Hydrophobic dissociation within

Expectation 2 That the ADP plus Pi state at the cross-bridge active site effects a repulsive AGap force for dissociation of hydrophobic domains within the cross-bridge. Relevance of the hydrophobic consilient mechanism to the motion of contraction requires that formation of the most polar state, ADP " Mg + HPO/", effects hydrophobic dissociation within the cross-bridge. This sets the stage for the loss of Pi, that is, of HPO/", that drives the hydrophobic association required by the hydrophobic consilient mechanism as... 

Another crucial factor characterizing PM is their kinetic stability. The kinetic stability of micelles refers to the actual rate of micelle dissociation below the CMC. Thus, even below the CMC, PM may still be kinetically stable, provided that the dissociation into unimers proceeds slowly. Systems for which dissociation takes place over hours or even days have been reported, as opposed to low molecular weight surfactants that dissociate within milliseconds below their CMC. Several properties of the copolymer can be modified to improve the kinetic stability. These include the hydrophobic/hydrophilic balance, the physical state of the micelle core, the size of the hydrophobic block, and the incorporation of hydrophobic compounds (Figure 4.4). For instance, Creutz et showed that the rate of disassembly could be slowed down by increasing the hydrophobic/hydrophilic balance of the core-forming block. Increases in the hydrophobicity... 

The primary effect of micelles on light-induced electron transfer involves the intervention of an interfacial region which can significantly influence the radical ion association and dissociation equilibria by a combination of electrostatic and hydro-phobic interactions. Diffusive encounters of reaction partners are controlled within a micelle by the diffusion of one reactant to the highly polar surface, by collision of two reactants confined within the hydrophobic region in the interior of the micelle, and by the reaction of two reactants whose motions are confined to diffusion along the micellar surface. 

Despite the size of the protein subunits, their integrity does not depend on cross-linking via disulfide bonds (63) and no disulfide bridges have been identified within the partially completed amino acid sequence (41, 6Sa). Nor is there any evidence that association of subunits depends on covalent bonding rather, it appears to involve mainly hydrophobic interactions (50). Of particular interest in this context is the observation that some forms of acatalasemia are attributable to the formation of a catalase variant, of approximately normal specific activity, but with a tendency to dissociate into subunits (64). 

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