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.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Rising A,Hjälm G,Engström W,Johansson Jdoi
10.1021/bm060693xsubject
Has Abstractpub_date
2006-11-01 00:00:00pages
3120-4issue
11eissn
1525-7797issn
1526-4602journal_volume
7pub_type
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