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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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| Publicat a: | Biomol NMR Assign |
|---|---|
| Autors principals: | , , , , , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
2015
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| Matèries: | |
| Accés en línia: | 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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