Protein Water Interaction

It has long been recognized that protein-water interactions play an important role in the determination and maintenance of the three-dimensional structure of proteins. Water in proteins involves stability, dynamics, and function of the proteins (46). Important states of water molecules surrounding protein molecules are structural water and monolayer water. The structural water refers to the water molecules that are part of the protein structure bound through hydrogen bonding. These 10-20 water molecules per protein molecule are unavailable for chemical reactions. The monolayer water refers to the water molecules tightly bound to the protein surface via dipole-induced dipole (hydrophobic hydration), ion-dipole (ionic hydration), and dipole-dipole (hydrogen bonding) interactions. At the saturated monolayer coverage, most proteins absorb about 0.3-0.5 g of water per gram of protein. This bound water is unfreezable and does not participate in any chemical reaction. Unlike the monolayer water, the multilayer water is available for chemical reactions, but some of these water molecules are unfreezable (47).

Most proteins exhibit the least water-binding capacity and solubility at isoelectric pH, presumably because of protonation of the carboxyl groups and enhanced hydrophobic interaction between protein molecules (47).

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