Improved detection of long-range residual dipolar couplings in weakly aligned samples by Lee-Goldburg decoupling of homonuclear dipolar truncation

Pernille Rose Jensen, Hans-Jürgen Sass, Stephan Grzesiek

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Homonuclear H-1 residual dipolar couplings (RDCs) truncate the evolution of transverse H-1 magnetization of weakly aligned molecules in high-resolution NMR experiments. This leads to losses in sensitivity or resolution in experiments that require extended H-1 evolution times. Lee-Goldburg decoupling schemes have been shown to remove the effects of homonuclear dipolar couplings, while preserving chemical shift evolution in a number of solid-state NMR applications. Here, it is shown that the Lee-Goldburg sequence can be effectively incorporated into INEPT- or HMQC-type transfer schemes in liquid state weak alignment experiments in order to increase the efficiency of the magnetization transfer. The method is applied to the sensitive detection of (HN)-H-1-C-13 long-range RDCs in a three-dimensional HCN experiment. As compared to a conventional HCN experiment, an average sensitivity increase by a factor of 2.4 is obtained for a sample of weakly aligned protein G. This makes it possible to detect 170 long-range (HN-13C)-H-1 RDCs for distances up to 4.9 Angstrom.
Original languageEnglish
JournalJournal of Biomolecular N M R
Volume30
Issue number4
Pages (from-to)443-450
ISSN0925-2738
DOIs
Publication statusPublished - 2004
Externally publishedYes

Keywords

  • Carbon Isotopes
  • Nerve Tissue Proteins
  • Nuclear Magnetic Resonance, Biomolecular
  • Protons
  • Sensitivity and Specificity
  • G-substrate
  • Spectroscopy
  • Biochemistry, Genetics and Molecular Biology (all)
  • Biochemistry
  • NMR
  • Protein
  • Structure
  • Weak alignment
  • carbon 13
  • nitrogen 15
  • protein G
  • proton
  • article
  • controlled study
  • liquid
  • magnetism
  • mathematical analysis
  • nuclear magnetic resonance spectroscopy
  • priority journal
  • protein analysis
  • protein structure
  • proton nuclear magnetic resonance
  • sensitivity analysis
  • solid state
  • time
  • BIOCHEMISTRY
  • SPECTROSCOPY
  • NMR-SPECTROSCOPY
  • PROTEIN-STRUCTURE
  • PULSE SEQUENCES
  • PHASE
  • FIELD
  • EXCITATION
  • ALIGNMENT
  • SOLIDS
  • protein
  • structure
  • weak alignment
  • Chemistry
  • Polymer Sciences
  • Animal Anatomy / Morphology / Histology
  • homonuclear dipolar truncation
  • Lee-Goldburg decoupling
  • magnetization transfer
  • 10060, Biochemistry studies - General
  • HCN experiment laboratory techniques
  • nuclear magnetic resonance NMR laboratory techniques, spectrum analysis techniques
  • Biochemistry and Molecular Biophysics

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