Molecular studies of a novel dragline silk from a nursery web spider, Euprosthenops sp. (Pisauridae).
Various spider species produce dragline silks with different mechanical properties. The primary structure of silk proteins is thought to contribute to the elasticity and strength of the fibres. Previously published work has demonstrated that the dragline silk of Euprosthenops sp. is stiffer then comparable silk of Nephila edulis, Araneus diadematus and Latrodectus mactans. Our studies of Euprosthenops dragline silk at the molecular level have revealed that nursery web spider fibroin has the highest polyalanine content among previously characterised silks and this is likely to contribute to the superior qualities of pisaurid dragline.
Institute of Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, UK.
Natalia N
NN
Pouchkina-Stantcheva
Simon J
SJ
McQueen-Mason
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry; D018076:DNA, Complementary / Q000378:metabolism; D019992:Databases as Topic; D005349:Fibroins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D047011:Silk / Q000737:chemistry*; D013045:Species Specificity; D013112:Spiders
D018076:DNA, Complementary; D010455:Peptides; D047011:Silk; C019529:polyalanine; D004247:DNA; D005349:Fibroins