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Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils
Amyloid fibril deposits observed in Alzheimer's disease comprise amyloid-β (Aβ) protein possessing a structured hydrophobic core and a disordered N-terminal domain (residues 1–16). The internal flexibility of the disordered domain is likely essential for Aβ aggregation. Here, we used (2)H stati...
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| Publicado no: | J Biol Chem |
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| Main Authors: | , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Biochemistry and Molecular Biology
2019
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6463690/ https://ncbi.nlm.nih.gov/pubmed/30737281 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.006559 |
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