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pH‐Dependent Dimerization and Salt‐Dependent Stabilization of the N‐terminal Domain of Spider Dragline Silk—Implications for Fiber Formation

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Citations

22

References

2010

Year

Abstract

One of the toughest protein fibers: The N-terminal domain (NTD) of spider dragline silk shows a pH-dependent monomer–dimer equilibrium: The N-terminal domain silk protein is stored as a stabilized monomer at neutral pH and high salt concentration, whereas during fiber assembly at a lower pH value this domain is able to form antiparallel dimers. Multivalent linking results in endless and highly stable fibers (see picture). Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.

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