Hydrophobic Molecules Do Not Fear Water

When two people do not like each other they are said to mix about as well as oil and water. One of the most familiar classifications in chemistry is one that differentiates hydrophilic ( water-loving ) molecules (and parts of molecules) from hydrophobic ( water-fearing ) molecules (and parts of molecules). The structures of Langmuir monolayer micelles, described in chapter 2, and cell membrane bilayers are often said to result from hydrophobic bonding of long hydrophobic hydrocarbon chains. 

In 1959, Walter J. Kauzmann (1916- ) at Princeton clarified the notions of hydrophobic bonding when he noted that water is actually attracted to hydrophobic molecules with a very small amount of heat released upon association. This is the result of nonbonding (van der Waals) attraction and in some cases (e.g., benzene) some 

The ordered structures of proteins (alpha-helices, beta-sheexs) readily explain the fact that all protein molecules (on Earth at least) are comprised of L-a-amino acids (since an occasional D-amino add would disrupt the ordered structure of L-enantiomers). The configurations of L-amino acids are described by the structure below they are consistent with carbohydrate nomenclature as seen by comparison with the D-glyceraldehyde structure shown earlier in this chapter. In both classes. 

Three-dimensional and Fischer prelection of L-amino acids 

Three-point attachment schematic of enzyme binding of substrates 

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