Quantifying the fraction of glycine and alanine in β-sheet and helical conformations in spider dragline silk using solid-state NMR

Gregory P. Holland, Janelle E. Jenkins, Melinda S. Creager, Randolph V. Lewis, Jeffery Yarger

Research output: Contribution to journalArticle

59 Scopus citations


Solid-state two-dimensional refocused INADEQUATE MAS NMR experiments resolve distinct helical and β-sheet conformational environments for both alanine and glycine in Nephila clavipes dragline silk fibers; the fraction of alanine and glycine in β-sheet structures is determined to be 82% ± 4% and 28% ± 5%, respectively.

Original languageEnglish (US)
Pages (from-to)5568-5570
Number of pages3
JournalChemical Communications
Issue number43
Publication statusPublished - 2008


ASJC Scopus subject areas

  • Metals and Alloys
  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Catalysis
  • Chemistry(all)

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