| Literature DB >> 16253207 |
Alexander Sponner1, Wolfram Vater, Winfried Rommerskirch, Fritz Vollrath, Eberhard Unger, Frank Grosse, Klaus Weisshart.
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.Mesh：
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Year: 2005 PMID： 16253207 DOI： 10.1016/j.bbrc.2005.10.048
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575