S. Pylaeva, H. Elgabarty, and D. Sebastiani
Theoretical Chemistry, Institute of Chemistry, Martin Luther University Halle-Wittenberg, Von-Danckelmann-Platz 4, 06120, Halle, Germany
Salt bridges are important components of protein structure stability. They can be defined as an interaction of two aminoacid side chains of opposite charge . Such Coulomb attraction interaction is sensitive to presence of other charged species in the vicinity. Concentration of charged species – free ions can be significant in a crowded environment of a living cell. Additionally Hofmeister ion series have been shown to have a significant impact on structure and dynamics of water and solvated proteins [2, 3].
We have investigated effects of Hofmeister ion series on an arginine – aspartic acid salt bridge by means of computer simulations . Changes in thermodynamic properties of a salt bridge and dynamic properties of their solvation shells will be discussed in a poster.
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