Titelangaben
    
    Eisoldt, Lukas ; Thamm, Christopher ; Scheibel, Thomas:
The role of terminal domains during storage and assembly of spider silk proteins.
  
   
    
    In: Biopolymers.
      
      Bd. 97
      
      (2012)
       Heft  6
    .
     - S. 355-361.
    
    
ISSN 1097-0282
    
    
      
DOI: https://doi.org/10.1002/bip.22006
    
    
    
     
  
  
Abstract
Fibrous proteins in nature fulfill a wide variety of functions in different structures ranging from cellular scaffolds to very resilient structures like tendons and even extra-corporal fibers such as silks in spider webs or silkworm cocoons. Despite their different origins and sequence varieties many of these fibrous proteins share a
common building principle: they consist of a large repetitive core domain flanked by relatively small nonrepetitive terminal domains. Amongst protein fibers, spider dragline silk shows prominent mechanical properties that exceed those of man-made fibers like Kevlar. Spider silk fibers assemble in a spinning process allowing the transformation from an aqueous solution into a solid fiber within milliseconds. Here, we highlight the role of the non-repetitive terminal domains of spider dragline silk proteins during storage in the gland and initiation of the fiber assembly process.
        
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