Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-state NMR spectroscopy

J Am Chem Soc. 2008 Apr 30;130(17):5618-9. doi: 10.1021/ja7108135. Epub 2008 Apr 5.

Abstract

Solid-state NMR spectroscopy is applied to intact peptidoglycan sacculi of the Gram-negative bacterium Escherichia coli. High-quality solid-state NMR spectra allow atom-resolved investigation of the peptidoglycan structure and dynamics as well as the study of protein-peptidoglycan interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Isotopes / chemistry
  • Escherichia coli / chemistry*
  • Escherichia coli / metabolism
  • Magnetic Resonance Spectroscopy / methods*
  • Nitrogen Isotopes / chemistry
  • Peptidoglycan* / chemistry
  • Peptidoglycan* / metabolism
  • Proteins / chemistry
  • Proteins / metabolism*

Substances

  • Carbon Isotopes
  • Nitrogen Isotopes
  • Peptidoglycan
  • Proteins