Heteronuclear correlation experiments for the determination of one-bond coupling constants

J Biomol NMR. 1998 May;11(4):445-50. doi: 10.1023/a:1008206212145.

Abstract

Spin-state selective experiments, HSQC-alpha/beta and CT-HMQC-alpha/beta, are proposed for the simple and rapid measurement of scalar one-bond coupling constants in two-dimensional, 1H-detected 15N-1H or 13C-1H correlation experiments based on HSQC and HMQC schemes. Pairs of subspectra are obtained, containing either the high-field or the low-field component of the doublet representing the one-bond coupling constant. The subspectral editing procedure retains the full sensitivity of HSQC and HMQC spectra recorded without heteronuclear decoupling during data acquisition, with a spectral resolution similar to that of decoupled spectra.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Escherichia coli
  • Escherichia coli Proteins*
  • Nuclear Magnetic Resonance, Biomolecular / instrumentation
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Structure, Secondary
  • Repressor Proteins / chemistry

Substances

  • ArgR protein, Bacteria
  • ArgR protein, E coli
  • Bacterial Proteins
  • Escherichia coli Proteins
  • Repressor Proteins