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Potassium and sodium ions are crucial for many physiological processes inliving systems and play different roles when interacting with proteins andenzymes. Intracellular concentration of potassium is always maintained higherthan that of sodium, which provides a suitable environment for biochemicalmachinery. These cations also possess different properties in physico-chemicalHofmeister phenomena. It is now accepted that the main physical reason forthese ion-specific effects is due to formation of ion pairs. The greaterability of sodium over potassium to destabilize protein solutions waspreviously rationalized by sodium stronger pairing with carboxylates, which arethe main anionic moiety of proteins. While ion pairing of cations withcarboxylates was studied in detail previously, understanding of the molecularmechanisms of cation-specific mediation of protein-protein interactions isstill lacking. In this work with the use of molecular dynamics we studied theeffect of sodium and potassium on interactions between model compounds thatbear typical positively and negatively charged groups of proteins, namely,methylammonium and acetate molecules. We found only a weak difference in thecontacts of charged groups depending on the cation type present in thesolution. Our results suggest that a strength of cation-carboxylate binding isnot critical, but structural features may be more important.

Specific and non-specific effects of sodium and potassium ions on the interactions between model charged groups of proteins