The role of terminal domains during storage and assembly of spider silk proteins

Authors

  • Lukas Eisoldt,

    1. Universität Bayreuth, Fakultät für Angewandte Naturwissenschaften, Lehrstuhl Biomaterialien, Universitätsstraße 30, Bayreuth 95447, Germany
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  • Christopher Thamm,

    1. Universität Bayreuth, Fakultät für Angewandte Naturwissenschaften, Lehrstuhl Biomaterialien, Universitätsstraße 30, Bayreuth 95447, Germany
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  • Thomas Scheibel

    Corresponding author
    1. Universität Bayreuth, Fakultät für Angewandte Naturwissenschaften, Lehrstuhl Biomaterialien, Universitätsstraße 30, Bayreuth 95447, Germany
    • Universität Bayreuth, Fakultät für Angewandte Naturwissenschaften, Lehrstuhl Biomaterialien, Universitätsstraße 30, Bayreuth 95447, Germany
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  • This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

Abstract

Fibrous proteins in nature fulfill a wide variety of functions in different structures ranging from cellular scaffolds to very resilient structures like tendons and even extra-corporal fibers such as silks in spider webs or silkworm cocoons. Despite their different origins and sequence varieties many of these fibrous proteins share a common building principle: they consist of a large repetitive core domain flanked by relatively small non-repetitive terminal domains. Amongst protein fibers, spider dragline silk shows prominent mechanical properties that exceed those of man-made fibers like Kevlar. Spider silk fibers assemble in a spinning process allowing the transformation from an aqueous solution into a solid fiber within milliseconds. Here, we highlight the role of the non-repetitive terminal domains of spider dragline silk proteins during storage in the gland and initiation of the fiber assembly process. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 355–361, 2012.

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