Detection of side-chain proton resonances of fully protonated biosolids in nano-litre volumes by magic angle spinning solid-state NMR

J Biomol NMR. 2018 Mar;70(3):177-185. doi: 10.1007/s10858-018-0168-3. Epub 2018 Mar 3.


We present a new solid-state NMR proton-detected three-dimensional experiment dedicated to the observation of protein proton side chain resonances in nano-liter volumes. The experiment takes advantage of very fast magic angle spinning and double quantum 13C-13C transfer to establish efficient (H)CCH correlations detected on side chain protons. Our approach is demonstrated on the HET-s prion domain in its functional amyloid fibrillar form, fully protonated, with a sample amount of less than 500 µg using a MAS frequency of 70 kHz. The majority of aliphatic and aromatic side chain protons (70%) are observable, in addition to Hα resonances, in a single experiment providing a complementary approach to the established proton-detected amide-based multidimensional solid-state NMR experiments for the study and resonance assignment of biosolid samples, in particular for aromatic side chain resonances.

Keywords: Amyloid fibrils; Protein NMR; Proton detection; Solid-state NMR; Very fast MAS.

MeSH terms

  • Amyloid / chemistry
  • Carbon Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Prions / chemistry
  • Protons*


  • Amyloid
  • Carbon Isotopes
  • Prions
  • Protons
  • Carbon-13