Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS: "missing" resonances at the dimer interface.
作者信息
Buchko Garry W, Edwards Thomas E, Hewitt Stephen N, Phan Isabelle Q H, Van Voorhis Wesley C, Miller Samuel I, Myler Peter J
机构信息
Seattle Structural Genomics Center for Infectious Disease, Seattle, USA.
Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
出版信息
Biomol NMR Assign. 2015 Oct;9(2):381-5. doi: 10.1007/s12104-015-9614-2. Epub 2015 May 9.
Abstract
Using a deuterated sample, all the observable backbone (1)H(N), (15)N, (13)C(a), 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 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.
摘要
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