Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel.
J Am Soc Mass Spectrom. 2010 Apr;21(4):487-500. doi: 10.1016/j.jasms.2009.12.017. Epub 2010 Jan 4.
Physical interactions between proteins and the formation of stable complexes form the basis of most biological functions. Therefore, a critical step toward understanding the integrated workings of the cell is to determine the structure of protein complexes, and reveal how their structural organization dictates function. Studying the three-dimensional organization of protein assemblies, however, represents a major challenge for structural biologists, due to the large size of the complexes, their heterogeneous composition, their flexibility, and their asymmetric structure. In the last decade, mass spectrometry has proven to be a valuable tool for analyzing such noncovalent complexes. Here, I illustrate the breadth of structural information that can be obtained from this approach, and the steps taken to elucidate the stoichiometry, topology, packing, dynamics, and shape of protein complexes. In addition, I illustrate the challenges that lie ahead, and the future directions toward which the field might be heading.
蛋白质之间的物理相互作用和稳定复合物的形成是大多数生物功能的基础。因此，理解细胞综合运作的关键步骤是确定蛋白质复合物的结构，并揭示其结构组织如何决定功能。然而，由于复合物的体积庞大、组成异质、结构灵活且不对称，研究蛋白质组装的三维组织对结构生物学家来说是一个重大挑战。在过去的十年中，质谱已被证明是分析这种非共价复合物的一种有价值的工具。在这里，我说明了可以从这种方法获得的结构信息的广度，以及为阐明蛋白质复合物的计量学、拓扑结构、包装、动态和形状而采取的步骤。此外，我还说明了未来面临的挑战和该领域可能的发展方向。
