Back تأثير كره الماء Arabic Efecte hidròfob Catalan Hydrophober Effekt German Interacción hidrofóbica Spanish اثر آبگریز Persian Hydrofobinen vuorovaikutus Finnish Effet hydrophobe French Efecto hidrófobo Galician אפקט הידרופובי HE जलविरोधी प्रभाव Hindi

Hydrophobic effect

A droplet of water forms a spherical shape, minimizing contact with the hydrophobic leaf.
Cocoa powder, an example of a "hydrophobic substance".

The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and to be excluded by water.[1][2] The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes the entropy of water and minimizes the area of contact between water and nonpolar molecules. In terms of thermodynamics, the hydrophobic effect is the free energy change of water surrounding a solute.[3] A positive free energy change of the surrounding solvent indicates hydrophobicity, whereas a negative free energy change implies hydrophilicity.

The hydrophobic effect is responsible for the separation of a mixture of oil and water into its two components. It is also responsible for effects related to biology, including: cell membrane and vesicle formation, protein folding, insertion of membrane proteins into the nonpolar lipid environment and protein-small molecule associations. Hence the hydrophobic effect is essential to life.[4][5][6][7] Substances for which this effect is observed are known as hydrophobes.

  1. ^ IUPAC, Compendium of Chemical Terminology, 2nd ed. (the "Gold Book") (1997). Online corrected version: (2006–) "hydrophobic interaction". doi:10.1351/goldbook.H02907
  2. ^ Chandler D (2005). "Interfaces and the driving force of hydrophobic assembly". Nature. 437 (7059): 640–7. Bibcode:2005Natur.437..640C. doi:10.1038/nature04162. PMID 16193038. S2CID 205210634.
  3. ^ Schauperl, M; Podewitz, M; Waldner, BJ; Liedl, KR (2016). "Enthalpic and Entropic Contributions to Hydrophobicity". Journal of Chemical Theory and Computation. 12 (9): 4600–10. doi:10.1021/acs.jctc.6b00422. PMC 5024328. PMID 27442443.
  4. ^ Kauzmann W (1959). "Some factors in the interpretation of protein denaturation". Advances in Protein Chemistry Volume 14. Vol. 14. pp. 1–63. doi:10.1016/S0065-3233(08)60608-7. ISBN 9780120342143. PMID 14404936. {{cite book}}: |journal= ignored (help)
  5. ^ Charton M, Charton BI (1982). "The structural dependence of amino acid hydrophobicity parameters". Journal of Theoretical Biology. 99 (4): 629–644. Bibcode:1982JThBi..99..629C. doi:10.1016/0022-5193(82)90191-6. PMID 7183857.
  6. ^ Lockett MR, Lange H, Breiten B, Heroux A, Sherman W, Rappoport D, Yau PO, Snyder PW, Whitesides GM (2013). "The binding of benzoarylsulfonamide ligands to human carbonic anhydrase is insensitive to formal fluorination of the ligand". Angew. Chem. Int. Ed. Engl. 52 (30): 7714–7. doi:10.1002/anie.201301813. PMID 23788494. S2CID 1543705.
  7. ^ Breiten B, Lockett MR, Sherman W, Fujita S, Al-Sayah M, Lange H, Bowers CM, Heroux A, Krilov G, Whitesides GM (2013). "Water networks contribute to enthalpy/entropy compensation in protein-ligand binding". J. Am. Chem. Soc. 135 (41): 15579–84. CiteSeerX 10.1.1.646.8648. doi:10.1021/ja4075776. PMID 24044696. S2CID 17554787.
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