We have performed all-atom molecular dynamics simulations using GROMACS package. OPLS-AA force field is used to collect the topological parameters for the ammonium-based protein secondary structure stabilizer choline chloride and the protein denaturant urea, which is consistent with our recent works. OPLS-AA performs quite well to reproduce experimentally verified physical properties. For example, in a very recent study, Doherty and Acevedo could reproduce physical properties like density, viscosity, surface tension and heat capacity of ChCl based DES that included urea too, for a wide range of temperature using the OPLS force field. Again in a recent work, Zhu et al. also showed that OPLS-AA force field could effectively reproduce the osmotic coefficient of sixteen drug-like small molecules. The force field parameters of the small molecules used in this investigation are represented elsewhere. To suffice the purpose of force field validation of the small molecules used here, we have computed the bulk densities of the investigated solutions (Table and Fig S1 in Supplementary Information) and compare it with the experimentally verified one. We have found a good agreement between the experimental and simulated bulk density. SPC/E water model is used for our study. A 5000-steps energy minimization is performed for each system using the steepest descent method to remove the initial steric clashes. Subsequently, a 500 ps equilibration under NVT ensemble is performed using the V-rescale thermostat 83 to equilibrate each system at a temperature of 310K and to avoid the possibility of void formation in the simulation box.