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

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.