(2) h⊕t,V (z), that is nearly identical to the free energy profile of DS - binding to the ACWI. Additionally, the tail effects on the total solute-solvent energy and entropy, ∆ t E h⊕t,V and -T ∆ t S h⊕t,V are qualitatively similar to the hydrophobc DS 0 solute-solvent energy and entropy profiles, reflecting the fact that the hydrophobic "head" group on DS 0 does not qualitatively change the adsorption thermodynamics for the ACWI. The differences between the solid and dashed lines show the head-solvent reorganization energy and entropy terms, which are relatively small. Fig. shows the tail effect on the binding of DS -to the AWI. As was the case for DS -binding to the ACWI, the tail effects in the AWI are qualitatively similar to the thermodynamics of DS 0 binding to the AWI. Additionally, the head-solvent reorganization effects are small for DS -binding to the AWI.