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. Author manuscript; available in PMC: 2023 Sep 12.
Published in final edited form as: Phys Rev Lett. 2022 Jan 21;128(3):038102. doi: 10.1103/PhysRevLett.128.038102

FIG. 2.

FIG. 2.

MD simulations reveal the importance of stoichiometry to the dynamical properties of the condensate. (a) MD model for the multivalent associative proteins. Colored spheres represent A and B domains. (b) Representative snapshot of the dense, network-forming liquid condensate. (c) Bond relaxation time (see text) as a function of stoichiometry for different binding strengths. Symbols indicate MD simulations; solid curves indicate theory [Eq. (1)] with cAB estimated assuming full binding of the minority domains and with fitted values vcage=11.4, v0=0.4, and τ0=0.37. (d) Bond relaxation time τrel as a function of binding strength is consistent with predicted scaling for both equal and unequal stoichiometries [Eq. (1), Fig. 1(g)]. (e) Mean squared displacement (MSD) of individual domains as a function of time reveals diffusive scaling (dashed line) at long times (here δ=0). (f) Diffusion coefficient of the minority species as a function of binding strength at equal and unequal stoichiometry. (g) Longtime diffusion coefficient plotted against bond relaxation time, for all values of δ and ΔF. The dotted black line indicates Dτrel-1. Transparent circles correspond to systems where one component is in large excess, |δ|>0.2ctot. (h) Viscosity, obtained using the Green-Kubo relation, as a function of binding strength, reflects the scaling of the bond relaxation time (d).