Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10767881 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
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.
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Authors
Alexander Sponner, Wolfram Vater, Winfried Rommerskirch, Fritz Vollrath, Eberhard Unger, Frank Grosse, Klaus Weisshart,