/D exchange previously determined on another structural polymorph. This comparison reveals secondary structural differences between the two polymorphs suggesting that the two polymorphisms can be classified as segmental polymorphs Show more
Journal / seriesPLoS ONE
Pages / Article No.
PublisherPublic Library of Science
Organisational unit03782 - Riek, Roland / Riek, Roland
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