title: Review the role of terminal domains during storage and assembly of spider silk proteins.
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.
authors: Universität Bayreuth, Fakultät für Angewandte Naturwissenschaften, Lehrstuhl Biomaterialien, Universitätsstraße 30, Bayreuth 95447, Germany.
authors: Lukas
authors: L
authors: Eisoldt
authors: Christopher
authors: C
authors: Thamm
authors: Thomas
authors: T
authors: Scheibel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000502:physiology; D005349:Fibroins / Q000737:chemistry* / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013112:Spiders / Q000502:physiology*
chemical_list: D008823:Micelles; D005349:Fibroins