Multiple analyses of protein dynamics in solution
Multiple analyses of protein dynamics in solution
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溶液中蛋白质动力学的多重分析
DOI：
10.1007/s12551-017-0354-7
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发表时间：
2017
影响因子：
--
通讯作者：
Hirokawa Nobutaka
中科院分区：
文献类型：
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作者：
Ogawa Tadayuki;Hirokawa Nobutaka
对蛋白质在溶液中行为的准确描述的需求在各个领域都变得重要，包括生物物理学、生物化学、结构生物学、药物发现和抗体药物。为了达到所需的准确度，应该对目标分子进行多次精确分析，比较并有效组合。本文主要介绍了分子排阻色谱（SEC）、多角光散射（MALS）、小角X射线散射（SAXS）、分析超离心（AUC）以及原子力显微镜（AFM）和质谱（MS）等多种分析方法的组合。我们还讨论了确定的摩尔质量值之间的比较，不仅标准的蛋白质，但作为一个例子的靶分子微管蛋白和其解聚蛋白，KIF2。不同方法的估计摩尔质量值的比较提供了关于靶分子的额外信息，因为该值反映了溶液中靶分子的动态变化状态。多种方法的结合和整合将使人们更深入地了解溶液中的蛋白质动力学。
The need for accurate description of protein behavior in solution has gained importance in various fields, including biophysics, biochemistry, structural biology, drug discovery, and antibody drugs. To achieve the desired accuracy, multiple precise analyses should be performed on the target molecule, compared, and effectively combined. This review focuses on the combination of multiple analyses in solution: size-exclusion chromatography (SEC), multi-angle light scattering (MALS), small-angle X-ray scattering (SAXS), analytical ultracentrifugation (AUC), and their complementary methods, such as atomic force microscopy (AFM) and mass spectrometry (MS). We also discuss the comparison between the determined molar mass value of not only the standard proteins, but of a target molecule tubulin and its depolymerizing protein, KIF2, as an example. The comparison of the estimated molar mass value from the different methods provides additional information about the target molecule, because the value reflects the dynamically changing states of the target molecule in solution. The combination and integration of multiple methods will permit a deeper understanding of protein dynamics in solution.