Phase Separation and Single-Chain Compactness of Charged Disordered Proteins Are Strongly Correlated

Liquid-liquid phase separation of intrinsically disordered proteins (IDPs) is a major undergirding factor in the regulated formation of membraneless organelles in the cell. The phase behavior of an IDP is sensitive to its amino acid sequence. Here we apply a recent random-phase-approximation polymer theory to investigate how the tendency for multiple chains of a protein to phase-separate, as characterized by the critical temperature T∗cr, is related to the protein's single-chain average radius of gyration 〈Rg〉.

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