title: Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-state NMR spectroscopy.
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.
authors.affiliation: Institut de Biologie Structurale, UMR5075 (CEA/CNRS/UJF), 38027 Grenoble, France.
authors.forename: Thomas
authors.initials: T
authors.lastname: Kern
authors.forename: Sabine
authors.initials: S
authors.lastname: Hediger
authors.forename: Patrick
authors.initials: P
authors.lastname: Müller
authors.forename: Cécile
authors.initials: C
authors.lastname: Giustini
authors.forename: Bernard
authors.initials: B
authors.lastname: Joris
authors.forename: Catherine
authors.initials: C
authors.lastname: Bougault
authors.forename: Waldemar
authors.initials: W
authors.lastname: Vollmer
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Simorre
mesh_terms: D002247:Carbon Isotopes / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009587:Nitrogen Isotopes / Q000737:chemistry; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010457:Peptidoglycan; D011506:Proteins