An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid
X-ray diffraction and other biophysical tools reveal features of the atomic structure of an amyloid-like crystal. Sup35, a prion-like protein in yeast, forms fibrillar amyloid assemblies intrinsic to its prion function. We have identified a polar peptide from the N-terminal prion-determining domain...
Tallennettuna:
| Julkaisussa: | Proc Natl Acad Sci U S A |
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| Päätekijät: | , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
2001
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC30146/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11226247/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.041617698 |
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