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

POWRE：寡聚化的固态 NMR 研究：大肠杆菌硫氧还蛋白的 B 链拉链

• 批准号: 0075115
• 负责人: Maria Luisa Tasayco
• 金额: --
• 依托单位: CUNY City College
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-09-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=0075115&HistoricalAwards=false
• 关键词: POWRE; Solid; State; NMR; Studies

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.

Tasayco0075115这项研究的目的是通过b链的拉链建立无序多肽链齐聚的基本原理。氧化的大肠杆菌硫氧还蛋白是一个由108个残基组成的单域a/b蛋白，通过片段互补得到了很好的研究，它为在缺乏完全互补片段的情况下研究寡聚提供了一个独特的机会。片段1-37自组装形成大分子量均聚体，并与片段74-108相互作用形成杂寡体。将使用最近开发的固态核磁共振(SS核磁共振)方法以及互补的生化和生物物理标准技术来确定拓扑结构，以检查这些同质和异质低聚物。固体核磁共振方法是进行低聚物详细结构分析的有力工具。这是POWRE的一项建议，PI是研究片段互补识别蛋白质的领先者，与附近机构的一位在SS核磁共振方面经验丰富的同事合作，并学习这些技术。