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- W2022255243 abstract "Proton-decoupled 15N solid-state NMR spectra are used to analyze the structure, dynamics, and membrane topology of proteins uniformly labeled with 15N. Preparation of the proteins by bacterial overexpression results in the labeling not only of the backbone amides but also of nitrogens localized within the side chains of arginine, glutamine, tryptophan, asparagines, lysines, and histidines. Most of these side chain resonances appear in the spectral region of the anisotropic backbone amides, and residual intensities have been observed also in cross-polarization spectra. In the past this issue has received little attention although it can cause ambiguities during assignment. Here we show that by combining cross-polarization and Hahn echo solid-state NMR experiments, it is possible to differentiate between side chain and backbone resonances. This is demonstrated using experimental and simulated 15N spectra of oriented purple membranes, diphtheria toxin T domain and Bcl-xL." @default.
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- W2022255243 date "2009-04-17" @default.
- W2022255243 modified "2023-09-23" @default.
- W2022255243 title "Side Chain Resonances in Static Oriented Proton-Decoupled <sup>15</sup>N Solid-State NMR Spectra of Membrane Proteins" @default.
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- W2022255243 doi "https://doi.org/10.1021/ja900677b" @default.
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