Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5406513 | Journal of Magnetic Resonance | 2010 | 8 Pages |
Abstract
13C NMR of isotopically labeled methyl groups has the potential to combine spectroscopic simplicity with ease of labeling for protein NMR studies. However, in most high resolution separated local field experiments, such as polarization inversion spin exchange at the magic angle (PISEMA), that are used to measure 1H-13C hetero-nuclear dipolar couplings, the four-spin system of the methyl group presents complications. In this study, the properties of the 1H-13C hetero-nuclear dipolar interactions of 13C-labeled methyl groups are revealed through solid-state NMR experiments on a range of samples, including single crystals, stationary powders, and magic angle spinning of powders, of 13C3 labeled alanine alone and incorporated into a protein. The spectral simplifications resulting from proton detected local field (PDLF) experiments are shown to enhance resolution and simplify the interpretation of results on single crystals, magnetically aligned samples, and powders. The complementarity of stationary sample and magic angle spinning (MAS) measurements of dipolar couplings is demonstrated by applying polarization inversion spin exchange at the magic angle and magic angle spinning (PISEMAMAS) to unoriented samples.
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Authors
Chin H. Wu, Bibhuti B. Das, Stanley J. Opella,