Stowers Institute for Medical Research, Kansas City, MO, USA.
Crit Rev Biochem Mol Biol. 2011 Jun;46(3):216-28. doi: 10.3109/10409238.2011.567244. Epub 2011 Mar 26.
Knowledge of structure and dynamics of proteins and protein complexes is important to unveil the molecular basis and mechanisms involved in most biological processes. Protein complex dynamics can be defined as the changes in the composition of a protein complex during a cellular process. Protein dynamics can be defined as conformational changes in a protein during enzyme activation, for example, when a protein binds to a ligand or when a protein binds to another protein. Mass spectrometry (MS) combined with affinity purification has become the analytical tool of choice for mapping protein-protein interaction networks and the recent developments in the quantitative proteomics field has made it possible to identify dynamically interacting proteins. Furthermore, hydrogen/deuterium exchange MS is emerging as a powerful technique to study structure and conformational dynamics of proteins or protein assemblies in solution. Methods have been developed and applied for the identification of transient and/or weak dynamic interaction partners and for the analysis of conformational dynamics of proteins or protein complexes. This review is an overview of existing and recent developments in studying the overall dynamics of in vivo protein interaction networks and protein complexes using MS-based methods.
了解蛋白质和蛋白质复合物的结构和动态对于揭示大多数生物过程中涉及的分子基础和机制非常重要。蛋白质复合物的动态可以定义为在细胞过程中蛋白质复合物组成的变化。蛋白质动力学可以定义为酶激活过程中蛋白质构象的变化，例如，当蛋白质与配体结合或当蛋白质与另一个蛋白质结合时。质谱 (MS) 与亲和纯化相结合已成为绘制蛋白质-蛋白质相互作用网络的首选分析工具，而定量蛋白质组学领域的最新发展使得鉴定动态相互作用的蛋白质成为可能。此外，氢/氘交换 MS 正在成为研究溶液中蛋白质或蛋白质组装体结构和构象动力学的强大技术。已经开发和应用了方法来鉴定瞬时和/或弱动态相互作用伴侣，并分析蛋白质或蛋白质复合物的构象动力学。本综述概述了使用基于 MS 的方法研究体内蛋白质相互作用网络和蛋白质复合物整体动态的现有和最新进展。
