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Tailoring (13)C labeling for triple-resonance solid-state NMR experiments on aligned samples of proteins
In order to develop triple-resonance solid-state NMR spectroscopy of membrane proteins, we have implemented several different (13)C labeling schemes with the purpose of overcoming the interfering effects of (13)C–(13)C dipole–dipole couplings in stationary samples. The membrane-bound form of the maj...
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| Vydáno v: | Magn Reson Chem |
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| Hlavní autoři: | , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2007
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5010364/ https://ncbi.nlm.nih.gov/pubmed/18157808 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/mrc.2121 |
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