Characterization of peptidoglycan stem lengths by solid-state 13C and 15N NMR

Jacob Schaefer, Joel R. Garbow, Gary S. Jacob, Theresa M. Forrest, G. Edwin Wilson

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Lyophilized whole cells of Aerococcus viridans (Gaffkya homari) grown on a synthetic medium containing D-[2-13C, 15N]Ala, or containing both L-[1-13C]Lys and D-[15N]Ala, have been examined by double cross-polarization magic-angle spinning 13C and 15N nuclear magnetic resonance. Results from the double-labeled alanine experiment confirm the absence of metabolic scrambling of alanine by A. viridans. Results from the combined single-label experiment can be used to count directly the number of adjacent L-Lys and D-Ala units in peptide chains of cell-wall peptidoglycan. This count leads to the conclusion that there are no terminal D-Ala or D-Ala-D-Ala units in uncross-linked chains of the peptidoglycan of A. viridans.

Original languageEnglish
Pages (from-to)736-741
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Jun 13 1986


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