SELF ASSOCIATION PROPERTIES OF HISTIDINE KINASE CHEA

组氨酸激酶 Chea 的自联特性

• 批准号: 7956725
• 负责人: JAYA BHATNAGAR
• 金额: $ 0.22万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-09-01 至 2010-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7956725
• 关键词: Binding; Computer Retrieval of Information on Scientific Projects Database; Disulfides; Funding; Grant; Institution; Magnetism; Physiologic pulse; Property; Research; Research Personnel; Resources; Solutions; Source; Structure; Technology; United States National Institutes of Health; crosslink; protein-histidine kinase; research study

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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 我们观察到，289，其由CheA的结构域P3-P4-P5组成，在溶液中弱聚集。在晶体结构中，CheA289个分子通过P5结构域的亚结构域2末端的疏水界面相互结合。我们使用磁稀释实验，二硫化物交联实验和脉冲偶极ESR进一步研究这种结合界面。