Intrinsically disordered proteins at the nano-scale
Intrinsically disordered proteins at the nano-scale
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DOI：
10.1088/2399-1984/abfb7c
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发表时间：
2021-06-01
期刊：
影响因子：
2.1
通讯作者：
Beck, R.
中科院分区：
文献类型：
--
作者：
Ehm, T.;Shinar, H.;Beck, R.
人类蛋白质组富含不能折叠成稳定的3D结构的蛋白质。这些内在无序的蛋白质（IDP）自发地在其天然形式的大量构型之间波动。值得注意的是，这种疾病不会像变性折叠蛋白那样导致功能障碍。事实上，与变性蛋白质不同，最近的证据有力地表明，多种生物功能源于这种结构可塑性。在这里，我们集中在纳米尺度上，回顾了IDP研究的最新进展，并讨论了这个非常有前途的领域的一些未来方向。
The human proteome is enriched in proteins that do not fold into a stable 3D structure. These intrinsically disordered proteins (IDPs) spontaneously fluctuate between a large number of configurations in their native form. Remarkably, the disorder does not lead to dysfunction as with denatured folded proteins. In fact, unlike denatured proteins, recent evidence strongly suggests that multiple biological functions stem from such structural plasticity. Here, focusing on the nanometer length-scale, we review the latest advances in IDP research and discuss some of the future directions in this highly promising field.