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.
|State||Published - 2021|
Bibliographical noteFunding Information:
This work was supported by the National Science Foundation under Grant No. 1715627, the United States-Israel Bi-national Science Foundation under Grant No. 2016696, and the Israel Science Foundation under Grant Nos. 1454/19.
© 2021 IOP Publishing Ltd.
- Intrinsically disordered proteins
- NMR FCS
- Nanoscopic characterization
- Single-molecule force spectroscopy