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

doi:10.1088/2399-1984/abfb7c

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

Tel Aviv University

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Article number	022501
Journal	Nano Futures
Volume	5
Issue number	2
DOIs	https://doi.org/10.1088/2399-1984/abfb7c
State	Published - 2021

Keywords

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

All Science Journal Classification (ASJC) codes

Bioengineering
General Chemistry
Atomic and Molecular Physics, and Optics
Biomedical Engineering
General Materials Science
Electrical and Electronic Engineering

Access to Document

10.1088/2399-1984/abfb7c

Cite this

@article{8c1a3ea4598042dc94c8fedaed4e2793,

title = "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.",

keywords = "FRET, Intrinsically disordered proteins, NMR FCS, Nanoscopic characterization, SAXS, Single-molecule force spectroscopy",

author = "T. Ehm and H. Shinar and S. Meir and A. Sekhon and V. Sethi and Morgan, {I. L.} and G. Rahamim and Saleh, {O. A.} and R. Beck",

note = "Publisher Copyright: {\textcopyright} 2021 IOP Publishing Ltd.",

year = "2021",

doi = "10.1088/2399-1984/abfb7c",

language = "الإنجليزيّة",

volume = "5",

journal = "Nano Futures",

issn = "2399-1984",

publisher = "Institute of Physics Publishing",

number = "2",

}

TY - JOUR

T1 - Intrinsically disordered proteins at the nano-scale

AU - Ehm, T.

AU - Shinar, H.

AU - Meir, S.

AU - Sekhon, A.

AU - Sethi, V.

AU - Morgan, I. L.

AU - Rahamim, G.

AU - Saleh, O. A.

AU - Beck, R.

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

KW - FRET

KW - Intrinsically disordered proteins

KW - NMR FCS

KW - Nanoscopic characterization

KW - SAXS

KW - Single-molecule force spectroscopy

UR - http://www.scopus.com/inward/record.url?scp=85108617847&partnerID=8YFLogxK

U2 - 10.1088/2399-1984/abfb7c

DO - 10.1088/2399-1984/abfb7c

M3 - مقالة

SN - 2399-1984

VL - 5

JO - Nano Futures

JF - Nano Futures

IS - 2

M1 - 022501

ER -

Intrinsically disordered proteins at the nano-scale

Abstract

Keywords

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this