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- W4311683533 abstract "Abstract Many biological macromolecules can phase-separate in the cell and form highly concentrated condensates. The mesoscopic dynamics of these assemblies have been widely characterized, but their behavior at the molecular scale has remained more elusive. Here we investigate condensates of two highly charged disordered human proteins as a characteristic example of liquid-liquid phase separation. The dense phase is 1000 times more concentrated and has 300 times higher bulk viscosity than the dilute phase. However, single-molecule spectroscopy in individual droplets reveals that the polypeptide chains are remarkably dynamic, with sub-microsecond reconfiguration times. We rationalize this behavior with large-scale all-atom molecular-dynamics simulations, which reveal an unexpectedly similar short-range molecular environment in the dense and dilute phases, suggesting that local biochemical processes and interactions can remain exceedingly rapid in phase-separated systems." @default.
- W4311683533 created "2022-12-28" @default.
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- W4311683533 date "2022-12-14" @default.
- W4311683533 modified "2023-10-18" @default.
- W4311683533 title "Ultrafast molecular dynamics observed within a dense protein condensate" @default.
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- W4311683533 doi "https://doi.org/10.1101/2022.12.12.520135" @default.
- W4311683533 hasPublicationYear "2022" @default.
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