Line narrowing in spectra of proteins dissolved in a dilute liquid crystalline phase by band-selective adiabatic decoupling: Application to 1H(N)-15N residual dipolar coupling measurements

Craig W. Vander Kooi, Eriks Kupče, Erik R.P. Zuiderweg, Maurizio Pellecchia

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

Residual heteronuclear dipolar couplings obtained from partially oriented protein samples can provide unique NMR constraints for protein structure determination. However, partial orientation of protein samples also causes severe 1H line broadening resulting from residual 1H-1H dipolar couplings. In this communication we show that band-selective 1H homonuclear decoupling during data acquisition is an efficient way to suppress residual 1H-1H dipolar couplings, resulting in spectra that are still amenable to solution NMR analysis, even with high degrees of alignment. As an example, we present a novel experiment with improved sensitivity for the measurement of one-bond 1H(N)-15N residual dipolar couplings in a protein sample dissolved in magnetically aligned liquid crystalline bicelles.

Original languageEnglish
Pages (from-to)335-338
Number of pages4
JournalJournal of Biomolecular NMR
Volume15
Issue number4
DOIs
StatePublished - 1999

Bibliographical note

Funding Information:
This work was supported by a University of Michigan Regent’s Fellowship to C.W.V.K. and by the National Institutes of Health Grant GM 52421.

Keywords

  • Adiabatic decoupling
  • Bicelles
  • Homonuclear decoupling
  • Protein alignment
  • Residual dipolar coupling

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy

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