Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-state NMR spectroscopy.
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.
Kern
Thomas
T
Institut de Biologie Structurale, UMR5075 (CEA/CNRS/UJF), 38027 Grenoble, France.
Hediger
Sabine
S
Müller
Patrick
P
Giustini
Cécile
C
Joris
Bernard
B
Bougault
Catherine
C
Vollmer
Waldemar
W
Simorre
Jean-Pierre
JP
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*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010457:Peptidoglycan; D011506:Proteins