title: Short and long range order of the morphology of silk from Latrodectus hesperus (Black Widow) as characterized by atomic force microscopy.
abstract: The surfaces of both stretched and unstretched silk threads from the cobweb weaver, Latrodectus hesperus (Black Widow) have been examined by atomic force microscopy (AFM). AFM images of cobweb scaffolding threads show both unordered and highly ordered regions. Two types of fibers within the threads were observed: thicker (approximately 300 nm in diameter) fibers oriented parallel to the thread axis and thinner (10-100 nm) fibrils oriented across the thread axis. While regions which lacked parallel fibers or fibrils were observed on threads at all strain values, the probability of observing fibers and/or fibrils increased with strain. High-resolution AFM images show that with increasing strain, both mean fiber and fibril diameters decrease and that fibrils align themselves more closely with the thread axis. The observation of fibers and fibrils within the cobweb threads has implications for current models of the secondary and tertiary structure and organization of spider silk.
authors.affiliation: W.M. Keck Science Center, The Claremont Colleges, CA 91711-5916, USA. gould@physics.claremont.edu
authors.forename: S A
authors.initials: SA
authors.lastname: Gould
authors.forename: K T
authors.initials: KT
authors.lastname: Tran
authors.forename: J C
authors.initials: JC
authors.lastname: Spagna
authors.forename: A M
authors.initials: AM
authors.lastname: Moore
authors.forename: J B
authors.initials: JB
authors.lastname: Shulman
mesh_terms: D000818:Animals; D019476:Insect Proteins / Q000737:chemistry* / Q000648:ultrastructure; D018625:Microscopy, Atomic Force; D047011:Silk; D013112:Spiders / Q000737:chemistry*; D013312:Stress, Physiological
chemical_list: D019476:Insect Proteins; D047011:Silk