Bonding hydrophobic

This is a very difficult term to define. To biologists, it simply relates to the tendency of non-polar groups in biomolecules to stay together. This is, of course, a total effect for lipids in water, but for proteins, which comprise a polar backbone with side groups that are often non-polar, there are regions in the tertiary structures in which non-polar units are in close contact. This situation is caused, in a negative way, by water which cannot solvate these regions, and in a positive way by attractive Van der Waals forces. 

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Other factors that can stabili2e such a forming complex are hydrophobic bonding by a variety of mechanisms (Van der Waals, Debye, ion-dipole, charge-transfer, etc). Such forces complement the stronger hydrogen-bonding and electrostatic interactions. 

Hydrophobic Interaction. This is the tendency of hydrophobic groups, especially alkyl chains such as those present in synthetic fibers, and disperse dyes to associate together and escape from the aqueous environment. Hydrophobic bonding is considered (7) to be a combination of van der Waals forces and hydrogen bonding taking place simultaneously rather than being a completely new type of bond or intermolecular force. 

Hydrophobic bonds, or, more accurately, interactions, form because nonpolar side chains of amino acids and other nonpolar solutes prefer to cluster in a nonpolar environment rather than to intercalate in a polar solvent such as water. The forming of hydrophobic bonds minimizes the interaction of nonpolar residues with water and is therefore highly favorable. Such clustering is entropically driven. The side chains of the amino acids in the interior or core of the protein structure are almost exclusively hydrophobic. Polar amino acids are almost never found in the interior of a protein, but the protein surface may consist of both polar and nonpolar residues. 

The reverse-phase technique is used less, however, with the advent of hydrophobic bonded phases (Section 8.2(3)). 

Menashi et al.153) could confirm the results of Privalov and Tiktopulo152 and inter-prete the described effects as follows In the case of native tropocollagen, the pyrrolidine residues are probably directed away from the fibrillar axis and are mostly coated by water which is structured in the immediate neighbourhood to the pyrrolidine residues. During the denaturation these pyrrolidine residues form hydrophobic bonds with each other or with other apolar residues within the same chain (endothermic interaction) while the structure of water breaks down (increase of entropy). 

Hydrophobic interaction refers to the tendency of nonpolar compounds to self-associate in an aqueous environment. This self-association is driven neither by mutual attraction nor by what are sometimes incorrectly referred to as hydrophobic bonds. Self-association arises from the need to minimize energetically unfavorable interactions between nonpolar groups and water. 

Deutsch and Hansch applied this principle to the sweet taste of the 2-substituted 5-nitroanilines. Using the data available (see Table VII), the calculated regression Eqs. 5-7 (using the method of least squares) optimally expressed the relationship between relative sweetness (RS), the Hammett constant, cr, and the hydrophobic-bonding constant, ir. 

Hermann, R. B. (1971) Theory of hydrophobic bonding. II. The correlation of hydrocarbon solubility in water with solvent cavity surface area. J. Phys. Chem. 76, 2754—2758. 

Hansch C., Anderson, S. (1967) The effect of intramolecular hydrophobic bonding on partition coefficients. J. Org. Chem. 32, 2583-2586. 

Many other types of solid phase adsorbents, including those based on conventional and specialty materials like restricted access media (RAM), can increase analysis speed and improve assay performance. These types of materials, also known as internal reversed-phase packings, are especially useful for assaying target compounds in biological samples such as serum and plasma. They are chemically modified porous silicas that have hydrophilic external surfaces and restricted-access hydrophobic internal surfaces. The ratio of interior to external surface areas is large. Macromolecules such as proteins cannot enter the pores of the RAM (they are excluded from the hydrophobic internal surface) and they elute quickly through the column. However, the smaller analyte molecules that can enter the pores are retained via interactions with the hydrophobic bonded phase within... 

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