Molecular chain orientation in supercontracted and re-extended spider silk.
The dragline silk from Nephila clavipes was studied by wide angle X-ray diffraction in its original state, after supercontraction to L/Lo = 0.46, and during re-extension to its original length Lo. The fibers were carefully dried before each exposure. The molecular orientation in the crystalline regions is found to follow the simple predictions of affine deformation, indicating that the crystals act as inert rigid filler particles. The crystals retain considerable orientation after supercontraction, when non-crystalline orientation is weak. This shows that crystallization occurs after orientation as the fiber forms. The oriented amorphous material, treated as a phase of constant volume fraction, also follows affine deformation. These results do not contain any indication of a special structure in the protein fiber.
Grubb
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DT
Department of Materials Science, Cornell University, Ithaca, NY 14853, USA. dtg1@cornel.edu
Ji
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D000818:Animals; D003285:Contractile Proteins / Q000737:chemistry*; D005260:Female; D019476:Insect Proteins / Q000737:chemistry*; D015233:Models, Statistical; D015394:Molecular Structure; D047011:Silk; D013112:Spiders / Q000737:chemistry*; D014961:X-Ray Diffraction
D003285:Contractile Proteins; D019476:Insect Proteins; D047011:Silk