Characterization of peptide O∙∙∙HN hydrogen bonds via multidimensional 1H-detected 15N/17O solid-state nuclear magnetic resonance spectroscopy


  • Ivan Hung National High Magnetic Field Laboratory ,
  • Wenping Mao National High Magnetic Field Laboratory ,
  • Eric G. Keeler New York Structural Biology Center & Massachusetts Institute of Technology ,
  • Robert G. Griffin Massachusetts Institute of Technology & Francis Bitter Magnet Laboratory ,
  • Peter L. Gor'kov National High Magnetic Field Laboratory ,
  • Zhehong Gan National High Magnetic Field Laboratory


Solid-state NMR methods with high resolution and sensitivity are presented for identification and charaterization of hydrogen-bonded 15N/17O atomic pairs in peptide samples. Indirect 1H detection under fast magic-angle spinning, and the stronger 1H-15N and 1H-17O couplings are leveraged to significantly improve sensitivity over previous methods that use direct 15N-17O interactions.


Supplementary material

Additional experimental details.
Detailed solid-state NMR experimental parameters and schematic pulse sequences for the OhNH experiments.