Multiple-Quantum Line Narrowing for Measurement of Hα—HβJ Couplings in Isotopically Enriched Proteins

Stephan Grzesiek, Hitoshi Kuboniwa, Ad Bax, Andrew P. Hinck

Research output: Contribution to journalArticlepeer-review

125 Scopus citations


Uniform 13C enrichment of proteins is commonly used for NMR studies of proteins that are not amenable to conventional homonuclear 2D NMR spectroscopy. In such studies, the one-bond 1H—13C dipolar interaction is usually the dominant source of 1H line broadening. 1H—13C zero- and double-quantum coherences are, to first order, not affected by this dipolar relaxation mechanism. The relatively long relaxation time of such 1Hα13Cαmultiple-quantum coherences is exploited for measurement of Hα—HβJ couplings in a sample of uniformly 13C-enriched calcium-free calmodulin (16.7 kD) and a sample of TGF-β1 (25 kDa). 7(Hα—Hβ) provides information on the stereospecific resonance assignment for residues with nonequivalent Hβmethylene protons and on the χ1 torsion angles.

Original languageEnglish (US)
Pages (from-to)5312-5315
Number of pages4
JournalJournal of the American Chemical Society
Issue number19
StatePublished - May 1995
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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