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这项研究的目的是建立通过B链的拉链来建立无序多肽链的低聚的原理。氧化大肠杆菌硫氧还蛋白的片段是通过片段互补很好地研究的108个残基的单个结构域A /B蛋白，在没有完全互补的片段的情况下为研究寡聚的独特机会提供了独特的机会。片段1-37自组装以产生大分子量的同性恋者，并与片段74-108相互作用以形成异弱者。将使用最近开发的固态核磁共振（SSNMR）方法以及互补的生化和生物物理标准技术来检查这些同源和杂酸体，以确定拓扑结构。固态核磁共振方法是用于详细的低聚物结构分析的强大工具。这是POWRE的建议，对于PI，通过片段补充研究蛋白质识别的领导者，与附近的机构中经验丰富的同事合作，并学习这些技术。