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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7dec962a6e3241d294a8b3fa08fe5322
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id	oai:doaj.org-article:7dec962a6e3241d294a8b3fa08fe5322
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spelling	oai:doaj.org-article:7dec962a6e3241d294a8b3fa08fe53222021-12-02T14:41:27ZConformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk10.1038/s41467-018-04570-52041-1723https://doaj.org/article/7dec962a6e3241d294a8b3fa08fe53222018-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04570-5https://doaj.org/toc/2041-1723β-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.Nur Alia OktavianiAkimasa MatsugamiAli D. MalayFumiaki HayashiDavid L. KaplanKeiji NumataNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Nur Alia Oktaviani Akimasa Matsugami Ali D. Malay Fumiaki Hayashi David L. Kaplan Keiji Numata Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
description	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.
format	article
author	Nur Alia Oktaviani Akimasa Matsugami Ali D. Malay Fumiaki Hayashi David L. Kaplan Keiji Numata
author_facet	Nur Alia Oktaviani Akimasa Matsugami Ali D. Malay Fumiaki Hayashi David L. Kaplan Keiji Numata
author_sort	Nur Alia Oktaviani
title	Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
title_short	Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
title_full	Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
title_fullStr	Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
title_full_unstemmed	Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
title_sort	conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/7dec962a6e3241d294a8b3fa08fe5322
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Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk

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