J-based 2D homonuclear and heteronuclear correlation in solid-state proteins

Lingling Chen, J. Michael Kaiser, Jinfeng Lai, Tatyana Polenova, Jun Yang, Chad M. Rienstra, Leonard J. Mueller

Research output: Contribution to journalArticlepeer-review


Scalar-based two-dimensional heteronuclear experiments are reported for NCO and NCA chemical shift correlation in the solid state. In conjunction with homonuclear CACO correlation, these experiments form a useful set for tracing connectivities and assigning backbone resonances in solid-state proteins. The applicability of this approach is demonstrated on two proteins, the β 1 immunoglobulin binding domain of protein G at 9.4 T and reassembled thioredoxin at 14.1 T, using different decoupling conditions and MAS frequencies. These constant-time J-based correlation experiments exhibit increased resolution in the indirect dimension owing to homonuclear and heteronuclear decoupling, and because the indirect evolution and transfer periods are combined into a single constant time interval, this increased resolution is not obtained at the cost of sensitivity. These experiments are also shown to be compatible with in-phase anti-phase (IPAP) selection, giving increased resolution in the directly detected dimension.

Original languageEnglish (US)
Pages (from-to)S84-S92
JournalMagnetic Resonance in Chemistry
Issue numberSUPPL.
StatePublished - Dec 2007


  • NMR
  • Protein
  • Scalar-coupling-driven correlation
  • Solid-state NMR
  • Through-bond correlation

ASJC Scopus subject areas

  • General Chemistry
  • General Materials Science


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