Intrinsically disordered proteins at the nano-scale

T. Ehm, H. Shinar, S. Meir, A. Sekhon, V. Sethi, I. L. Morgan, G. Rahamim, O. A. Saleh, R. Beck

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


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.

Original languageEnglish
Article number022501
JournalNano Futures
Issue number2
StatePublished - 2021
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2021 IOP Publishing Ltd.


  • FRET
  • Intrinsically disordered proteins
  • Nanoscopic characterization
  • SAXS
  • Single-molecule force spectroscopy


Dive into the research topics of 'Intrinsically disordered proteins at the nano-scale'. Together they form a unique fingerprint.

Cite this