Entropy water

See also Hydrogen Bonds, Structure and Properties of Water, Entropy... 

Two important aspects of Uposome formation must be emphasized here. First, in some cases we observe the formation of ordered supramolecular structures starting from a chaotic disordered mixture of surfactants (as in the ethanol injection method . As noticed before, this increase of order is attended by a simultaneous increase of water entropy and a decrease of overall free energy (Upids and solvent). Secondly, every time a liposome forms, there is the anergence of a division, with an inside world that is different from the external environment, even if the two worlds actually interact with each other. The discrimination between inside and outside, appUcable to lipid vesicles, is the first structural pre-requisite for the living cell. It is therefore clear that lipid or fatty acid vesicles may be considered relevant experimental model of simplified cells, and their role on... 

Wood and DeLaney have measured the solubility of He, Ng, Ar, and ethane in pure A-methylacetamide from 35 to 70°C and used the data to calculate the free energy, heat and entropy of solution, as well as the change in heat capacity for the dissolution process. (See Appendix 2.3.2.) Non-polar solutes appear to be much more soluble in iV-methyl-acetamide than in water. Entropies of solution are not as negative as for aqueous solutions, but the change in heat capacity on dissolution is much more negative than in water. These results lead to some interesting conclusions as to the structural effects of non-polar solutes on this solvent. 

According to (D.5), we neglect also the pressure dependence of liquid water entropy. Then... 

The state of an adsorbate is often described as mobile or localized, usually in connection with adsorption models and analyses of adsorption entropies (see Section XVII-3C). A more direct criterion is, in analogy to that of the fluidity of a bulk phase, the degree of mobility as reflected by the surface diffusion coefficient. This may be estimated from the dielectric relaxation time Resing [115] gives values of the diffusion coefficient for adsorbed water ranging from near bulk liquids values (lO cm /sec) to as low as 10 cm /sec. 

Water-soluble globular proteins usually have an interior composed almost entirely of non polar, hydrophobic amino acids such as phenylalanine, tryptophan, valine and leucine witl polar and charged amino acids such as lysine and arginine located on the surface of thi molecule. This packing of hydrophobic residues is a consequence of the hydrophobic effeci which is the most important factor that contributes to protein stability. The molecula basis for the hydrophobic effect continues to be the subject of some debate but is general considered to be entropic in origin. Moreover, it is the entropy change of the solvent that i... 

The hydrophobic effect. Water molecules around a non-polar solute form a cage-like structure, which ices the entropy. When two non-polar groups associate, water molecules are liberated, increasing the entropy. 

Figure 5-11 Pitrtiiil MMII Output Shinvirig Entropy and Heat Capacities for Water. E. perimerital values are 4. i. IS eal K iiiol for the absolute entropy and H.OS eal K iiiol i or the heat eaitaeity.

Figure 1.4. Temperature dependence of the change in Gihhs energy, enthalpy and entropy upon transfer of ethane and butane from the gas phase to water. The data refer to transfer from the vapour phase at 0.101 MPa to a hypothetical solution of unit mole fraction and are taken from ref. 125.

As is suggested frequently , this term might well result from the restriction of the hydrogen bonding possibilities experienced by the water molecules in the first hydration shell. For each individual water molecule this is probably a relatively small effect, but due to the small size of the water molecules, a large number of them are entangled in the first hydration shell, so that the overall effect is appreciable. This theory is in perfect agreement with the observation that the entropy of hydration of a nonpolar molecule depends linearly on the number of water molecules in the first hydration shell ". ... 

What distinguishes water from ordinary organic solvents and justifies the term hydrophobic interaction is the molecular origin of the effect, being entropy driven in pure water at room temperature and resulting primarily from the strong water-water interactions. 

The theory predicts high stabilities for hard acid - hard base complexes, mainly resulting from electrostatic interactions and for soft acid - soft base complexes, where covalent bonding is also important Hard acid - soft base and hard base - soft acid complexes usually have low stability. Unfortunately, in a quantitative sense, the predictive value of the HSAB theory is limited. Thermodynamic analysis clearly shows a difference between hard-hard interactions and soft-soft interactions. In water hard-hard interactions are usually endothermic and occur only as a result of a gain in entropy, originating from a liberation of water molecules from the hydration shells of the... 

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. 

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