在没有溶剂的情况下蛋白质溶液结构的转变稳定性:坚固的能量景观和类似玻璃的行为

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Tyler C Cropley¹, Fanny C Liu¹, Mengqi Chai¹

¹Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida 32304, United States.

Journal of the American Chemical Society

|April 10, 2024

概括

原生离子流动性质谱显示,无溶剂的无素保留了原生折叠. 这种技术在真空中探测蛋白质结构,显示蛋白质展开速度在没有溶剂的情况下要慢得多,这表明溶剂有助于蛋白质运动.

科学领域:

生物化学
结构生物学
质谱学

背景情况:

原生离子移动性质谱 (IM-MS) 是一种用于蛋白质组结构查的强大工具.
然而,IM-MS在没有溶剂的环境中描述了蛋白质结构,这引发了关于生物相关性的问题.
在没有溶剂的情况下了解蛋白质的行为对于解释IM-MS数据至关重要.

研究的目的:

通过使用新的计算和实验IM-MS方法在无溶剂环境中研究ubiquitin的展开.
为了确定无溶剂 ubiquitin 的结构完整性和动态性.
为了比较无溶剂和溶液状态下的泛素的展开路径.

主要方法:

使用新开发的计算和实验性离子移动/离子移动/质谱 (IM-IM/MS) 技术.
在无溶剂条件下研究了无素的展开动态.
进行时间解析的IM-IM/MS测量和分子动力学模拟.

主要成果:

无溶剂的乌比基保持了很大程度上本地折叠,包括β-抓取动机和α-螺旋.
蛋白质呈现出动态稳定的子群体,反映出溶液结构的异质性.
在无溶剂条件下,展开速度常数比在水中小800-20,000倍,有效地阻止了展开.
展开的路径与溶液相路径有相似之处,表明一个保存的机制.

结论:

无溶剂蛋白质的能量格局很粗,类似于玻璃系统.
蛋白质动力学受到氨基酸序列的显著影响.
溶剂在蛋白质运动中起到促进作用,而不是控制作用.

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