AGha consilient mechanism

Energy Resources of the Consilient Mechanism Changing the Free Energy (AGha) for Hydrophobic Association... 

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... 

Summary Hexagon of Energy Conversions by the Consilient Mechanism of AGha... 

Coherence Between AG p and AGha Calculated Using Different Experimental Data Demonstrates Presence and Dominance of the Consilient Mechanism in Model Proteins... 

Demonstrations of these predictions constitute the message of this section 8.4, and its success introduces the perspective of a conjoined hydrophobic elastic consilient mechanism. With the values in Table 5.3 and the crystal structure with three different states of occupancy, empty, ATP, and ADP, the three sides of the rotor can be identified and the respective Gibbs free energies of hydrophobic association, AGha, have been estimated to be -20, 0, and +9kcal/mole. The most hydrophobic face associates with the empty site, the neutral face with the ATP bound site, and the most polar face with the ADP site which in the synthesis mode would be in position to add Pj. As expected from the magnitude of the resulting AG,p for a series of crystal structures wherein the least polar occupancy state for the catalytic site could be defined, the most hydrophobic side of the rotor resides in apposition to the least polar site. 

As required for the hydrophobic consilient mechanism to be operative for an ATP synthase/Fi-ATPase protein-based machine, the three faces of the y-rotor exhibit very different hydrophobicities, that is, different AGha values, namely, approximately -20,0, and +9kcal/mole. 

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