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

doi:10.1016/0006-291X(86)91140-X

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 journal › Article › peer-review

11 Scopus citations

Abstract

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 language	English
Pages (from-to)	736-741
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	137
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(86)91140-X
State	Published - Jun 13 1986

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title = "Characterization of peptidoglycan stem lengths by solid-state 13C and 15N NMR",

abstract = "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.",

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T1 - Characterization of peptidoglycan stem lengths by solid-state 13C and 15N NMR

AU - Schaefer, Jacob

AU - Garbow, Joel R.

AU - Jacob, Gary S.

AU - Forrest, Theresa M.

AU - Wilson, G. Edwin

PY - 1986/6/13

Y1 - 1986/6/13

N2 - 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.

AB - 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.

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

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