Hydrophobic association energy

Hydrophobic association energy, mineral surfaces. In turn, the proportion of hydrophilic and hydrophobic groups in the flotation reagents is relevant in the determination of 0 value. 

CH2), showing that the hydrophobic association energy of alkylamines when adsorbed on mineral surfaces is about 2.3 kJ/mol(-CH2-). 

In asi-casein, it is arguable that because the hydrophobic interaction surfaces are well separated from Ca2+ ion-binding sites, the electrostatic and hydrophobic free energies of association can be treated as separate and additive, leading to the Z2 dependence of the rate of aggregation under many circumstances. Likewise, the nearly bifunctional nature of the aggregation reaction is consistent with the formation of linear polymers, as observed in the absence of Ca2+ (Thurn etal., 1987b), and may involve the apposition of hydrophobic surfaces formed from the N- and C-terminal peptides. 

This approximate law holds for both native structure [22] and folding dynamics [2], In this regard, this wrapping motif may be regarded as a structural element that captures the basic component of energy transduction from hydrophobic association to structure formation. Furthermore, it implies that a fundamental constraint in protein architecture applicable to native structures applies also throughout the folding trajectory. 

The total association energy, AG, can be considered to be the sum of free energies for hydrophobic and hydrophilic groups, AGn and AGp. 

The hydrophobic free energy associated with the transfer of the hydrocarbon tail from water to the hydrocarbon mixture in the micellar core. This contribution can be obtained from available solubility data. 

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)...

The energy dissipated during the reversible cycles ((/hys) can be interpreted as the sum of the dissociation energies of hydrophobic associations broken down reversibly during the cyclic tests [98, 99] ... 

In Chapter 8, more structural background and molecular details of contraction exhibited by the linear myosin II motor are considered after, in Chapter 5, the physical basis for the apolar (oil-like)-polar (vinegar-like) repulsive energy that controls hydrophobic association is experimentally and analytically developed. The crystal structures of the cross-bridge of scallop muscle provide remarkable examples of the consilient mechanism functioning in this protein-based machine ... 

Due to the struggle to survive under circumstances of limited food supply, organisms evolve to use the most efficient mechanism available to their composition. The most efficient mechanism available to the proteins that sustain Life would seem to be the apolar-polar repulsive free energy of hydration as observed for the inverse temperature transitions for hydrophobic association. The efficiency of designed elastic-contractile protein-based machines and a number of additional properties make designed protein-based materials of substantial promise for the marketplace of the future. 

---