Native mass spectrometry is applied for the investigation of proteins and protein complexes worldwide. The challenge in native mass spectrometry is maintaining the features of the proteins of interest, such as oligomeric state, bound ligands, or the conformation of the protein complex, during transfer from solution to gas phase. This is an essential prerequisite to allow conclusions about the solution state protein complex, based on the gas phase measurements. Therefore, soft ionization techniques are required. Widely used for the analysis of protein complexes are nanoelectro spray ionization (nESI) mass spectrometers. A newer ionization method is laser induced liquid bead ion desorption (LILBID), which is based on the release of protein complexes from solution phase via infrared (IR) laser desorption. We use both methods in our lab, depending on the requirements of the biological system we are interested in. Here we benchmark the performance of our LILBID mass spectrometer in comparison to a nESI instrument, regarding sample conditions, buffer and additive tolerances, dissociation mechanism and applicability towards soluble and membrane protein complexes. Graphical Abstract ᅟ.

中文翻译：

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LILBID和nESI：不同的天然质谱技术作为结构生物学的工具。

天然质谱法被用于研究全世界的蛋白质和蛋白质复合物。天然质谱的挑战是在从溶液到气相的转移过程中保持目标蛋白质的特征，如低聚状态，结合的配体或蛋白质复合物的构象。这是必要的前提条件，可以根据气相测量结果得出有关溶液状态蛋白质复合物的结论。因此，需要软电离技术。纳米电喷雾电离（nESI）质谱仪广泛用于蛋白质复合物的分析。激光诱导液珠离子解吸（LILBID）是一种较新的电离方法，该方法基于通过红外（IR）激光解吸从溶液相释放蛋白质复合物的过程。我们在实验室中同时使用两种方法，取决于我们感兴趣的生物学系统的要求。在这里，我们将LILBID质谱仪的性能与nESI仪器进行比较，涉及样品条件，缓冲液和添加剂的耐受性，解离机理以及对可溶性和膜蛋白复合物的适用性。图形摘要ᅟ。