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- W4210955266 abstract "Protein aggregates are typically more thermodynamically stable than the native and unfolded states, under physiologically relevant conditions. Therefore, if protein structure were under thermodynamic control, many proteins would be largely aggregated above their critical concentration, both in vitro and within living organisms. Here, we show that many proteins are kinetically protected from forming insoluble aggregates under physiologically relevant conditions. This kinetic control of protein solubility applies to some unicellular systems on a proteome-wide scale, and it persists over time spans longer than the organism doubling time." @default.
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- W4210955266 date "2022-02-01" @default.
- W4210955266 modified "2023-09-27" @default.
- W4210955266 title "Exploring kinetically controlled protein solubility under physiologically relevant conditions" @default.
- W4210955266 doi "https://doi.org/10.1016/j.bpj.2021.11.1801" @default.
- W4210955266 hasPublicationYear "2022" @default.
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