Nonpolar solute

Kang T J, Yu J and Berg M 1990 Rapid solvation of a nonpolar solute measured by ultrafast transient hole burning Chem. Phys. Lett. 174 476-80... 

Hydrophobic effects include two distinct processes hydrophobic hydration and hydrophobic interaction. Hydrophobic hydration denotes the way in which nonpolar solutes affect the organisation of the water molecules in their immediate vicinity. The hydrophobic interaction describes the tendency of nonpolar molecules or parts thereof to stick together in aqueous media " . A related frequently encountered term is hydrophobicity . This term is essentially not correct since overall attractive interactions exist between water and compounds commonly referred to as... 

The solvation thermodynamics have been interpreted in a classical study by Frank and Evans in terms of the iceberg model . This model states that the water molecules around an nonpolar solute show an increased quasi-solid structuring. This pattern would account for the strongly negative... 

In the traditional view hydrophobic interactions are assumed to be driven by the release of water molecules from the hydrophobic hydration shells upon the approach of one nonpolar solute to another. Although the ideas about the structure of the hydrophobic hydration shell have changed, this view is essentially unaltered... 

The distinction between pairwise and bulk hydrophobic interactions is often made, although some authors doubt the existence of an intrinsic difference between the two ". Pairwise hydrophobic interactions denote the interactions behveen two isolated nonpolar solutes in aqueous solution. They occur in the regime where no aggregation takes place, hence below the critical aggregation concentration or solubility limit of the particular solute. If any breakdown of the hydrophobic hydration shell occurs, it will be only transient. 

If one would ask a chemist not burdened with any knowledge about the peculiar thermodynamics that characterise hydrophobic hydration, what would happen upon transfer of a nonpolar molecule from the gas phase to water, he or she would probably predict that this process is entropy driven and enthalpically highly unfavourable. This opinion, he or she wo ild support with the suggestion that in order to create room for the nonpolar solute in the aqueous solution, hydrogen bonds between water molecules would have to be sacrificed. 

Finally, also size and shape of the nonpolar solute seem to influence the formation of hydrophobic hydration shells. Particularly the curvature of the nonpolar surface has been suggested to be... 

Equation 22 is a special appHcation of the general Lewis-RandaH ideal solution model (3,10) that is typically used for near-ambient pressures and concentrated nonpolar solutes. 

Modem understanding of the hydrophobic effect attributes it primarily to a decrease in the number of hydrogen bonds that can be achieved by the water molecules when they are near a nonpolar surface. This view is confirmed by computer simulations of nonpolar solutes in water [15]. To a first approximation, the magnimde of the free energy associated with the nonpolar contribution can thus be considered to be proportional to the number of solvent molecules in the first solvation shell. This idea leads to a convenient and attractive approximation that is used extensively in biophysical applications [9,16-18]. It consists in assuming that the nonpolar free energy contribution is directly related to the SASA [9],... 

Hydrophobicity ( water-hate ) can dominate the behavior of nonpolar solutes in water. The key observations are (1) that very nonpolar solutes (such as saturated hydrocarbons) are nearly insoluble in water and (2) that nonpolar solutes in water tend to form molecular aggregates. Some authors refer to item 1 as the hydrophobic effect and to item 2 as the hydrophobic interaction. Two extreme points of view have been taken to account for these observations. 

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. 

When 1.32 g of a nonpolar solute was dissolved in 50.0 g of phenol, the latter s freezing point was lowered by 1.454°C. Calculate the molar mass of the solute. 

The same system is run using a nonpolar solute. The WS parameters are changed to reflect this attribute of the solute using T b(WS) = 0.8 and J(WS) = 0.25. Record the number of S cells out of five layers from the wall. Repeat using the other combinations of solute and wall states as shown in Table 6.5. 

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