Coupling Amplification in 2D MAS NMR and Its Application to Torsion Angle Determination in Peptides

Mei Hong, John D. Gross, Chad M. Rienstra, Robert G. Griffin, Kristin K. Kumashiro, Klaus Schmidt-Rohr

Research output: Contribution to journalArticlepeer-review


A technique for amplifying the apparent magnitudes of 13C-1H and 15N-1H dipolar interactions in magic-angle spinning experiments is described. By inserting rotor-synchronized 180 ° pulses in the evolution period of a 2D dipolar-chemical shift experiment, heteronuclear dipolar couplings are doubled or quadrupled relative to the spinning speed. The increased number of dipolar side-bands is desirable for retaining structural information in the indirectly detected dipolar dimension while resolving inequivalent sites in the isotropic chemical shift dimension at relatively high spinning speeds. This coupling amplification method is incorporated into an experiment that determines the peptide torsion angle φ through the relative orientation of the Cα-Hα and N-HN bonds. It is shown both experimentally and theoretically that the angular resolution of the measurement is enhanced significantly by the selective doubling of the N-HN coupling.

Original languageEnglish (US)
Pages (from-to)85-92
Number of pages8
JournalJournal of Magnetic Resonance
Issue number1
StatePublished - Nov 1997
Externally publishedYes


  • Dipolar coupling
  • Magic-angle spinning
  • Peptide structure
  • Solid-state NMR
  • Torsion angle

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics


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