AGha estimated values

Gross estimates of AGha using the T,-values in the right column in combination with the T, versus AGha values from Figure 5.10. 

When estimating the value of AGha, as derived in section 5.1.3.4 and defined in Equation... 

For the following estimates, Tb values are available for guest amino acid residues without functional groups. With Equation (5.10b), the calculated values for the residues more hydrophobic than glycine (Gly, G), that is, AGha(GGGVP —> GXGVP) substitutions, in... 

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...

The notation (from graph) indicates that the value of T, from Table 5.1 was used with the sigmoid curve of Figure 5.10 to estimate AGha(x)-Source Adapted from Urry. ... 

Figure 7.48. Stereo view of the aqueous chamber side of the GroES cap at the GroEL-GroES junction for the asymmetric (ADP)7-GroEL structure. The purpose is to estimate surface polarity by obtaining a sum over AGha for the face and to compare the value to the inner faces of GroEL as...

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. 

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