SELF ASSOCIATION PROPERTIES OF HISTIDINE KINASE CHEA

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 我们观察到由CHEA的结构域P3-P4-P5组成的CheA289在溶液中弱聚集。在晶体结构中，CheA289分子通过P5结构域亚结构域2末端的疏水界面相互作用。我们利用磁稀释实验、二硫化物交联实验和脉冲偶极ESR实验进一步研究了这种结合界面。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We observed that CheA289, which is composed of domains P3-P4-P5 of CheA weakly aggregates in solution. In the crystal structure, CheA289 molecules associate with each other via a hydrophobic interface at the end of sub-domain 2 of P5 domain. We use magnetic dilution experiments, disulphide cross-linking experiments and pulsed dipolar ESR to further investigate this binding interface.