The conserved C-termini contribute to the properties of spider silk fibroins.
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.
Sponner
Alexander
A
Institute of Molecular Biotechnology and Leibniz Institute for Age Research-Fritz Lipmann Institute, Beutenbergstrasse 11, D-07745 Jena, Germany.
Vater
Wolfram
W
Rommerskirch
Winfried
W
Vollrath
Fritz
F
Unger
Eberhard
E
Grosse
Frank
F
Weisshart
Klaus
K
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
D005349:Fibroins