Solid-state NMR comparison of various spiders' dragline silk fiber

Melinda S. Creager; Janelle E. Jenkins; Leigh A. Thagard-Yeaman; Amanda E. Brooks; Justin A. Jones; Randolph V. Lewis; Gregory P. Holland; Jeffery Yarger

doi:10.1021/bm100399x

Solid-state NMR comparison of various spiders' dragline silk fiber

Melinda S. Creager, Janelle E. Jenkins, Leigh A. Thagard-Yeaman, Amanda E. Brooks, Justin A. Jones, Randolph V. Lewis, Gregory P. Holland, Jeffery Yarger

CLAS-NS: Molecular Sciences, School of (SMS)

Research output: Contribution to journal › Article

49 Scopus citations

Abstract

Major ampullate (dragline) spider silk is a coveted biopolymer due to its combination of strength and extensibility. The dragline silk of different spiders have distinct mechanical properties that can be qualitatively correlated to the protein sequence. This study uses amino acid analysis and carbon-13 solid-state NMR to compare the molecular composition, structure, and dynamics of major ampullate dragline silk of four orb-web spider species (Nephila clavipes, Araneus gemmoides, Argiope aurantia, and Argiope argentata) and one cobweb species (Latrodectus hesperus). The mobility of the protein backbone and amino acid side chains in water exposed silk fibers is shown to correlate to the proline content. This implies that regions of major ampullate spidroin 2 protein, which is the only dragline silk protein with any significant proline content, become significantly hydrated in dragline spider silk.

Original language	English (US)
Pages (from-to)	2039-2043
Number of pages	5
Journal	Biomacromolecules
Volume	11
Issue number	8
DOIs	https://doi.org/10.1021/bm100399x
State	Published - Aug 9 2010

ASJC Scopus subject areas

Bioengineering
Biomaterials
Polymers and Plastics
Materials Chemistry

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Creager, M. S., Jenkins, J. E., Thagard-Yeaman, L. A., Brooks, A. E., Jones, J. A., Lewis, R. V., Holland, G. P., & Yarger, J. (2010). Solid-state NMR comparison of various spiders' dragline silk fiber. Biomacromolecules, 11(8), 2039-2043. https://doi.org/10.1021/bm100399x

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abstract = "Major ampullate (dragline) spider silk is a coveted biopolymer due to its combination of strength and extensibility. The dragline silk of different spiders have distinct mechanical properties that can be qualitatively correlated to the protein sequence. This study uses amino acid analysis and carbon-13 solid-state NMR to compare the molecular composition, structure, and dynamics of major ampullate dragline silk of four orb-web spider species (Nephila clavipes, Araneus gemmoides, Argiope aurantia, and Argiope argentata) and one cobweb species (Latrodectus hesperus). The mobility of the protein backbone and amino acid side chains in water exposed silk fibers is shown to correlate to the proline content. This implies that regions of major ampullate spidroin 2 protein, which is the only dragline silk protein with any significant proline content, become significantly hydrated in dragline spider silk.",

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AU - Creager, Melinda S.

AU - Jenkins, Janelle E.

AU - Thagard-Yeaman, Leigh A.

AU - Brooks, Amanda E.

AU - Jones, Justin A.

AU - Lewis, Randolph V.

AU - Holland, Gregory P.

AU - Yarger, Jeffery

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N2 - Major ampullate (dragline) spider silk is a coveted biopolymer due to its combination of strength and extensibility. The dragline silk of different spiders have distinct mechanical properties that can be qualitatively correlated to the protein sequence. This study uses amino acid analysis and carbon-13 solid-state NMR to compare the molecular composition, structure, and dynamics of major ampullate dragline silk of four orb-web spider species (Nephila clavipes, Araneus gemmoides, Argiope aurantia, and Argiope argentata) and one cobweb species (Latrodectus hesperus). The mobility of the protein backbone and amino acid side chains in water exposed silk fibers is shown to correlate to the proline content. This implies that regions of major ampullate spidroin 2 protein, which is the only dragline silk protein with any significant proline content, become significantly hydrated in dragline spider silk.

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