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.

中文翻译：

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纳米级的固有无序蛋白质

人类蛋白质组富含不会折叠成稳定 3D 结构的蛋白质。这些本质上无序的蛋白质 (IDP) 在其天然形式的大量构型之间自发地波动。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，最近的证据强烈表明多种生物学功能源于这种结构可塑性。在这里，重点关注纳米长度尺度，我们回顾了 IDP 研究的最新进展，并讨论了这个极具前景的领域的一些未来方向。