title: The mechanical design of spider silks: from fibroin sequence to mechanical function.
abstract: Spiders produce a variety of silks, and the cloning of genes for silk fibroins reveals a clear link between protein sequence and structure-property relationships. The fibroins produced in the spider's major ampullate (MA) gland, which forms the dragline and web frame, contain multiple repeats of motifs that include an 8-10 residue long poly-alanine block and a 24-35 residue long glycine-rich block. When fibroins are spun into fibres, the poly-alanine blocks form (&bgr;)-sheet crystals that crosslink the fibroins into a polymer network with great stiffness, strength and toughness. As illustrated by a comparison of MA silks from Araneus diadematus and Nephila clavipes, variation in fibroin sequence and properties between spider species provides the opportunity to investigate the design of these remarkable biomaterials.
authors.affiliation: Department of Zoology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4. gosline@zoology.ubc.ca
authors.forename: J M
authors.initials: JM
authors.lastname: Gosline
authors.forename: P A
authors.initials: PA
authors.lastname: Guerette
authors.forename: C S
authors.initials: CS
authors.lastname: Ortlepp
authors.forename: K N
authors.initials: KN
authors.lastname: Savage
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001696:Biomechanical Phenomena; D012831:Bombyx / Q000737:chemistry / Q000378:metabolism; D004548:Elasticity; D005349:Fibroins / Q000737:chemistry*; D019476:Insect Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D047011:Silk; D013112:Spiders / Q000737:chemistry / Q000378:metabolism*; D013718:Tensile Strength
chemical_list: D019476:Insect Proteins; D047011:Silk; D005349:Fibroins