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Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations
Aβ amyloid fibrils, which are related to Alzheimer’s disease, have a cross-β structure consisting of two β-sheets: β1 and β2. The Aβ peptides are thought to be serially arranged in the same molecular conformation along the fibril axis. However, to understand the amyloid extension mechanism, we must...
| Autores principales: | , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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Nature Publishing Group
2016
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5146922/ https://www.ncbi.nlm.nih.gov/pubmed/27934893 http://dx.doi.org/10.1038/srep38422 |