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

Nature Communications
Nur Alia OktavianiKeiji Numata

Abstract

The β-sheet is the key structure underlying the excellent mechanical properties of spider silk. However, the comprehensive mechanism underlying β-sheet formation from soluble silk proteins during the transition into insoluble stable fibers has not been elucidated. Notably, the assembly of repetitive domains that dominate the length of the protein chains and structural features within the spun fibers has not been clarified. Here we determine the conformation and dynamics of the soluble precursor of the repetitive domain of spider silk using solution-state NMR, far-UV circular dichroism and vibrational circular dichroism. The soluble repetitive domain contains two major populations: ~65% random coil and ~24% polyproline type II helix (PPII helix). The PPII helix conformation in the glycine-rich region is proposed as a soluble prefibrillar region that subsequently undergoes intramolecular interactions. These findings unravel the mechanism underlying the initial step of β-sheet formation, which is an extremely rapid process during spider silk assembly.

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Citations

Aug 4, 2018·Macromolecular Rapid Communications·Meghan McGillDavid L Kaplan
Sep 20, 2018·Macromolecular Bioscience·Kenjiro YazawaKeiji Numata
Jan 16, 2020·Scientific Reports·Axel AbeleinHenrik Biverstål
Jul 1, 2020·Nature Chemical Biology·Shao-Peng WeiXiao-Xia Xia
Jul 15, 2021·ACS Biomaterials Science & Engineering·Chun-Fei HuXiao-Xia Xia
Jun 10, 2019·ACS Biomaterials Science & Engineering·Yingjie HangDavid L Kaplan
Jan 20, 2021·ACS Biomaterials Science & Engineering·Vladimir G Debabov, Vladimir G Bogush
Jan 19, 2021·ACS Biomaterials Science & Engineering·Noy Cohen, Claus D Eisenbach

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Datasets Mentioned

BETA
M37137.2

Methods Mentioned

BETA
NMR
X-ray
circular
circular dichroism
electrophoresis

Software Mentioned

SPARKY
ncSPC
NMRPipe

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