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N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins.
Biomacromolecules 2006; 7(11):3120-4B

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.

Authors+Show Affiliations

Department of Biomedical Sciences and Veterinary Public Health, Swedish University of Agricultural Sciences, SE-750 07 Uppsala, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17096540

Citation

Rising, Anna, et al. "N-terminal Nonrepetitive Domain Common to Dragline, Flagelliform, and Cylindriform Spider Silk Proteins." Biomacromolecules, vol. 7, no. 11, 2006, pp. 3120-4.
Rising A, Hjälm G, Engström W, et al. N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins. Biomacromolecules. 2006;7(11):3120-4.
Rising, A., Hjälm, G., Engström, W., & Johansson, J. (2006). N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins. Biomacromolecules, 7(11), pp. 3120-4.
Rising A, et al. N-terminal Nonrepetitive Domain Common to Dragline, Flagelliform, and Cylindriform Spider Silk Proteins. Biomacromolecules. 2006;7(11):3120-4. PubMed PMID: 17096540.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins. AU - Rising,Anna, AU - Hjälm,Göran, AU - Engström,Wilhelm, AU - Johansson,Jan, PY - 2006/11/14/pubmed PY - 2007/1/6/medline PY - 2006/11/14/entrez SP - 3120 EP - 4 JF - Biomacromolecules JO - Biomacromolecules VL - 7 IS - 11 N2 - 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. SN - 1525-7797 UR - https://www.unboundmedicine.com/medline/citation/17096540/N_terminal_nonrepetitive_domain_common_to_dragline_flagelliform_and_cylindriform_spider_silk_proteins_ L2 - https://dx.doi.org/10.1021/bm060693x DB - PRIME DP - Unbound Medicine ER -