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Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph
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) exchan...
Tallennettuna:
| Julkaisussa: | PLoS One |
|---|---|
| Päätekijät: | , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Public Library of Science
2017
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5358797/ https://ncbi.nlm.nih.gov/pubmed/28319116 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0172862 |
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