DNP NMR spectroscopy reveals new structures, residues and interactions in wild spider silks

Chem Commun (Camb). 2019 Apr 16;55(32):4687-4690. doi: 10.1039/c9cc01045a.

Abstract

DNP solid state NMR spectroscopy allows non-targeted analysis of wild spider silk in unprecedented detail at natural abundance, revealing hitherto unreported features across several species. A >50-fold signal enhancement for each silk, enables the detection of novel H-bonding networks and arginine conformations, and the post-translational modified amino acid, hydroxyproline.

MeSH terms

  • Animals
  • Carbon-13 Magnetic Resonance Spectroscopy
  • Fibroins / chemistry*
  • Hydrogen Bonding
  • Hydroxyproline / chemistry
  • Nitrogen Isotopes
  • Protein Conformation, beta-Strand
  • Spiders / chemistry*

Substances

  • Nitrogen Isotopes
  • Nitrogen-15
  • Fibroins
  • Hydroxyproline