Abstract
Liquid-liquid phase separation (LLPS) is now widely recognized to occur in a broad variety of cellular interactions, particularly inside the nucleus. Here, we have developed a coarse-grain (CG) model for the LLPS of intrinsically-disordered proteins (IDPs) together with nucleic acids (NAs). The model allows us to probe the effects of changing the salt concentration and protein charge patterning on IDP-NA LLPS. We use as our model peptide the disordered C-terminus of histone H1 (CH1), which phase separates with short dsDNA fragments at physiological salt concentrations.
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