| Literature DB >> 35179885 |
Anton Abyzov1, Martin Blackledge2,3,4, Markus Zweckstetter1,5.
Abstract
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.Entities:
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Year: 2022 PMID： 35179885 PMCID： PMC8949871 DOI： 10.1021/acs.chemrev.1c00774
Source DB: PubMed Journal: Chem Rev ISSN： 0009-2665 Impact factor: 60.622