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

Research output: Contribution to journalArticlepeer-review

62 Scopus citations


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 languageEnglish (US)
Pages (from-to)2039-2043
Number of pages5
Issue number8
StatePublished - Aug 9 2010

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry


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