Sensitivity enhancement of triple-resonance protein NMR spectra by proton evolution of multiple-quantum coherences using a simultaneous 1H and 13C costant-time evlution period

Zhigang Shang, G. V.T. Swapna, Carlos B. Rios, Gaetano T. Montelione

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10 Scopus citations

Abstract

Short transverse relaxation times of C(α) and H(α) single-quantum states in proteins reduce signal-to-noise ratios of heteronuclear correlation experiments involving transfers of C(α) and H(α) coherences. To overcome this 'short transverse relaxation problem', we have developed a simultaneous 1H and 13C constant-time (sim-CT) heteronuclear multiple-quantum coherence (HMC) scheme. New features in this design include: (i) utilization of heteronuclear multiple-quantum coherences for better transverse relaxation properties, (ii) concatenation of proton evolution into the simultaneous 1H and 13C Constant-time period to eliminate separate time periods for proton evolution, and (iii) use of simultaneous 1H and 13C constant-time to remove resonance splitting due to multiple two- and three- bond homo- and heteronuclear scalar couplings. This general approach for sensitivity enhancement is demonstrated for the HA(CA)(CO)NH triple-resonance experiment. Results on proteins show that, compared with the heteronuclear single-quantum coherence version of the same experiment, on average the sim-CT HMQC version of HA(CA)(CO)NH exhibits enhancements of ~20%.

Original languageEnglish (US)
Pages (from-to)9274-9278
Number of pages5
JournalJournal of the American Chemical Society
Volume119
Issue number39
DOIs
StatePublished - Oct 1 1997

All Science Journal Classification (ASJC) codes

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

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