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Solubilities of potassium chloride (KCl) and sodium chloride (NaCl) in aqueous systems containing the ionic liquid 1-butyl-3-methylimidazolium chloride ([Bmim]Cl) were determined by cloud-point measurements using the laser beam scattering method in a temperature range of (298.15 to 343.15) K at atmospheric pressure. The solubility data were correlated and calculated with the Pitzer model modified by Harvie and Weare. The interaction parameters of the mixed-electrolyte solution were obtained using experimental results. It was found that the addition of [Bmim]Cl leads to salting-out, triggering a marked decrease of salt solubility in the aqueous solutions. The results also show that [Bmim]Cl has different salting-out ratios on KCl and NaCl in the mass-fraction range of w [Bmim]Cl = (0.025 to 0.20). It is also shown that the modified Pitzer model gives a satisfactory prediction for the solubilities of KCl and NaCl in aqueous systems containing ionic liquid [Bmim]Cl.' EXPERIMENTAL SECTION Chemical Materials. KCl and NaCl (AR reagents from Shanghai Lingfeng chemical reagent factory) with a mass fraction purity greater than 0.998 were dried in a vacuum oven at 373.5 K

Understanding the interactions of drug molecules with biomacromolecules at a micro-scale level is essential to design potent drugs for the treatments of human genome diseases. To unravel the mechanism of binding of aristololactam-b-D-glucoside (ADG) and phenylalanine transfer RNA (tRNA Phe ), an integrated computational strategy combining quantum mechanics (QM) calculation, molecular docking and atomistic molecular dynamics (MD) simulation was present in this work. QM calculations were performed to derive the partial charges of ADG, molecular docking was used to determine the binding poses of ADG on the tRNA Phe , and atomistic MD simulations were conducted to examine the thermal stability of five predicted binding poses for the complex of ADG and the tRNA Phe . The binding free energies of the five complexes were then calculated using the molecular mechanics/generalized born surface area approach with the variable internal dielectric constant model. By comparing computed affinities and experimentally-measured values in the binding free energy, we identified a most likely binding structure of ADG and the tRNA Phe . Further analysis of energy of the ADG-tRNA complex revealed that the aristololactam of ADG provides binding specificity to the tRNA Phe , and the D-glucoce contributes to the affinity for binding with the tRNA Phe .[a] Dr.