Joseph L Watson, Estere Seinkmane, Christine T Styles, Andrei Mihut, Lara K Krüger, Kerrie E McNally, Vicente Jose Planelles-Herrero, Michal Dudek, Patrick M McCall, Silvia Barbiero, Michael Vanden Oever, Sew Yeu Peak-Chew, Benjamin T Porebski, Aiwei Zeng, Nina M Rzechorzek, David C S Wong, Andrew D Beale, Alessandra Stangherlin, Margot Riggi, Janet Iwasa, Jörg Morf, Christos Miliotis, Alina Guna, Alison J Inglis, Jan Brugués, Rebecca M Voorhees, Joseph E Chambers, Qing-Jun Meng, John S O'Neill, Rachel S Edgar, Emmanuel Derivery
Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and macromolecular interactions1 . Reciprocally, macromolecules restrict the movement of 'structured' water molecules within their hydration layers, reducing the available 'free' bulk solvent and therefore the total thermodynamic potential energy of water, or water potential. Here, within concentrated macromolecular solutions such as the cytosol, we found that modest changes in temperature greatly affect the water potential, and are counteracted by opposing changes in osmotic strength...
October 18, 2023: Nature