title: The conserved C-termini contribute to the properties of spider silk fibroins.
abstract: Spider silk fibroins can adopt different structural states at high protein concentrations. They are soluble within the spinning dope of the glands, but readily converted into insoluble polymers upon extrusion. A contribution of the C-termini to the maintenance and conversion of these states is suggested by their predicted secondary structures and biochemical behavior in vitro. Special sequence parts endow the C-termini with the capability to promote both the solubility and aggregation of the fibroins depending on the environmental conditions.
authors.affiliation: Institute of Molecular Biotechnology and Leibniz Institute for Age Research-Fritz Lipmann Institute, Beutenbergstrasse 11, D-07745 Jena, Germany.
authors.forename: Alexander
authors.initials: A
authors.lastname: Sponner
authors.forename: Wolfram
authors.initials: W
authors.lastname: Vater
authors.forename: Winfried
authors.initials: W
authors.lastname: Rommerskirch
authors.forename: Fritz
authors.initials: F
authors.lastname: Vollrath
authors.forename: Eberhard
authors.initials: E
authors.lastname: Unger
authors.forename: Frank
authors.initials: F
authors.lastname: Grosse
authors.forename: Klaus
authors.initials: K
authors.lastname: Weisshart
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D005349:Fibroins / Q000032:analysis / Q000737:chemistry* / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D013112:Spiders / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D005349:Fibroins