The mechanisms underlying synergy between IDPs and cosolutes can differ across other IDP families beyond LEA and CAHS proteins due to the unique structural and functional characteristics of each protein family. For example, other IDP families may have distinct sequence motifs or domains that interact differently with cosolutes, leading to varied effects on protein function. Additionally, the oligomerization behavior, conformational flexibility, and specific interactions with cosolutes can vary among different IDP families, influencing the overall synergy observed. These differences in molecular interactions and structural features contribute to the diverse mechanisms of synergy seen across various IDP families.