1H–1H MAS Correlation Spectroscopy and Distance Measurements in a Deuterated Peptide

In this Communication, we demonstrate the use of deuteration together with back substitution of exchangeable protons as a means of attenuating the strong 1H–1H couplings that broaden 1H magic angle spinning (MAS) spectra of solids. The approach facilitates 15N–1H correlation experiments as well as e...

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Bibliographic Details
Published in:Journal of magnetic resonance (1997) 2001-08, Vol.151 (2), p.320-327
Main Authors: Reif, B., Jaroniec, C.P., Rienstra, C.M., Hohwy, M., Griffin, R.G.
Format: Article
Language:English
Subjects:
Deuterium
Magnetic Resonance Spectroscopy - methods
Mathematics
Molecular Conformation
Peptides - chemistry
Signal Processing, Computer-Assisted
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Summary:In this Communication, we demonstrate the use of deuteration together with back substitution of exchangeable protons as a means of attenuating the strong 1H–1H couplings that broaden 1H magic angle spinning (MAS) spectra of solids. The approach facilitates 15N–1H correlation experiments as well as experiments for the measurement of 1H–1H distances. The distance measurement relies on the excellent resolution in the 1H MAS spectrum and homonuclear double quantum recoupling techniques. The 1H–1H dipolar recoupling can be analyzed in an analytical fashion by fitting the data to a 2- or 3-spin system. The experiments are performed on a sample of the dipeptide N–Ac–Val–Leu–OH, which was synthesized from uniformly [2H, 15N] labeled materials and back-exchanged in H2O.
ISSN:1090-7807
1096-0856
DOI:10.1006/jmre.2001.2354