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- W4212888384 endingPage "6748" @default.
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- W4212888384 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." @default.
- W4212888384 created "2022-02-24" @default.
- W4212888384 creator A5001250430 @default.
- W4212888384 creator A5003373050 @default.
- W4212888384 creator A5033249566 @default.
- W4212888384 date "2022-02-18" @default.
- W4212888384 modified "2023-10-18" @default.
- W4212888384 title "Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry" @default.
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