Constant-time through-bond 13C correlation spectroscopy for assigning protein resonances with solid-state NMR spectroscopy

Lingling Chen, Ryan A. Olsen, Douglas W. Elliott, John M. Boettcher, Donghua H. Zhou, Chad M. Rienstra, Leonard J. Mueller

Research output: Contribution to journalArticlepeer-review

Abstract

Even as available magnetic fields for NMR continue to increase, resolution remains one of the most critical limitations in assigning and solving structures of larger biomolecules. Here we present a novel constant-time through-bond correlation spectroscopy for solids that offers superior resolution for 13C chemical shift assignments in proteins. In this experiment, the indirect evolution and transfer periods are combined into a single constant time interval, offering increased resolution while not sacrificing sensitivity. In GB1, this allows us to resolve peaks that are otherwise unresolved and to make assignments in the absence of multibond transfers.

Original languageEnglish (US)
Pages (from-to)9992-9993
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number31
DOIs
StatePublished - Aug 9 2006

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry

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