Effects of Hofmeister Ions on the Hydrogen Bonding of Methyl Acetate

Effects of Hofmeister Ions on the Hydrogen Bonding of Methyl Acetate

Protein-salt interactions are prevalent in biochemical mechanisms, therefore, gaining a better understanding of these interactions would prove useful in understanding biochemical pathways. The Hofmeister series classifies ions in order of their ability to salt out or salt in proteins. However, the exact mechanism by which this occurs is unknown. Recent simulation studies have shown that interactions between ions and the water molecules contacting the proteins may underlie the mechanism of the Hofmeister series. In this study, temperature dependent FTIR spectroscopy is used to measure the effect of various cations and anions on the hydrogen bonding intermolecular forces of methyl acetate in deuterium oxide solutions. The enthalpy and entropy values are then used to determine potential ionic trends as concentrations are increased. The effects of sodium bromide are currently under study.