Suppr超能文献

通过动能和信号衰减分析将轨道阱碰撞截面测量扩展到天然蛋白质应用

Expanding Orbitrap Collision Cross-Section Measurements to Native Protein Applications Through Kinetic Energy and Signal Decay Analysis.

作者信息

James Virginia K, Sanders James D, Aizikov Konstantin, Fort Kyle L, Grinfeld Dmitry, Makarov Alexander, Brodbelt Jennifer S

机构信息

Department of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.

Thermo Fisher Scientific, Bremen 28199, Germany.

出版信息

Anal Chem. 2023 May 16;95(19):7656-7664. doi: 10.1021/acs.analchem.3c00594. Epub 2023 May 3.

Abstract

The measurement of collision cross sections (CCS, σ) offers supplemental information about sizes and conformations of ions beyond mass analysis alone. We have previously shown that CCSs can be determined directly from the time-domain transient decay of ions in an Orbitrap mass analyzer as ions oscillate around the central electrode and collide with neutral gas, thus removing them from the ion packet. Herein, we develop the modified hard collision model, thus deviating from the prior FT-MS hard sphere model, to determine CCSs as a function of center-of-mass collision energy in the Orbitrap analyzer. With this model, we aim to increase the upper mass limit of CCS measurement for native-like proteins, characterized by low charge states and presumed to be in more compact conformations. We also combine CCS measurements with collision induced unfolding and tandem mass spectrometry experiments to monitor protein unfolding and disassembly of protein complexes and measure CCSs of ejected monomers from protein complexes.

摘要

碰撞截面(CCS,σ)的测量提供了超出单纯质量分析的关于离子大小和构象的补充信息。我们之前已经表明,在轨道阱质谱分析仪中,当离子围绕中心电极振荡并与中性气体碰撞从而从离子包中移除时,可以直接根据离子的时域瞬态衰减来确定CCS。在此,我们开发了改进的硬碰撞模型,从而偏离了先前的傅里叶变换质谱(FT-MS)硬球模型,以确定轨道阱分析仪中作为质心碰撞能量函数的CCS。通过这个模型,我们旨在提高对天然样蛋白质的CCS测量的质量上限,这类蛋白质的特征是低电荷态且假定处于更紧凑的构象。我们还将CCS测量与碰撞诱导展开和串联质谱实验相结合,以监测蛋白质复合物的展开和拆卸,并测量从蛋白质复合物中弹出的单体的CCS。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验