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在四极杆/飞行时间质谱仪中,离子淌度分离的非共价复合物的表面诱导解离。

Surface-induced dissociation of ion mobility-separated noncovalent complexes in a quadrupole/time-of-flight mass spectrometer.

机构信息

Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721-0041, United States.

出版信息

Anal Chem. 2012 Jul 17;84(14):6016-23. doi: 10.1021/ac300810u. Epub 2012 Jun 29.

DOI:10.1021/ac300810u
PMID:22747517
Abstract

A custom in-line surface-induced dissociation (SID) device has been incorporated into a commercial ion mobility quadrupole/time-of-flight mass spectrometer in order to provide an alternative and potentially more informative activation method than the commonly used collision-induced dissociation (CID). Complicated sample mixtures can be fractionated by ion mobility (IM) and then dissociated by CID or SID for further structural analysis. Interpretation of SID spectra for cesium iodide clusters was greatly simplified with IM prior to dissociation because products originating from different precursors and overlapping in m/z but separated in drift time can be examined individually. Multiple conformations of two protein complexes, source-activated transthyretin tetramer and nativelike serum amyloid P decamer, were separated in ion mobility and subjected to CID and SID. CID spectra of the mobility separated conformations are similar. However, drastic differences can be observed for SID spectra of different conformations, implying different structures in the gas phase. This work highlights the potential of utilizing IM-SID to study quaternary structures of protein complexes and provides information that is complementary to our recently reported SID-IM approach.

摘要

为了提供一种不同于常用的碰撞诱导解离(CID)的替代且可能更具信息量的激活方法,我们将定制的在线表面诱导解离(SID)装置集成到了商业的离子淌度四极杆/飞行时间质谱仪中。复杂的样品混合物可以通过离子淌度(IM)进行分离,然后通过 CID 或 SID 进行解离,以进行进一步的结构分析。在解离之前进行 IM 可以大大简化碘化铯团簇的 SID 谱的解释,因为在 m/z 上重叠但在漂移时间上分离的来自不同前体的产物可以单独进行检查。两种蛋白质复合物,即源激活转甲状腺素蛋白四聚体和天然血清淀粉样蛋白 P 十聚体,在离子淌度中得到分离,并进行 CID 和 SID。经淌度分离的构象的 CID 谱相似。然而,不同构象的 SID 谱可以观察到明显的差异,这表明气相中存在不同的结构。这项工作强调了利用 IM-SID 研究蛋白质复合物的四级结构的潜力,并提供了与我们最近报道的 SID-IM 方法互补的信息。

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