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Decoding the role of DNA sequence on protein-DNA co-condensation
Fig 5
Sequence heterogeneity in partial 
-DNA engenders multiple condensates as metastable states.
A Schematic represents the Partial 
-DNA: Eleven kinds of monomers (yellow to maroon) are introduced, based on AT content of 10 base pairs, modeled as one monomer. The monomer-protein binding affinities vary in the range of 0.1 to 4 kBT depending on the AT content of the corresponding 10 bp motif that represents the monomer (see the model section). Proteins (green) bind to each other with an affinity of 2 kBT. B Snapshots shown for five independent realizations at 
and 
=84.50 
(top to down). C, D Representative kymograph showing visualization of coarsening kinetics for replicate 2 and 5. E Scaled radius of the larger condensate (black) and smaller condensate (red) is shown for replicate 2 which leads to a single condensate at equilibrium. F Scaled radius of the larger condensate (black) and smaller condensate (red) is shown for replicate 5 which shows coexistence of two condensates as a kinetically trapped state. G Bar plots show the average interfacial affinity (maroon) and volume (orange) for two condensates observed in the case of replicates 1, 4, and 5.
doi: https://doi.org/10.1371/journal.pcbi.1013829.g005