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Updated: Jan 15, 2026

High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
Published on: October 9, 2020
Vibrational Spectroscopy of Triple 13C18O15N Isotope-Edited N-Methylacetamide: Interplay between Experiment and
Luca Supovec1, Sara Gómez2,3, Tommaso Giovannini2,4
1Universität Duisburg-Essen, 45141 Essen, Germany.
Abstract:
Isotope editing of amide bonds is a powerful tool for site-specific vibrational spectroscopy of peptides and proteins. However, only single and double isotope labeling such as 13C18O and 13C15N has been reported so far. Here, we establish triple 13C118O15N isotope editing of the amide bond in N-methylacetamide (NMA) as the most widely employed model system for peptides. The effect of successive isotope labeling on the peak position of amide modes is systematically studied by comparing the IR, electronically nonresonant Raman, and UV resonance Raman (UVRR) spectra of NMA-13C1, NMA-13C118O, and NMA-13C118O15N. The experimental spectra agree well with theoretical predictions obtained by using atomistic, fully polarizable multiscale quantum mechanical (QM)/classical modeling of neat NMA (IR/Raman) and NMA in aqueous solution (UVRR). The presented triple-labeling approach paves the way for complementary site-specific studies of individual amide bonds and their prominent amide I, II, and III vibrations by using both IR and UVRR spectroscopy on the same 13C18O15N-labeled sample.
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