ORBi: Kern Thomas - Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-state NMR spectroscopy.

Reference : Toward the characterization of peptidoglycan structure and protein-peptidoglycan interac...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/23496

Title :	Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-state NMR spectroscopy.
Language :	English
Author, co-author :	Kern, Thomas [> > > >]
	Hediger, Sabine [> > > >]
	Muller, Patrick [> > > >]
	Giustini, Cecile [> > > >]
	Joris, Bernard [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes - Centre d'ingénierie des protéines >]
	Bougault, Catherine [> > > >]
	Vollmer, Waldemar [> > > >]
	Simorre, Jean-Pierre [> > > >]*
Publication date :	2008
Journal title :	Journal of the American Chemical Society
Publisher :	American Chemical Society
Volume :	130
Issue/season :	17
Pages :	5618-9
Audience :	International
ISSN :	0002-7863
e-ISSN :	1520-5126
City :	Washington
Country :	DC
Keywords :	[en] Carbon Isotopes/chemistry ; Escherichia coli/chemistry/metabolism ; Magnetic Resonance Spectroscopy/methods ; Nitrogen Isotopes/chemistry ; Peptidoglycan/chemistry/metabolism ; Proteins/chemistry/metabolism
Abstract :	[en] 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.
Permalink :	http://hdl.handle.net/2268/23496
DOI :	10.1021/ja7108135

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