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Amyloid self-assembly of hIAPP8-20 via the accumulation of helical oligomers, α-helix to β-sheet transition, and formation of β-barrel intermediates
Self-assembly of human islet amyloid polypeptide (hIAPP) into β-sheet rich nanofibrils is associated with the pathogeny of type 2 diabetes. Soluble hIAPP is intrinsically disordered with N-terminal residues 8-17 as α-helix. To understand the contribution of the N-terminal helix to the aggregation pr...
Tallennettuna:
| Julkaisussa: | Small |
|---|---|
| Päätekijät: | , , , , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2019
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6499678/ https://ncbi.nlm.nih.gov/pubmed/30908844 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/smll.201805166 |
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