Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9587525 | Journal of Magnetic Resonance | 2005 | 10 Pages |
Abstract
Recently, we reported an analysis of carbon lineshapes in high resolution solid-state NMR spectra of uniformly 13C-enriched amino acids. Application of a 13C J-decoupling protocol during the carbon chemical shift evolution period allowed us to separate the contribution of the second-order dipolar shift from that of the 13C-13C J-coupling interactions to carbon linewidths. In this work, we have extended this approach to microcrystalline proteins. We describe the performance of the J-decoupling sequence applied to remove homo-nuclear 13C J-couplings in the 13C spectra of ubiquitin. Analysis of the J-decoupling efficiency for Cα and carbonyl protein sites showed that a significant gain in resolution can be achieved.
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Authors
Tatyana I. Igumenova, Ann E. McDermott,