SOLUTION SCATTERING STUDIES OF CONFORMATIONS OF METHIONINE SYNTHASE

蛋氨酸合成酶构象的溶液散射研究

• 批准号: 7369170
• 负责人: MARTHA L LUDWIG
• 金额: $ 0.89万
• 依托单位: ILLINOIS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-04-01 至 2007-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7369170
• 关键词: SOLUTION; SCATTERING; STUDIES; CONFORMATIONS; METHIONINE

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 propose to use SAXS to determine the relative arrangements of the methionine synthase domains in solution. The first experiments would examine domain arrangements in the N- and Cterminal halves of the molecule, respectively. These appear to be tractable experiments and all of the proteins are available. Longer-term aims are to examine the distribution of domains in the three-module catalytic units of MetHs from E. coli and T. maritima, and to study the ligand- and temperature-dependence of the ensemble equilibria.

该子项目是利用 NIH/NCRR 资助的中心拨款提供的资源的众多研究子项目之一。子项目和研究者 (PI) 可能已从另一个 NIH 来源获得主要资金，因此可以在其他 CRISP 条目中得到体现。列出的机构是中心的机构，不一定是研究者的机构。我们建议使用 SAXS 来确定溶液中甲硫氨酸合酶结构域的相对排列。第一个实验将分别检查分子 N 端和 C 端部分的结构域排列。这些似乎是易于处理的实验，并且所有蛋白质都是可用的。长期目标是检查大肠杆菌和 T. maritima 的 MetH 的三模块催化单元中结构域的分布，并研究整体平衡的配体依赖性和温度依赖性。