SOLUTION SCATTERING STUDIES OF CONFORMATIONS OF METHIONINE SYNTHASE

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。 我们一直在使用SAXS来确定蛋氨酸合成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-半端和CT端半端的结构域排列。这些似乎是容易处理的实验，所有的蛋白质都是可用的。较长期的目标是检查来自大肠杆菌和毛滴虫的甲基的三模块催化单元中结构域的分布，并研究系综平衡的配体和温度依赖性。

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.