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

Nur Alia Oktaviani; Akimasa Matsugami; Ali D. Malay; Fumiaki Hayashi; David L. Kaplan; Keiji Numata

doi:10.1038/s41467-018-04570-5

Nature Communications (May 2018)

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

Nur Alia Oktaviani,
Akimasa Matsugami,
Ali D. Malay,
Fumiaki Hayashi,
David L. Kaplan,
Keiji Numata

Affiliations

Nur Alia Oktaviani: Biomacromolecules Research Team, RIKEN Center for Sustainable Resource Science
Akimasa Matsugami: Advanced NMR Application and Platform Team, NMR Research and Collaboration Group, NMR Science and Development Division, RIKEN SPring-8 Center, Yokohama
Ali D. Malay: Biomacromolecules Research Team, RIKEN Center for Sustainable Resource Science
Fumiaki Hayashi: Advanced NMR Application and Platform Team, NMR Research and Collaboration Group, NMR Science and Development Division, RIKEN SPring-8 Center, Yokohama
David L. Kaplan: Department of Biomedical Engineering, Tufts University
Keiji Numata: Biomacromolecules Research Team, RIKEN Center for Sustainable Resource Science

DOI: https://doi.org/10.1038/s41467-018-04570-5
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 11

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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