Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments - Archive ouverte HAL Access content directly
Journal Articles Progress in Nuclear Magnetic Resonance Spectroscopy Year : 2018

Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments

Sigrid Milles
Nicola Salvi
Martin Blackledge

Abstract

Over the last two decades, it has become increasingly clear that a large fraction of the human proteome is intrinsically disordered or contains disordered segments of significant length. These intrinsically disordered proteins (IDPs) play important regulatory roles throughout biology, underlining the importance of understanding their conformational behavior and interaction mechanisms at the molecular level. Here we review recent progress in the NMR characterization of the structure and dynamics of IDPs in various functional states and environments. We describe the complementarity of different NMR parameters for quantifying the conformational propensities of IDPs in their isolated and phosphorylated states, and we discuss the challenges associated with obtaining structural models of dynamic protein-protein complexes involving IDPs. In addition, we review recent progress in understanding the conformational behavior of IDPs in cell-like environments such as in the presence of crowding agents, in membrane-less organelles and in the complex environment of the human cell.
No file

Dates and versions

hal-01995911 , version 1 (28-01-2019)

Identifiers

Cite

Sigrid Milles, Nicola Salvi, Martin Blackledge, Malene Ringkjøbing Jensen. Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments. Progress in Nuclear Magnetic Resonance Spectroscopy, 2018, 109, pp.79-100. ⟨10.1016/j.pnmrs.2018.07.001⟩. ⟨hal-01995911⟩
58 View
0 Download

Altmetric

Share

Gmail Facebook X LinkedIn More