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Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires
Amyloid-like fibrils from a number of small peptides that are unrelated by sequence adopt a cross-β-spine in which the two sheets fully interdigitate to create a dry interface. Formation of such a dry interface is usually associated with self-assembly of extended hydrophobic surfaces. Here we invest...
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| Autors principals: | , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
National Academy of Sciences
2010
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3003024/ https://ncbi.nlm.nih.gov/pubmed/21098298 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1008616107 |
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