Gibbs free energy hydrophobic association

Before electron transfer, as fluctuations toward dissociation occur with occupancy by the hydrophobic QH2 molecule, sufficient hydrophobic hydration would form to result in water insolubility such that reassociation results. If, on the other hand, fluctuations toward dissociation occur for QH occupancy, as hydrophobic hydration formed it would be recruited to align for hydration of the positively charged QHi. Thus, increased hydrophobic hydration that ensured hydrophobic reassociation would not occur and hydrophobic dissociation would be the result. Without the favorable decrease in Gibbs free energy for association, the deforming force that caused extension of the tether would be gone, and elastic retraction would result. Additional mechanical details of the resulting domain movement follow below. 

The hydrophobic effect can be measured in terms of transfer of a molecule from gaseous phase or dissolved in nonpolar solvent to water. Since the change in Gibbs free energy AG is associated with changes in ethalpy JH, and entropy JS according to... 

Table 2 Dependence of transition temperature and standard Gibbs free energy of hydrophobic association for elastin-mimetic protein polymers based on the pentapeptide sequences (Val-Pro-Gly-Xaa-Gly)...

T, to a new value of T, caused by an energy input represented by % to provide a measure of the change in Gibbs free energy for hydrophobic association of the protein-based polymer. Therefore, Tt, the onset temperature for the inverse temperature transition, represents an intrinsic property of the hydrophobic consilient mechanism of energy conversion. 

Different Estimates of Transition Temperature Used in Calculating the Gibbs Free Energy for Hydrophobic Association, AGha, by Equation (5.10a)... 

AG ha The Change in Gibbs Free Energy for Hydrophobic Association Due to Change in Amino Acid Composition With AG A(Gly) = 0... 

Figure 5.10. An embodiment of the comprehensive hydrophobic effect in terms of a plot of the temperature for the onset of phase separation for hydrophobic association, Tb, versus AGha. the Gibbs free energy of hydrophobic association for the amino acid residues, calculated by means of Equation (5.10b) using the heats of the phase (inverse temperature) transition (AH,). Values were taken from Table 5.3. Tb and T, were determined from the onset of the phase separation as defined in Figure 5.1C,B, respectively. The estimates of AGha utilized the AH, data listed in Table 5.1 for fx = 0.2 but extrapolated to fx = 1, and the Gly (G) residue was taken as the...

Table 5.3. Hydrophobicity Scale in terms of AGha, the change in Gibbs free energy for hydrophobic association, for amino acid residue (X) of chemically synthesized poly[fv(GVGVP), fx(GXGVP)], 40m ml, mw = 100 kDa in 0.15 N NaCl, 0.01 M phosphate, using the net heat of the inverse temperature transition, AGha = [AH,(GGGVP) - AH.(GXGVP)] for the fx = 0.2 data extrapolated to f = 1.

Coupling of Functional Groups by Means of the Consilient Mechanism and by Means of Their Common Dependence on the Gibbs Free Energy of Hydrophobic Association, AGha... 

The change in Gibbs free energy for hydrophobic association, AGha, affects and is affected by the forms of energy utilized by living organ-... 

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