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.
Highlights
Motions in biomolecules are critical for biochemical reactions
Förster resonance energy transfer fluorescence correlation spectroscopy probes contact formation (
Polarizable force fields were proposed to better simulate water−protein interactions.[206−208] Additional improvements concerning force field backbone torsional angle sampling[203,209−212] were proposed, including an introduction of a specific sampling for residues enriched in disordered regions.[213−217] despite a remarkable progress achieved in the development of force fields and water models improving the quality of reproduction of experimental observables,[198] there are still disagreements in particular between the helical propensity of intrinsically disordered proteins (IDPs) calculated from an molecular dynamics (MD) trajectory and derived from nuclear magnetic resonance (NMR) data, requiring a residuespecific fine-tuning of force field parameters.[218]
Summary
NMR relaxation dispersion detects a contribution to NMR spin relaxation rates that is due to magnetization dephasing by interconversion between different conformations having distinct chemical shifts or transverse relaxation rates. P granules flowed off the nuclei, dripped, and fused into larger drops as classical liquids Their viscosity and surface tension values were close to typical values observed in colloidal and macromolecular liquids, and their contents exist in dynamic equilibrium with surrounding liquid. Their localization behavior inside germ cells could be explained by the ability of their components to transition between a soluble form and a dropletlike condensed phase. Review molecule concentration that often takes the form of liquidlike droplets and a surrounding diluted phase with low molecule concentration (Figure 1) This process is inherent to the thermodynamics of liquids.
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