NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.
Journal
Chemical reviews
ISSN: 1520-6890
Titre abrégé: Chem Rev
Pays: United States
ID NLM: 2985134R
Informations de publication
Date de publication:
25 05 2022
25 05 2022
Historique:
pubmed:
22
4
2022
medline:
27
5
2022
entrez:
21
4
2022
Statut:
ppublish
Résumé
Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each assigned resonance in the molecule, unveiling otherwise inaccessible insight into the reaction kinetics and thermodynamics that are essential for function. In this review, we describe recent applications of NMR-based approaches to understanding the conformational energy landscape, the nature and time scales of local and long-range dynamics and how they depend on the environment, even in the cell. Finally, we illustrate the ability of NMR to uncover the mechanistic basis of functional disordered molecular assemblies that are important for human health.
Identifiants
pubmed: 35446534
doi: 10.1021/acs.chemrev.1c01023
pmc: PMC9136928
doi:
Substances chimiques
Intrinsically Disordered Proteins
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
9331-9356Références
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