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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Publicado en:Biomol NMR Assign
Main Authors: Buchko, Garry W., Edwards, Thomas E., Hewitt, Stephen N., Phan, Isabelle Q.H., Van Voorhis, Wesley C., Miller, Samuel I., Mylera, Peter J.
Formato: Artigo
Idioma:Inglês
Publicado: 2015
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Article
Acceso en liña: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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