REVIEWS ON PROTEOMICS - AEBERSOLD

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 蛋白质组学的主要目标之一是描述多蛋白模块的组成、动力学和连接，这些模块催化细胞中广泛的生物学功能。质谱（MS）已被证明是一个非常强大的工具，用于表征纯化的复合物的组成。然而，由于MS不是定量技术，因此数据的有用性有限。例如，在没有定量测量的情况下，难以检测复合物组成的动态变化，并且可能难以区分真正的复合物组分与非特异性共纯化蛋白质。在这一章中，我们描述了一种策略，通过结合亲和纯化方法与稳定同位素标记和MS的组合物的蛋白质复合物的组成和它们的动态变化的特征。还描述了使用软件工具的数据进行统计分析。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. One of the primary goals of proteomics is the description of the composition, dynamics, and connections of the multiprotein modules that catalyze a wide range of biological functions in cells. Mass spectrometry (MS) has proven to be an extremely powerful tool for characterizing the composition of purified complexes. However, because MS is not a quantitative technique, the usefulness of the data is limited. For example, without quantitative measurements, it is difficult to detect dynamic changes in complex composition, and it can be difficult to distinguish bona fide complex components from nonspecifically copurifying proteins. In this chapter, we describe a strategy for characterizing the composition of protein complexes and their dynamic changes in composition by combining affinity purification approaches with stable isotope tagging and MS. The use of software tools for statistical analysis of the data is also described.