Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy
Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy
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DOI：
10.1038/s41565-020-00798-9
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发表时间：
2020-11-23
影响因子：
38.3
通讯作者：
Ando, Toshio
中科院分区：
文献类型：
--
作者：
Kodera, Noriyuki;Noshiro, Daisuke;Ando, Toshio
高速原子力显微镜（AFM）成像技术可以半定量、真实地描述内在无序蛋白质的动态结构，内在无序蛋白质（IDP）是一类普遍存在的完全或部分无序的蛋白质，在多种生物现象中起着重要作用。它们的结构动态地采样了大量的构象状态，从而使得它们的结构分析非常困难。在这里，我们探讨的潜力，高速原子力显微镜（HS-AFM）表征的结构和动态的IDP。IDP分子的连续HS-AFM图像不仅可以识别分子中不断折叠和不断无序的区域，而且还可以记录无序到有序的转变。此外，在这些无序区域中所含的氨基酸的数量可以粗略估计，使一个半定量的，现实的描述的动态结构的IDP。
High-speed AFM imaging enables a semiquantitative, realistic description of the dynamic structure of intrinsically disordered proteins.Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or partly and play important roles in diverse biological phenomena. Their structure dynamically samples a multitude of conformational states, thus rendering their structural analysis very difficult. Here we explore the potential of high-speed atomic force microscopy (HS-AFM) for characterizing the structure and dynamics of IDPs. Successive HS-AFM images of an IDP molecule can not only identify constantly folded and constantly disordered regions in the molecule, but can also document disorder-to-order transitions. Moreover, the number of amino acids contained in these disordered regions can be roughly estimated, enabling a semiquantitative, realistic description of the dynamic structure of IDPs.