We employ molecular dynamics simulations and the reference interaction site model (RISM) integral equation theory to Study the solvation structure and solvation thermodynamics of the transfer process from water to a water-Urea mixture. Simple positive and negative ions together With uncharged species of the same size are used as Crude models for the hydrophilic and hydrophobic groups of a protein. We find that Urea preferentially solvates positively charged species. The solvation free energies obtained indicate that larger Solutes favor the transfer from water to a water-Urea mixture. The decomposition of the transfer free energy into the energetic and entropic terms shows that the energetic part is much larger than the entropic one and tends to dominate the transfer process, Supporting the direct mechanism Of Urea-denaturation. In addition, the effect Of urea on the water liquid Structure is discussed from the viewpoint of solvation entropy.