Intrinsically disordered proteins at the nano-scale
Abstract
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.
- Publication:
-
Nano Futures
- Pub Date:
- June 2021
- DOI:
- 10.1088/2399-1984/abfb7c
- arXiv:
- arXiv:2101.06902
- Bibcode:
- 2021NanoF...5b2501E
- Keywords:
-
- intrinsically disordered proteins;
- nanoscopic characterization;
- single-molecule force spectroscopy;
- SAXS;
- FRET;
- NMR FCS;
- Physics - Biological Physics;
- Condensed Matter - Mesoscale and Nanoscale Physics;
- Condensed Matter - Soft Condensed Matter;
- Quantitative Biology - Biomolecules;
- Quantitative Biology - Quantitative Methods
- E-Print:
- 15 pages, 5 figures