title: Hierarchical chain model of spider capture silk elasticity.
abstract: Spider capture silk is a biomaterial with both high strength and high elasticity, but the structural design principle underlying these remarkable properties is still unknown. It was revealed recently by atomic force microscopy that an exponential force-extension relationship holds both for capture silk mesostructures and for intact capture silk fibers [N. Becker et al., Nat. Mater. 2, 278 (2003)]]. In this Letter a simple hierarchical chain model was proposed to understand and reproduce this striking observation. In the hierarchical chain model, a polymer is composed of many structural motifs which organize into structural modules and supramodules in a hierarchical manner. Each module in this hierarchy has its own characteristic force. The repetitive patterns in the amino-acid sequence of the major flagelliform protein of spider capture silk is in support of this model.
authors.affiliation: Max-Planck-Institute of Colloids and Interfaces, 14424 Potsdam, Germany.
authors.forename: Haijun
authors.initials: H
authors.lastname: Zhou
authors.forename: Yang
authors.initials: Y
authors.lastname: Zhang
mesh_terms: D000818:Animals; D003198:Computer Simulation; D004548:Elasticity; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D047011:Silk / Q000737:chemistry*; D013112:Spiders; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship
chemical_list: D047011:Silk