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A simple solid-state NMR method was used to study the structure of (13)C- and (15)N-enriched silk from two Australian orb-web spider species, Nephila edulis and Argiope keyserlingi. Carbon-13 and (15)N spectra from alanine- or glycine-labeled oriented dragline silks were acquired with the fiber axis aligned parallel or perpendicular to the magnetic field. The fraction of oriented component was determined from each amino acid, alanine and glycine, using each nucleus independently, and attributed to the ordered crystalline domains in the silk. The relative fraction of ordered alanine was found to be higher than the fraction of ordered glycine, akin to the observation of alanine-rich domains in silk-worm (Bombyx mori) silk. A higher degree of crystallinity was observed in the dragline silk of N. edulis compared with A. keyserlingi, which correlates with the superior mechanical properties of the former.

Original publication

DOI

10.1002/bip.20471

Type

Journal article

Journal

Biopolymers

Publication Date

05/06/2006

Volume

82

Pages

134 - 143

Keywords

Animals, Australia, Biopolymers, Female, Fibroins, Insect Proteins, Nuclear Magnetic Resonance, Biomolecular, Silk, Species Specificity, Spiders, Water