Skip to main navigation Skip to search Skip to main content

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 journalArticlepeer-review

Abstract

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
DOIs
StatePublished - 2008

ASJC Scopus subject areas

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

Fingerprint

Dive into the research topics of 'Quantifying the fraction of glycine and alanine in β-sheet and helical conformations in spider dragline silk using solid-state NMR'. Together they form a unique fingerprint.

Cite this