Issue 66, 2019

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

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

Supplementary files

Article information

Article type
Communication
Submitted
08 May 2019
Accepted
06 Jul 2019
First published
29 Jul 2019
This article is Open Access
Creative Commons BY license

Chem. Commun., 2019,55, 9761-9764

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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