NMR and EPR studies of membrane transporters
NMR and EPR studies of membrane transporters
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DOI：
10.1515/bc.2009.084
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发表时间：
2009-08-01
影响因子：
3.7
通讯作者：
Glaubitz, Clemens
中科院分区：
文献类型：
--
作者：
Hellmich, Ute A.;Glaubitz, Clemens
为了完成它们的功能，膜转运蛋白必须经过一系列构象和/或能量状态的循环。因此，了解构象动力学的作用似乎是阐明这些蛋白质作用机制的关键。然而，膜蛋白通常很难异源表达，而且在结构研究中也很难有足够的量。捕获一个稳定的能量极小值尤其具有挑战性，例如用于晶体分析。此外，结晶通常只有通过使蛋白质处于与其自然环境不同的条件下才可能实现，而晶体只能是选定构象状态的快照。核磁共振(核磁共振)和电子顺磁共振(EPR)谱是相互补充的方法，它们为研究膜蛋白在自然膜环境中的变化以及膜转运蛋白的功能构象变化、脂质相互作用、底物-脂质和底物-蛋白质相互作用、齐聚状态和整体动力学提供了独特的可能性。在这里，我们综述了该领域的最新进展，包括来自初级和次级活性转运蛋白的研究。
In order to fulfill their function, membrane transport proteins have to cycle through a number of conformational and/or energetic states. Thus, understanding the role of conformational dynamics seems to be the key for elucidation of the functional mechanism of these proteins. However, membrane proteins in general are often difficult to express heterologously and in sufficient amounts for structural studies. It is especially challenging to trap a stable energy minimum, e. g., for crystallographic analysis. Furthermore, crystallization is often only possible by subjecting the protein to conditions that do not resemble its native environment and crystals can only be snapshots of selected conformational states. Nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy are complementary methods that offer unique possibilities for studying membrane proteins in their natural membrane environment and for investigating functional conformational changes, lipid interactions, substrate-lipid and substrate-protein interactions, oligomerization states and overall dynamics of membrane transporters. Here, we review recent progress in the field including studies from primary and secondary active transporters.