期刊
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
卷 109, 期 -, 页码 79-100出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pnmrs.2018.07.001
关键词
Intrinsically disordered proteins; Post-translational modifications; Membrane-less organelles; Dynamic complexes; Conformational exchange
资金
- French Agence Nationale de la Recherche through ANR JCJC NMRSignal
- EMBO long-term fellowship [ALTF 468-2014]
- EC (EMBOCO-FUND2012) via Marie Curie Action [GA-2012-600394]
- Swiss National Science Foundation Advanced Postdoc Mobility Fellowship [P300P2_167742]
- French Agence Nationale de la Recherche through ANR T-ERC MAPKassembly
- Swiss National Science Foundation (SNF) [P300P2_167742] Funding Source: Swiss National Science Foundation (SNF)
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. (C) 2018 Elsevier B.V. All rights reserved.
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