energy gain decreases along with the entropic component. The hydrophobic effect depends on the temperature, which leads to "cold denaturation" of proteins. The hydrophobic effect can be calculated by comparing the free energy of solvation with bulk water. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions. See also Entropic force Hydrophobe Hydrophile Hydrophobicity scales Interfacial tension Superhydrophobe Superhydrophobic coating References Chemical bonding Supramolecular chemistry Intermolecular forces