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The 31 pages that link to Hydrophobic effect, each with the reason it gives.

• SolvationRelated: Its explanation depends on how water reorganizes around nonpolar solutes.

• Protein foldingRelated: It drives many nonpolar amino-acid side chains toward a protein’s interior.

• Protein denaturationRelated: Denaturation can expose buried nonpolar regions that normally cluster inside a folded protein.

• SurfactantRelated: It drives surfactant tails away from water and toward oils or one another.

• Van der Waals forceCompared with: This solvent-mediated effect can involve van der Waals attraction but is not itself a van der Waals force.

• Protein structureRelated: It often drives nonpolar side chains toward the interior of soluble proteins.

• Lipid bilayerRelated: This effect drives lipid tails away from water and toward the bilayer interior.

• MicelleRelated: It helps drive hydrophobic regions into the micelle’s interior.

• Membrane proteinRelated: It helps drive hydrophobic protein surfaces into the bilayer’s lipid interior.

• AmphiphileRelated: It drives amphiphilic tails to cluster away from water.

• Molecular recognitionRelated: Burial of nonpolar surfaces often contributes substantially to molecular association in aqueous environments.

• HydrophobicityRelated: It explains why nonpolar molecules cluster rather than remain dispersed in water.

• TryptophanRelated: Tryptophan's aromatic side chain often settles at protein interiors or membrane interfaces.

• Intrinsically disordered proteinCompared with: Unlike many compact globular proteins, disordered proteins often remain soluble despite exposed hydrophobic residues.

• CoagulationRelated: Unfolding exposes nonpolar protein regions that can associate during coagulation.

• PhenylalanineRelated: Its nonpolar aromatic side chain often favors burial within protein interiors.

• Phospholipid bilayerRelated: It pushes phospholipid tails away from water and helps assemble the bilayer.

• Critical micelle concentrationRelated: This effect helps drive surfactant tails to cluster inside micelles.

• Noncovalent interactionRelated: It drives association in aqueous environments, though it is not itself a simple pairwise force.

• FluoropolymersRelated: Fluorinated surfaces often resist wetting, though surface behavior depends on structure and treatment.

• Molecular self-assemblyRelated: It drives many amphiphilic molecules to form membranes and micelles in water.

• Supramolecular chemistryRelated: This solvent-driven effect organizes aqueous assemblies, including micelles and biological structures.

• WaxesRelated: Waxes’ nonpolar chains make their surfaces resist wetting by water.

• LeucineRelated: Leucine’s nonpolar side chain often packs into protein interiors.

• Fatty alcoholRelated: The long hydrocarbon portions of fatty alcohols avoid contact with water.

• LipophilicityRelated: It helps explain why nonpolar surfaces favor association with lipids rather than aqueous surroundings.

• Cetyl alcoholRelated: The long nonpolar chain avoids water and helps cetyl alcohol associate with oils.

• HydrophileCompared with: It describes the opposing behavior that helps distinguish water affinity from water avoidance.

• HydrophobicityRelated: It describes the solvent-driven mechanism behind many forms of hydrophobicity.

• 1-OctanolRelated: The eight-carbon chain resists water, shaping 1-octanol's limited aqueous solubility.

• Sodium dodecyl sulfateRelated: Sodium dodecyl sulfate’s hydrocarbon tail associates with nonpolar regions of proteins and oily materials.