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 [1]. 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 [4]. Changes in thermodynamic properties of a salt bridge and dynamic properties of their solvation shells will be discussed in a poster.
References
[1] J.E. Donald, D.W. Kulp, W.F. DeGrado, Proteins, 79(3), 898 (2011). (link)
[2] C. Allolio, N. Salas-Illanes, Y.S. Desmukh, M.R. Hansen, D. Sebastiani, JPCB 117(34), 9939 (2013) (link)
[3] M.D. Smith, L. Cruz, JPCB 117, 6614 (2013) (link)
[4] M. Fyta, R. Netz, JCP 136, 124103 (2012). (link)