Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry.
Journal
Chemical reviews
ISSN: 1520-6890
Titre abrégé: Chem Rev
Pays: United States
ID NLM: 2985134R
Informations de publication
Date de publication:
23 03 2022
23 03 2022
Historique:
pubmed:
19
2
2022
medline:
26
4
2022
entrez:
18
2
2022
Statut:
ppublish
Résumé
Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical reactions are executed inside of biomolecular condensates formed by ultradynamic intrinsically disordered proteins. A deep understanding of the conformational dynamics of intrinsically disordered proteins in biomolecular condensates is therefore of utmost importance but is complicated by diverse obstacles. Here we review emerging data on the motions of intrinsically disordered proteins inside of liquidlike condensates. We discuss how liquid-liquid phase separation modulates internal motions across a wide range of time and length scales. We further highlight the importance of intermolecular interactions that not only drive liquid-liquid phase separation but appear as key determinants for changes in biomolecular motions and the aging of condensates in human diseases. The review provides a framework for future studies to reveal the conformational dynamics of intrinsically disordered proteins in the regulation of biomolecular condensate chemistry.
Identifiants
pubmed: 35179885
doi: 10.1021/acs.chemrev.1c00774
pmc: PMC8949871
doi:
Substances chimiques
Intrinsically Disordered Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
6719-6748Références
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