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Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus.
Biomacromolecules 2004 May-Jun; 5(3):689-95B

Abstract

Molecular and material properties of major ampullate silk were studied for the cobweb-building black widow spider Latrodectus hesperus. Material properties were measured by stretching the silk to breaking. The strength was 1.0 +/- 0.2 GPa, and the extensibility was 34 +/- 8%. The secondary structure of the major ampullate silk protein was studied using carbon-13 NMR spectroscopy. Alanine undergoes a transition from a coiled structure in pre-spun silk to a beta sheet structure in post-spun silk. We have also isolated two distinct cDNAs (both about 500 bp) which encode proteins similar to major ampullate spidroin 1 and 2 (MaSp1 and MaSp2). The MaSp1-like silk contains polyalanine runs of 5-10 residues as well as GA and GGX motifs. The MaSp2-like silk contains polyalanine runs of varying length as well as GPG(X)(n) motifs. L. hesperus major ampullate silk is more like major ampullate silk from other species than other L. hesperus silks.

Authors+Show Affiliations

Department of Chemistry, Eastern Illinois University, Charleston, Illinois 61920, USA. cfball@eiu.eduNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

15132648

Citation

Lawrence, Barbara A., et al. "Molecular and Mechanical Properties of Major Ampullate Silk of the Black Widow Spider, Latrodectus Hesperus." Biomacromolecules, vol. 5, no. 3, 2004, pp. 689-95.
Lawrence BA, Vierra CA, Moore AM. Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus. Biomacromolecules. 2004;5(3):689-95.
Lawrence, B. A., Vierra, C. A., & Moore, A. M. (2004). Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus. Biomacromolecules, 5(3), pp. 689-95.
Lawrence BA, Vierra CA, Moore AM. Molecular and Mechanical Properties of Major Ampullate Silk of the Black Widow Spider, Latrodectus Hesperus. Biomacromolecules. 2004;5(3):689-95. PubMed PMID: 15132648.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus. AU - Lawrence,Barbara A, AU - Vierra,Craig A, AU - Moore,Anne M F, PY - 2004/5/11/pubmed PY - 2005/2/9/medline PY - 2004/5/11/entrez SP - 689 EP - 95 JF - Biomacromolecules JO - Biomacromolecules VL - 5 IS - 3 N2 - Molecular and material properties of major ampullate silk were studied for the cobweb-building black widow spider Latrodectus hesperus. Material properties were measured by stretching the silk to breaking. The strength was 1.0 +/- 0.2 GPa, and the extensibility was 34 +/- 8%. The secondary structure of the major ampullate silk protein was studied using carbon-13 NMR spectroscopy. Alanine undergoes a transition from a coiled structure in pre-spun silk to a beta sheet structure in post-spun silk. We have also isolated two distinct cDNAs (both about 500 bp) which encode proteins similar to major ampullate spidroin 1 and 2 (MaSp1 and MaSp2). The MaSp1-like silk contains polyalanine runs of 5-10 residues as well as GA and GGX motifs. The MaSp2-like silk contains polyalanine runs of varying length as well as GPG(X)(n) motifs. L. hesperus major ampullate silk is more like major ampullate silk from other species than other L. hesperus silks. SN - 1525-7797 UR - https://www.unboundmedicine.com/medline/citation/15132648/Molecular_and_mechanical_properties_of_major_ampullate_silk_of_the_black_widow_spider_Latrodectus_hesperus_ L2 - https://dx.doi.org/10.1021/bm0342640 DB - PRIME DP - Unbound Medicine ER -