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: 7601753
• 负责人: MARTHA L LUDWIG
• 金额: $ 1.18万
• 依托单位: ILLINOIS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-04-01 至 2008-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601753
• 关键词: Computer Retrieval of Information on Scientific Projects Database; Dependence; Equilibrium; Escherichia coli; Funding; Grant; Institution; Ligands; Methionine; Molecular Conformation; Proteins; Relative (related person); Research; Research Personnel; Resources; Solutions; Source; Temperature; United States National Institutes of Health; 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 have been using 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.

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。 我们一直在使用小角X射线散射来确定甲硫氨酸合酶结构域在溶液中的相对排列。第一个实验将分别检查分子的N-和C-末端半部分的结构域排列。这些似乎是易于处理的实验，所有的蛋白质都是可用的。长期的目标是研究结构域的分布在三个模块的催化单位的MetH从E。coli和T. maritima，并研究配体和温度依赖的合奏平衡。