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Aβ(1–40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated
The ability of a single polypeptide sequence to grow into multiple stable amyloid fibrils sets these aggregates apart from most native globular proteins. The existence of multiple amyloid forms is the basis for strain effects in yeast prion biology, and may also contribute to variations in Alzheimer...
Gorde:
| Egile Nagusiak: | , , , |
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| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
2010
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| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2919579/ https://ncbi.nlm.nih.gov/pubmed/20600131 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2010.06.023 |
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