Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk

Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk

β-sheet structure underlies the mechanical properties of spider silk but the mechanism to form β-sheet from soluble silk protein during transition into insoluble fibers has not been elucidated. Here the authors unravel the mechanism of β-sheet formation using NMR and circular dichroism spectroscopy....

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Autores principales: Nur Alia Oktaviani, Akimasa Matsugami, Ali D. Malay, Fumiaki Hayashi, David L. Kaplan, Keiji Numata
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
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Science
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Acceso en línea:https://doaj.org/article/7dec962a6e3241d294a8b3fa08fe5322
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