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Conformational Distribution and α-Helix to β-Sheet Transition of Human Amylin Fragment Dimer
Experiments suggested that the fibrillation of the 11–25 fragment (hIAPP(11–25)) of human islet amyloid polypeptide (hIAPP or amylin) involves the formation of transient α-helical intermediates, followed by conversion to β-sheet-rich structure. However, atomic details of α-helical intermediates and...
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| Vydáno v: | Biomacromolecules |
|---|---|
| Hlavní autoři: | , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2013
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6429924/ https://ncbi.nlm.nih.gov/pubmed/24313776 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bm401406e |
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