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The conserved C-termini contribute to the properties of spider silk fibroins |
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| Authors: | Sponner Alexander Vater Wolfram Rommerskirch Winfried Vollrath Fritz Unger Eberhard Grosse Frank Weisshart Klaus |
| Affiliation: | Institute of Molecular Biotechnology and Leibniz Institute for Age Research-Fritz Lipmann Institute, Beutenbergstrasse 11, D-07745 Jena, Germany. |
| 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. |
| Keywords: | Spider fibroins Spidroins Structural proteins Secondary structure predictions Atomic force microscopy |
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