Macromolecular condensation buffers intracellular water potential

• Published in: Nature (London) Vol. 623; no. 7988; pp. 842 - 852
• Main Authors: Watson, Joseph L., Seinkmane, Estere, Styles, Christine T., Mihut, Andrei, Krüger, Lara K., McNally, Kerrie E., Planelles-Herrero, Vicente Jose, Dudek, Michal, McCall, Patrick M., Barbiero, Silvia, Vanden Oever, Michael, Peak-Chew, Sew Yeu, Porebski, Benjamin T., Zeng, Aiwei, Rzechorzek, Nina M., Wong, David C. S., Beale, Andrew D., Stangherlin, Alessandra, Riggi, Margot, Iwasa, Janet, Morf, Jörg, Miliotis, Christos, Guna, Alina, Inglis, Alison J., Brugués, Jan, Voorhees, Rebecca M., Chambers, Joseph E., Meng, Qing-Jun, O’Neill, John S., Edgar, Rachel S., Derivery, Emmanuel
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 23.11.2023; Nature Publishing Group
• Subjects: 13; 13/62; 14; 14/19; 631/45/470; 631/57/2269; 631/80; 631/80/458; Cell Death; Cytosol - chemistry; Cytosol - metabolism; Denaturation; Homeostasis; Humanities and Social Sciences; Hydration; Hydrogen; Intracellular; Kinases; Low temperature; Macromolecular Substances - chemistry; Macromolecular Substances - metabolism; Macromolecules; Molecular dynamics; multidisciplinary; Osmolar Concentration; Pressure; Protein denaturation; Protein folding; Proteins; Proteins - chemistry; Proteins - metabolism; Science; Science (multidisciplinary); Solvents; Solvents - chemistry; Solvents - metabolism; Temperature; Temperature dependence; Thermodynamics; Time Factors; Water - chemistry; Water - metabolism; Water availability; Water content; Water potential

Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and macromolecular interactions 1 . Reciprocally, macromolecules restrict the movement of ‘structured’ water molecules within their hydration layers, reduci...