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1. Hydrophobic Interaction

   Linked via "hydrophobic effect"

   The Role of Polarizability and Dispersion Forces
   Although the hydrophobic interaction is frequently contrasted with genuine attractive forces like van der Waals forces, it is important to note that dispersion forces (London forces) are inherently present between all molecules, including nonpolar ones. The aggregation driven by the hydrophobic effect significantly increases the surface area available for these instantaneous dipole-induced dipole interactions betwe…

2. Protein Denaturation

   Linked via "hydrophobic effect"

   Thermodynamic Basis and Entropic Considerations
   The denaturation process is fundamentally an alteration in the Gibbs free energy ($\Delta G$) of the system. For a protein to unfold spontaneously, the free energy change must be negative ($\Delta G < 0$). In many biological contexts, denaturation is driven by unfavorable shifts in the hydrophobic effect, where nonpolar side chains, previously sequestered in the protein core, become exposed to the aqueous solvent.
   The change in entropy ($\Delta S$) plays a c…

3. Van Der Waals Forces

   Linked via "hydrophobic effect"

   Van der Waals Forces and Solvent Effects
   In solution chemistry, van der Waals forces play a critical, often subtle, role, particularly in mediating the hydrophobic effect. While the hydrophobic interaction is primarily driven by entropic changes related to the structured layering of water molecules around nonpolar solutes, the actual physical contact between aggregated nonpolar molecules is stabilized by [dispersi…