REDOR with a relative full-echo reference

J Magn Reson. 2003 Jul;163(1):182-7. doi: 10.1016/s1090-7807(03)00078-8.

Abstract

REDOR and REDOR-like 13C[19F] and 2H[19F] NMR experiments have been performed on lyophilized whole cells of Staphylococcus aureus. The bacteria were grown to maturity on media containing L-[13C(3)]alanine or L-[methyl-d(3)]alanine, and then complexed with the 4-fluorobiphenyl derivative of chloroeremomycin, an analogue of the widely used antibiotic, vancomycin. The position of the 19F of the drug bound in the bacterial cell wall was determined relative to L-alanine 13C and 2H labels in the peptidoglycan peptide stem that was closest to the fluorinated biphenyl moiety of the drug. These determinations were made by dipolar recoupling methods that do not require an absolute measurement of the REDOR full echo (the signal observed without rotor-synchronized dephasing pulses) of the labels in the peptide stem.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, U.S. Gov't, P.H.S.
  • Validation Study

MeSH terms

  • Alanine / chemistry*
  • Alanine / metabolism*
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / metabolism
  • Binding Sites
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Computer Simulation
  • Deuterium
  • Isotope Labeling / methods
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Models, Biological
  • Models, Chemical
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Binding
  • Spin Labels
  • Staphylococcus aureus / chemistry*
  • Staphylococcus aureus / metabolism*
  • Staphylococcus aureus / ultrastructure
  • Vancomycin / analogs & derivatives*
  • Vancomycin / chemistry*
  • Vancomycin / metabolism

Substances

  • Anti-Bacterial Agents
  • Membrane Proteins
  • Spin Labels
  • chloroeremomycin
  • Vancomycin
  • Deuterium
  • Alanine