Detergent Release Prolongs the Lifetime of Native-like Membrane Protein Conformations in the Gas-Phase
Detergent Release Prolongs the Lifetime of Native-like Membrane Protein Conformations in the Gas-Phase
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DOI：
10.1021/ja401736v
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发表时间：
2013-04-24
影响因子：
15
通讯作者：
Robinson, Carol V.
中科院分区：
文献类型：
--
作者：
Borysik, Antoni J.;Hewitt, Dominic J.;Robinson, Carol V.
最近的研究表明，去污剂可以保护膜蛋白的结构，在他们从溶液到气相的转变。在这里，我们提供了这一过程的机制的见解，通过询问膜蛋白洗涤剂组件的结构，在气相中使用离子迁移质谱。我们显示了一个明确的相关性之间的人口的天然蛋白质构象和洗涤剂附着的蛋白质在气相中的程度。这些蛋白质洗涤剂组件的询问，通过串联质谱，使我们能够定义的机制，洗涤剂保持天然样蛋白质构象在无溶剂的环境中。我们表明，释放洗涤剂是更中央的生存这些构象比洗涤剂结合到蛋白质的物理存在。我们建议，洗涤剂释放竞争与结构崩溃的离子的内部能量，并允许观察瞬态天然样膜蛋白构象，否则失去了在气相中的结构重排。
Recent studies have suggested that detergents can protect the structure of membrane proteins during their transition from solution to the gas-phase. Here we provide mechanistic insights into this process by interrogating the structures of membrane protein-detergent assemblies in the gas-phase using ion mobility mass spectrometry. We show a clear correlation between the population of native-like protein conformations and the degree of detergent attachment to the protein in the gas-phase. Interrogation of these protein-detergent assemblies, by tandem mass spectrometry, enables us to define the mechanism by which detergents preserve native-like protein conformations in a solvent free environment. We show that the release of detergent is more central to the survival of these conformations than the physical presence of detergent bound to the protein. We propose that detergent release competes with structural collapse for the internal energy of the ion and permits the observation of transient native-like membrane protein conformations that are otherwise lost to structural rearrangement in the gas-phase.