Department of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Adv Exp Med Biol. 2018;1105:101-121. doi: 10.1007/978-981-13-2200-6_8.
During the last two decades, cross-linking combined with mass spectrometry (MS) has evolved as a valuable tool to gain structural insights into proteins and protein assemblies. Structural information is obtained by introducing covalent connections between amino acids that are in spatial proximity in proteins and protein complexes. The distance constraints imposed by the cross-linking reagent provide information on the three-dimensional arrangement of the covalently connected amino acid residues and serve as basis for de-novo or homology modeling approaches. As cross-linking/MS allows investigating protein 3D-structures and protein-protein interactions not only in-vitro, but also in-vivo, it is especially appealing for studying protein systems in their native environment. In this chapter, we describe the principles of cross-linking/MS and illustrate its value for investigating protein 3D-structures and for unraveling protein interaction networks.
在过去的二十年中，交联结合质谱（MS）已发展成为一种获取蛋白质和蛋白质复合物结构见解的有价值的工具。通过在空间上接近的氨基酸之间引入共价连接来获得结构信息，这些氨基酸存在于蛋白质和蛋白质复合物中。交联试剂施加的距离约束提供了共价连接的氨基酸残基的三维排列的信息，并作为从头或同源建模方法的基础。由于交联/MS 不仅可以在体外，还可以在体内研究蛋白质的 3D 结构和蛋白质-蛋白质相互作用，因此特别适合研究其天然环境中的蛋白质系统。在本章中，我们描述了交联/MS 的原理，并说明了其在研究蛋白质 3D 结构和揭示蛋白质相互作用网络方面的价值。
