Molecular and mechanical properties of major ampullate silk of the black widow spider, Latrodectus hesperus.
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.
Lawrence
Barbara A
BA
Department of Chemistry, Eastern Illinois University, Charleston, Illinois 61920, USA. cfball@eiu.edu
Vierra
Craig A
CA
Moore
Anne M F
AM
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001740:Black Widow Spider / Q000737:chemistry*; D017931:DNA Primers; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D047011:Silk / Q000737:chemistry*
D017931:DNA Primers; D047011:Silk