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...
Сохранить в:
| Опубликовано в:: | Proc Natl Acad Sci U S A |
|---|---|
| Главные авторы: | , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
National Academy of Sciences
2001
|
| Предметы: | |
| Online-ссылка: | 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 |
| Метки: |
Нет меток, Требуется 1-ая метка записи!
|