分子大象的气相结构是持久的还是短暂的? 时间依赖,并联离子移动性的结果
Benjamin P Zercher1, Seoyeon Hong1, Addison E Roush1
1Department of Chemistry, University of Washington, Box 351700, Seattle, Washington 98195-1700, United States.
Analytical chemistry
|June 9, 2023
概括
气相蛋白离子表现出显著的动力稳定性,保留了溶液相结构. 单体离子可能会随着时间的推移改变形状,但在质谱学实验中,大型蛋白质复合体在结构上保持完整.
科学领域:
- 质谱测量质量谱测量
- 结构生物学 结构生物学
- 生物物理学的生物物理.
背景情况:
- 生物分子在气相中的结构稳定性对于质谱应用至关重要.
- 了解气相离子行为,有助于结构生物学研究.
研究的目的:
- 用时间依赖的离子运动来评估与原生类蛋白质离子的动力稳定性.
- 为了比较时间依赖的结构变化与能量依赖的 (碰撞诱导的展开) 实验.
主要方法:
- 进行了双重离子移动 (IM) 实验,在第一个IM维度后选择离子,并将其捕获长达14秒.
- 在第二个IM维度中测量了依赖时间的碰撞横截面分布.
- 为了进行比较,进行了能源依赖碰撞诱导的展开实验.
主要成果:
- 单质蛋白离子显示结构变化取决于蛋白质类型和电荷状态.
- 大型蛋白质复合体在实验时间范围内没有显著的结构变化.
- 在依赖时间的实验中观察到的结构被动态捕获,保留了溶液相记忆,与高能碰撞中的结构不同.
结论:
- 质量较高的蛋白离子在气相中表现出显著的动力稳定性.
- 虽然高电荷的单体离子可以在结构上演变,但较大的复合体保持其构造.
- 气相离子结构可以保留它们的溶液相形状的记忆.
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