Thread: NMR paper Quenched hydrogen-deuterium exchange NMR of a disease-relevant A?(1-42) amyloid polymorph.
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Default Quenched hydrogen-deuterium exchange NMR of a disease-relevant A?(1-42) amyloid polymorph.
Quenched hydrogen-deuterium exchange NMR of a disease-relevant A?(1-42) amyloid polymorph.

Related Articles Quenched hydrogen-deuterium exchange NMR of a disease-relevant A?(1-42) amyloid polymorph.

PLoS One. 2017;12(3):e0172862

Authors: Wälti MA, Orts J, Riek R

Abstract
Alzheimer's disease is associated with the aggregation into amyloid fibrils of A?(1-42) and A?(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 A?(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.


PMID: 28319116 [PubMed - indexed for MEDLINE]



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