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 evidences strongly suggest that multiple biological functions stem from such structural plasticity. Here, focusing on the nanoscopic length-scale, we review the latest advances in IDP research and discuss some of the future directions in this highly promising field.
@article{arxiv.2101.06902,
title = {Intrinsically Disordered Proteins at the Nano-scale},
author = {Tamara Ehm and Hila Shinar and Sagi Meir and Amandeep Sekhon and Vaishali Sethi and Ian L. Morgan and Gil Rahamim and Omar A. Saleh and Roy Beck},
journal= {arXiv preprint arXiv:2101.06902},
year = {2021}
}