Titelangaben
Eisoldt, Lukas ; Thamm, Christopher ; Scheibel, Thomas:
The role of terminal domains during storage and assembly of spider silk proteins.
In: Biopolymers.
Bd. 97
(2012)
Heft 6
.
- S. 355-361.
ISSN 1097-0282
DOI: https://doi.org/10.1002/bip.22006
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 nonrepetitive 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.