Cropley Tyler C, Chai Mengqi, Liu Fanny C, Bleiholder Christian
Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, USA.
Department of Chemistry, Washington University in St. Louis, Saint-Louis, Missouri, USA.
Front Anal Sci. 2023;3. doi: 10.3389/frans.2023.1106752. Epub 2023 Jan 18.
Cellular processes are usually carried out collectively by the entirety of all proteins present in a biological cell, i.e. the proteome. Mass spectrometry-based methods have proven particularly successful in identifying and quantifying the constituent proteins of proteomes, including different molecular forms of a protein. Nevertheless, protein sequences alone do not reveal the function or dysfunction of the identified proteins. A straightforward way to assign function or dysfunction to proteins is characterization of their structures and dynamics. However, a method capable to characterize detailed structures of proteins and protein complexes in a large-scale, systematic manner within the context of cellular processes does not yet exist. Here, we discuss the potential of -ion mobility / mass spectrometry (tandem-IM/MS) methods to provide such ability. We highlight the capability of these methods using two case studies on the protein systems ubiquitin and avidin using the tandem-TIMS/MS technology developed in our laboratory and discuss these results in the context of other developments in the broader field of tandem-IM/MS.
细胞过程通常是由生物细胞中存在的所有蛋白质整体，即蛋白质组共同执行的。基于质谱的方法在鉴定和定量蛋白质组的组成蛋白质（包括蛋白质的不同分子形式）方面已证明特别成功。然而，仅蛋白质序列并不能揭示所鉴定蛋白质的功能或功能障碍。将功能或功能障碍赋予蛋白质的一种直接方法是对其结构和动力学进行表征。然而，目前还不存在一种能够在细胞过程的背景下大规模、系统地表征蛋白质和蛋白质复合物详细结构的方法。在这里，我们讨论了淌度离子迁移/质谱（串联IM/MS）方法提供这种能力的潜力。我们使用在我们实验室开发的串联TIMS/MS技术，通过关于泛素和抗生物素蛋白这两种蛋白质系统的两个案例研究，突出了这些方法的能力，并在串联IM/MS更广泛领域的其他进展背景下讨论了这些结果。
