Abstract

Spider silk has been extensively studied for its outstanding mechanical properties. Partial intermediate and C-terminal sequences of different spider silk proteins have been determined, and during the past decade also N-terminal domains have been characterized. However, only some of these N-terminal domains have been reported to contain signal peptides, leaving the mechanism whereby they enter the secretory pathway open to speculation. Here we present the sequence of a 394-residue N-terminal region of the Euprosthenops australis major ampullate spidroin 1 ( MaSp1). A close comparison with published sequences from other species revealed the presence of N-terminal signal peptides followed by an approximately 130-residue nonrepetitive domain. From secondary structure predictions, helical wheel analysis, and circular dichroism spectroscopy this domain is concluded to contain five alpha-helices and is a conserved constituent of hitherto analyzed dragline, flagelliform, and cylindriform spider silk proteins

Published in

Biomacromolecules
2006, Volume: 7, number: 11, pages: 3120-3124
Publisher: AMER CHEMICAL SOC

SLU Authors

• Engström, Wilhelm

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

• Johansson, Jan

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

• Rising, Anna

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Animal and Dairy Science
Veterinary Science


Publication identifier

DOI: https://doi.org/10.1021/bm060693x

Permanent link to this page (URI)

https://res.slu.se/id/publ/10560