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Downloaded from Digital Engineering Library @ McGraw-Hill (www.digitalengineeringlibrary.com) Copyright 2004 The McGraw-Hill Companies. All rights reserved. Any use is subject to the Terms of Use as given at the website.
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Both an increase in enthalpy (needed to break some of the water-water hydrogen bonds) and a decrease in entropy (the restricted movement of water molecules at the surface of the hydrophobic molecule) contribute to an increase in the Gibbs energy. Thus mixing of water and hydrophobic substances is energetically unfavorable. This energetic cost can be minimized by minimizing contact between the water and the hydrophobic molecules. In the case of oil and water mixed together, the oil droplets begin to coalesce into larger drops, eventually separating into two phases. The result is a decrease in the Gibbs energy by minimizing contact between the oil and water. So the process of oil and water separating is spontaneous, that is, energetically favored. The hydrophobic molecules that concern us in biological systems are mostly hydrocarbons, molecules made up of only hydrogen and carbon. Hydrocarbons are found abundantly in living systems. Fats and oils are mostly hydrocarbons. Many biomolecules are not purely hydrophobic, but have a portion of the molecule that is hydrophobic and a portion of the molecule that is hydrophilic. Hydrophilic means that the molecule interacts favorably with water (lowers the Gibbs energy). Typically a hydrophilic molecule (or the hydrophilic part of a molecule) is highly polar, and easily forms hydrogen bonds with water. Molecules that are both hydrophobic and hydrophilic are called amphipathic or amphiphilic. These mean the same thing. (You may occasionally see the incorrect word amphiphatic which is a common mistake made by incorrectly combining amphipathic and amphiphilic.) Phospholipids, which make up the membranes of cells, are amphipathic. Phospholipids have a highly polar (negatively charged) phosphate head that is covalently bonded to a long, hydrophobic hydrocarbon tail. See Fig. 6-15. Many protein molecules also have parts that are hydrophobic and other parts that are hydrophilic.
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