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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.

Original publication




Journal article


Biochem Biophys Res Commun

Publication Date





897 - 902


Amino Acid Sequence, Animals, Binding Sites, Conserved Sequence, Fibroins, Molecular Sequence Data, Molecular Weight, Protein Binding, Sequence Homology, Amino Acid, Spiders, Structure-Activity Relationship