ArticleBiomacromolecules2025
Cationic Amino Acid Identity and Net Charge Influence Condensate Properties in
Article in Biomacromolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Biomolecular condensates (BMCs) are central to subcellular organization, influencing processes from RNA metabolism to the stress response and amyloid pathologies. Despite their near ubiquity, we still do not fully understand how the primary sequence of biomolecules influences the formation and dynamics of condensates. Here, we examine how cationic amino acid identity shapes the properties of protein-RNA coacervates. Using engineered recombinant proteins, we find that phase boundaries depend on both amino acid identity and protein net charge. Despite identical charge at physiological pH, arginine promotes a higher salt resistance in vitro, enhanced condensate formation in
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