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The role of terminal domains during storage and assembly of spider silk proteins
Author(s) -
Eisoldt Lukas,
Thamm Christopher,
Scheibel Thomas
Publication year - 2012
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22006
Subject(s) - spider silk , silk , spider , fiber , polymer science , chemistry , kevlar , terminal (telecommunication) , storage protein , biophysics , nanotechnology , microbiology and biotechnology , materials science , biology , computer science , composite material , biochemistry , ecology , epoxy , organic chemistry , telecommunications , gene
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.