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- W3119082520 startingPage "1015" @default.
- W3119082520 abstract "Many intrinsically disordered proteins (IDPs) in nature may undergo liquid–liquid phase separation to assemble membraneless organelles with varied liquid-like properties and stability/dynamics. While solubility changes underlie these properties, little is known about hydration dynamics in phase-separating IDPs. Here, by studying IDP polymers of similar composition but distinct liquid-like dynamics and stability upon separation, namely, thermal hysteresis, we probe at a nanoscopic level hydration/dehydration dynamics in IDPs as they reversibly switch between phase separation states. Using continuous-wave electron paramagnetic resonance (CW EPR) spectroscopy, we observe distinct backbone and amino acid side-chain hydration dynamics in these IDPs. This nanoscopic view reveals that side-chain rehydration creates a dynamic water shield around the main-chain backbone that effectively and counterintuitively prevents water penetration and governs IDP solubility. We find that the strength of this superficial water shell is a sequence feature of IDPs that encodes for the stability of their phase-separated assemblies. Our findings expose and offer an initial understanding of how the complexity of nanoscopic water–IDP interactions dictate their rich phase separation behavior." @default.
- W3119082520 created "2021-01-18" @default.
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- W3119082520 date "2021-01-06" @default.
- W3119082520 modified "2023-09-24" @default.
- W3119082520 title "Nanoscopic Dynamics Dictate the Phase Separation Behavior of Intrinsically Disordered Proteins" @default.
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- W3119082520 doi "https://doi.org/10.1021/acs.biomac.0c01768" @default.
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- W3119082520 hasPublicationYear "2021" @default.
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