Effects of charge on protein ion structure: Lessons from cation‐to‐anion, proton‐transfer reactions
Effects of charge on protein ion structure: Lessons from cation‐to‐anion, proton‐transfer reactions
复制标题
电荷对蛋白质离子结构的影响：从阳离子到阴离子、质子转移反应的经验教训
DOI：
10.1002/mas.21847
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发表时间：
2023
影响因子：
6.6
通讯作者：
Bush, Matthew F.
中科院分区：
文献类型：
--
作者：
Gozzo, Theresa A.;Bush, Matthew F.
碰撞截面值可以通过离子迁移率实验确定，对蛋白质离子的结构敏感，可用于结构生物学和生物物理学。具有不同电荷状态的蛋白质离子可以表现出非常不同的碰撞截面值，但对这种关系的全面理解仍然是难以捉摸的。在这里，我们回顾阳离子到阴离子质子转移反应（CAPTR），一种通过四极选择阳离子与偶电子单阴离子反应产生一系列电荷减少的蛋白质阳离子的方法。使用离子迁移率、质谱和碰撞活化的组合分析所得CAPTR产物。我们将CAPTR与其他电荷操纵策略进行比较，并回顾各种基于CAPTR的实验结果，探索它们对更深入理解蛋白质离子结构和电荷状态之间关系的贡献。
Collision cross‐section values, which can be determined using ion mobility experiments, are sensitive to the structures of protein ions and useful for applications to structural biology and biophysics. Protein ions with different charge states can exhibit very different collision cross‐section values, but a comprehensive understanding of this relationship remains elusive. Here, we review cation‐to‐anion, proton‐transfer reactions (CAPTR), a method for generating a series of charge‐reduced protein cations by reacting quadrupole‐selected cations with even‐electron monoanions. The resulting CAPTR products are analyzed using a combination of ion mobility, mass spectrometry, and collisional activation. We compare CAPTR to other charge‐manipulation strategies and review the results of various CAPTR‐based experiments, exploring their contribution to a deeper understanding of the relationship between protein ion structure and charge state.