In the literature, it is reported that the phase-separating behavior of disordered proteins can be generally associated with their single-chain compactness, and the sequencedeterminant of the compaction of disordered proteins is not only related to the overall protein charge, but also affected by the organization of charged and aromatic residues along the length . At physiological pH, DHH1N is electrostatically neutral, but its charged residues, i.e., negatively-charged Asp and positively-charged Lys, Arg, are mostly focused within the C-terminal portion of the sequence from Asp16 onwards.