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Issue 66, 2019
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Ion effects on the conformation and dynamics of repetitive domains of a spider silk protein: implications for solubility and β-sheet formation

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Abstract

The effect of ions on the structure and dynamics of a spider silk protein is elucidated. Chaotropic ions prevent intra- and inter-molecular interactions on the repetitive domain, which are required to maintain the solubility, while kosmotropic ions promote hydrogen bond interactions in the glycine-rich region, which are a prerequisite for β-sheet formation.

Graphical abstract: Ion effects on the conformation and dynamics of repetitive domains of a spider silk protein: implications for solubility and β-sheet formation

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Publication details

The article was received on 08 May 2019, accepted on 06 Jul 2019 and first published on 29 Jul 2019


Article type: Communication
DOI: 10.1039/C9CC03538A
Chem. Commun., 2019,55, 9761-9764
  • Open access: Creative Commons BY license
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    Ion effects on the conformation and dynamics of repetitive domains of a spider silk protein: implications for solubility and β-sheet formation

    N. A. Oktaviani, A. Matsugami, F. Hayashi and K. Numata, Chem. Commun., 2019, 55, 9761
    DOI: 10.1039/C9CC03538A

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