  Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-state NMR spectroscopy.; ; et al in Journal of the American Chemical Society (2008), 130(17), 5618-9 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 ... [more ▼] 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. [less ▲] Detailed reference viewed: 23 (2 ULg)1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function.; ; et al in Biomolecular NMR assignments (2007), 1(1), 89-91 The ampG gene codes for a permease required to uptake anhydro-muropeptides into bacterial cytoplasm. Located upstream in the same operon, is another 579-base-pair-long open reading frame encoding a ... [more ▼] The ampG gene codes for a permease required to uptake anhydro-muropeptides into bacterial cytoplasm. Located upstream in the same operon, is another 579-base-pair-long open reading frame encoding a putative lipoprotein YajG, whose nearly complete 1H,13C,15N assignments are reported here. [less ▲] Detailed reference viewed: 18 (1 ULg) |
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