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Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS – “missing” resonances at the dimer interface
Using a deuterated sample, all the observable backbone (1)H(N), (15)N, (13)C(α), and (13)C′ chemical shifts for the dimeric, periplasmic sensor domain of the Burkholderia pseudomallei histidine kinase RisS were assigned. Approximately one-fifth of the amide resonances are “missing” in the (1)H-(15)N...
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| Vydáno v: | Biomol NMR Assign |
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| Hlavní autoři: | , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2015
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4569509/ https://ncbi.nlm.nih.gov/pubmed/25957069 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s12104-015-9614-2 |
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