1H detection
amyloid β1-42
dynamic nuclear polarization
magic-angle spinning
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
04 01 2022
04 01 2022
Historique:
accepted:
03
11
2021
entrez:
31
12
2021
pubmed:
1
1
2022
medline:
5
3
2022
Statut:
ppublish
Résumé
Several publications describing high-resolution structures of amyloid-β (Aβ) and other fibrils have demonstrated that magic-angle spinning (MAS) NMR spectroscopy is an ideal tool for studying amyloids at atomic resolution. Nonetheless, MAS NMR suffers from low sensitivity, requiring relatively large amounts of samples and extensive signal acquisition periods, which in turn limits the questions that can be addressed by atomic-level spectroscopic studies. Here, we show that these drawbacks are removed by utilizing two relatively recent additions to the repertoire of MAS NMR experiments-namely,
Identifiants
pubmed: 34969859
pii: 2114413119
doi: 10.1073/pnas.2114413119
pmc: PMC8740738
pii:
doi:
Substances chimiques
Amyloid beta-Peptides
0
Peptide Fragments
0
amyloid beta-protein (1-42)
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM132079
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM132997
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG058504
Pays : United States
Informations de copyright
Copyright © 2021 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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