Liquid-liquid (L-L) type phase transitions in water-salt dispersions of native (N*, N) globular proteins in the temperature range between thermal (D*) and cold (D) denaturation have been considered. Protein intermediates (I, I*) arising as a result of the ion non-equilibrium (de)sorption in the process of D↔N and D*↔N* transitions are assumed to be involved in the L-L phase transition forming clusters and fibrils in the main phase of N and N* proteins. Thus, they compensate for their excess chemical potential (ChPot) caused by unbalanced distribution of adsorbed salt ions in protein structure as compared to N protein. A temperature model for the behavior of ChPots (∆µi) of various states of the protein (low-temperature i = D, N, I and high-temperature i = D*, N*, I*, transitions between them), as well as the temperature dependence of the solvent ChPot (∆µ1) are presented in the form of phase diagrams. The relationship between the values of ∆µ1 and the temperatures of L-L transitions (upper and lower critical solution temperatures) as well as the reasons for the nonideal behavior of osmotic pressure in water-salt protein dispersions are discussed on this basis.
protein intermediates, clusters, liquid-liquid phase transitions, phase diagram, osmotic pressure
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