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 journalArticle

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Abstract

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
Volume117
Issue number19
DOIs
Publication statusPublished - May 1995

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ASJC Scopus subject areas

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

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