POWRE: Solid State NMR Studies of Oligomerization: Zippering B-Strands from E. Coli Thioredoxin

Tasayco 0075115本研究的目的是通过B链的拉链化建立无序多肽链寡聚化的基本原理。氧化型E.大肠杆菌硫氧还蛋白是一种108个残基的单结构域a /B蛋白，通过片段互补得到了很好的研究，为在缺乏完全互补片段的情况下研究寡聚化提供了独特的机会。片段1-37自组装以产生大分子量的同源寡聚物，并且还与片段74-108相互作用以形成异源寡聚物。这些同源和异源寡聚体将使用最近开发的固态核磁共振（SSNMR）方法，以及互补的生物化学和生物物理标准技术，以确定拓扑结构进行检查。固态核磁共振方法是对低聚物进行详细结构分析的有力工具。这是一个POWRE建议，PI是研究片段互补蛋白质识别的领导者，与附近机构的一位在SSNMR方面经验丰富的同事合作，并学习这些技术。

Tasayco0075115The objective of this research is to establish the principles underlying oligomerization of disordered polypeptide chains through the zippering of b strands. Fragments of oxidized E. coli thioredoxin, a single domain a /b proteins of 108 residues well studied by fragment complementation, provide a unique opportunity to study oligomerization in the absence of the fully complementary fragment. The fragment 1-37 self assembles to produce large molecular weight homo-oligomers, and also interacts with fragment 74-108 to form hetero-oligomers. These homo and hetero-oligomers will be examined using recently developed solid-state nuclear magnetic resonance (SSNMR) methods, as well as complementary biochemical and biophysical standard techniques to determine the topology. Solid state nuclear magnetic resonance methodologies are a powerful tool for detailed structural analysis of oligomers. This is a POWRE proposal, for the PI, a leader in studying protein recognition by fragment complementation, to collaborate with a colleague in a nearby institution who is experienced in SSNMR, and to learn these techniques.