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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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13C and 15N-chemical shift anisotropy of ampicillin and penicillin-V studied by 2D-PASS and CP/ MAS NMR.

The principal values of the chemical shift tensors of all 13C and 15N sites in two antibiotics, ampicillin and penicillin-V, were determined by 2-dimensional phase adjusted spinning sideband (2D-PASS) and conventional CP/ MAS experiments. The 13C and 15N chemical shift anisotropies (CSA), and their confidence limits, were evaluated using a Mathematica program. The CSA values suggest a revised assignment of the 2-methyl 13C sites in the case of ampicillin. We speculate on a relationship between the chemical shift principal values of many of the 13C and 15N sites and the beta-lactam ring conformation.[1]

References

  1. 13C and 15N-chemical shift anisotropy of ampicillin and penicillin-V studied by 2D-PASS and CP/MAS NMR. Antzutkin, O.N., Lee, Y.K., Levitt, M.H. J. Magn. Reson. (1998) [Pubmed]
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