NATIVE ESI AND ECD OF NATIVE PROTEIN COMPLEXES

天然蛋白质复合物的天然 ESI 和 ECD

• 批准号: 8361429
• 负责人: MICHAEL L GROSS
• 金额: $ 0.94万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-01-01 至 2011-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361429
• 关键词: Biological Process; Cells; Development; Dissociation; Fourier transform ion cyclotron resonance; Funding; Grant; Mass Spectrum Analysis; Methods; National Center for Research Resources; Principal Investigator; Proteins; Proteomics; Research; Research Infrastructure; Resources; SHFM1 gene; Source; Structure-Activity Relationship; Techniques; Technology; United States National Institutes of Health; base; biomedical resource; cost; insight; ion mobility; macromolecular assembly; protein complex; research study; structural biology; tandem mass spectrometry

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Many biological functions are performed by protein complexes. With the development of modern proteomics technology, all the proteins in cells can be identified. The next step is to study the interactions of various proteins in terms of structure-function relationship. So far the popular approach is Q-TOF with the assistance of ion mobility technique to characterize those macromolecular assemblies in native form. Standard bottom-up proteomics is used to identify the constituent components after the whole assembly is denatured and enzymaticall digested. Various fragmentation methods, especially collisionally activated dissociation (CAD), employed in tandem mass spectrometry are used to break the whole assembly into smaller pieces to obtain insights into how the subunits interact with each other. We recently developed a top-down approach to obtain proteomics and structural biology information in one experiment based on the Bruker 12 tesla FTICR platform.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 许多生物学功能是由蛋白质复合物执行的。随着现代蛋白质组学技术的发展，细胞内的所有蛋白质都可以被识别。下一步是从结构-功能关系的角度研究各种蛋白质的相互作用。到目前为止，流行的方法是 Q-TOF 借助离子淌度技术来表征这些天然形式的大分子组装体。标准的自下而上蛋白质组学用于在整个组件变性和酶消化后鉴定其组成成分。串联质谱中采用的各种裂解方法，尤其是碰撞激活解离 (CAD)，可将整个组装体分解成更小的片段，以深入了解亚基如何相互作用。我们最近开发了一种自上而下的方法，可在基于 Bruker 12 tesla FTICR 平台的实验中获取蛋白质组学和结构生物学信息。