Czaplewski Cezary, Gong Zhou, Lubecka Emilia A, Xue Kai, Tang Chun, Liwo Adam
Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland.
Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan, China.
Front Mol Biosci. 2021 Dec 24;8:765562. doi: 10.3389/fmolb.2021.765562. eCollection 2021.
Many proteins can fold into well-defined conformations. However, intrinsically-disordered proteins (IDPs) do not possess a defined structure. Moreover, folded multi-domain proteins often digress into alternative conformations. Collectively, the conformational dynamics enables these proteins to fulfill specific functions. Thus, most experimental observables are averaged over the conformations that constitute an ensemble. In this article, we review the recent developments in the concept and methods for the determination of the dynamic structures of flexible peptides and proteins. In particular, we describe ways to extract information from nuclear magnetic resonance small-angle X-ray scattering (SAXS), and chemical cross-linking coupled with mass spectroscopy (XL-MS) measurements. All these techniques can be used to obtain ensemble-averaged restraints or to re-weight the simulated conformational ensembles.
许多蛋白质能够折叠成明确的构象。然而，内在无序蛋白（IDP）并不具有确定的结构。此外，折叠的多结构域蛋白常常偏离为其他构象。总体而言，构象动力学使这些蛋白质能够履行特定功能。因此，大多数实验观测结果是在构成一个系综的构象上进行平均的。在本文中，我们综述了用于确定柔性肽和蛋白质动态结构的概念和方法的最新进展。特别地，我们描述了从核磁共振、小角X射线散射（SAXS）以及化学交联结合质谱（XL-MS）测量中提取信息的方法。所有这些技术都可用于获得系综平均约束或对模拟的构象系综进行重新加权。
