Abstract:
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.
