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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Main Authors:	Nur Alia Oktaviani, Akimasa Matsugami, Ali D. Malay, Fumiaki Hayashi, David L. Kaplan, Keiji Numata
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-05-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-018-04570-5

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spelling	doaj-7dec962a6e3241d294a8b3fa08fe53222021-05-11T09:28:20ZengNature Publishing GroupNature Communications2041-17232018-05-019111110.1038/s41467-018-04570-5Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silkNur Alia Oktaviani0Akimasa Matsugami1Ali D. Malay2Fumiaki Hayashi3David L. Kaplan4Keiji Numata5Biomacromolecules Research Team, RIKEN Center for Sustainable Resource ScienceAdvanced NMR Application and Platform Team, NMR Research and Collaboration Group, NMR Science and Development Division, RIKEN SPring-8 Center, YokohamaBiomacromolecules Research Team, RIKEN Center for Sustainable Resource ScienceAdvanced NMR Application and Platform Team, NMR Research and Collaboration Group, NMR Science and Development Division, RIKEN SPring-8 Center, YokohamaDepartment of Biomedical Engineering, Tufts UniversityBiomacromolecules Research Team, RIKEN Center for Sustainable Resource Scienceβ-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.https://doi.org/10.1038/s41467-018-04570-5
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Nur Alia Oktaviani Akimasa Matsugami Ali D. Malay Fumiaki Hayashi David L. Kaplan Keiji Numata
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-05-01
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.
url	https://doi.org/10.1038/s41467-018-04570-5
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Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk

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