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• W272047255 abstract "Using a deuterated sample, all the observable backbone 1HN, 15N, 13Ca, and 13C′ 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 1H–15N HSQC spectrum and map primarily onto α-helices at the dimer interface observed in a crystal structure suggesting this region either undergoes intermediate timescale motion (μs–ms) and/or is heterogeneous." @default.
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• W272047255 date "2015-05-09" @default.
• W272047255 modified "2023-10-12" @default.
• W272047255 title "Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS: “missing” resonances at the dimer interface" @default.
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• W272047255 doi "https://doi.org/10.1007/s12104-015-9614-2" @default.
• W272047255 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4569509" @default.
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