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.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 许多生物学功能由蛋白质复合物进行。随着现代蛋白质组学技术的发展，可以鉴定出细胞中的所有蛋白质。下一步是研究各种蛋白质在结构功能关系方面的相互作用。到目前为止，流行的方法是在离子迁移率技术的帮助下Q-TOF来表征本机形式的大分子组件。标准的自下而上的蛋白质组学用于识别整个组件变性并消化酶促的成分。在串联质谱法中采用的各种碎片化方法，尤其是碰撞激活的解离（CAD）（CAD），用于将整个组件分解为较小的片段，以获取有关亚基如何相互相互作用的见解。我们最近开发了一种自上而下的方法，以基于Bruker 12 Tesla Fticr平台的一个实验中获取蛋白质组学和结构生物学信息。