STRUCTURE DETERMINATION OF A BRANCH POINT DOMAIN

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。子项目及 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的研究机构。 第二组内含子是天然存在的自我剪接核酶，主要是低等真核生物和细菌，表现出与哺乳动物剪接体相似的催化机制。为了在原子水平上破译剪接体的机制相似性和差异，我们感兴趣的是II组内含子ai 5 g的结构域6中的分支点的确切构象及其对金属离子的存在、浓度和性质的依赖性。为此，我们计划测量D 6的39聚体RNA发夹的残余偶极偶联以及1D NOE实验。

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. Group II introns are naturally occurring self splicing ribozymes of mainly lower eukaryotes and bacteria, that exhibit a similar catalytic mechanism as the mammalian spliceosome. To decipher the mechanistic similarities and differences to the spliceosome on an atomic level, we are interested in the exact conformation of the branch point in domain 6 of the group II intron ai5g and its dependence on the presence, concentration and nature of metal ions. To this end we are planning to measure residual dipolar couplings as well as 1D NOE experiments of our 39mer RNA hairpin of D6.