Orientational order of Australian spider silks as determined by solid-state NMR

B. Bonev; S. Grieve; M. E. Herberstein; A. I. Kishore; A. Watts; F. Separovic

doi:10.1002/bip.20471

Orientational order of Australian spider silks as determined by solid-state NMR

B. Bonev, S. Grieve, M. E. Herberstein, A. I. Kishore, A. Watts, F. Separovic^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

Abstract

A simple solid-state NMR method was used to study the structure of ¹³C- and ¹⁵N-enriched silk from two Australian orb-web spider species, Nephila edulis and Argiope keyserlingi. Carbon-13 and ¹⁵N 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 language	English
Pages (from-to)	134-143
Number of pages	10
Journal	Biopolymers
Volume	82
Issue number	2
DOIs	https://doi.org/10.1002/bip.20471
Publication status	Published - 5 Jun 2006

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abstract = "A simple solid-state NMR method was used to study the structure of 13C- and 15N-enriched silk from two Australian orb-web spider species, Nephila edulis and Argiope keyserlingi. Carbon-13 and 15N 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.",

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AU - Bonev, B.

AU - Grieve, S.

AU - Herberstein, M. E.

AU - Kishore, A. I.

AU - Watts, A.

AU - Separovic, F.

PY - 2006/6/5

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AB - A simple solid-state NMR method was used to study the structure of 13C- and 15N-enriched silk from two Australian orb-web spider species, Nephila edulis and Argiope keyserlingi. Carbon-13 and 15N 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.

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Orientational order of Australian spider silks as determined by solid-state NMR

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