SELF ASSOCIATION PROPERTIES OF HISTIDINE KINASE CHEA

组氨酸激酶 Chea 的自联特性

• 批准号: 8364040
• 负责人: JAYA BHATNAGAR
• 金额: $ 0.3万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-09-01 至 2012-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8364040
• 关键词: Binding; Disulfides; Funding; Grant; Magnetism; National Center for Research Resources; Physiologic pulse; Principal Investigator; Property; Research; Research Infrastructure; Resources; Solutions; Source; Structure; Technology; United States National Institutes of Health; cost; 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其他NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 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。