Hydrophobic associations schematic representation

Fig. 9. Schematic representation of hydrophobic association diagonal lines—water assembly stippling—van der Waals interaction cross-hatched lines—water assembly destroyed by the guest association.

Figure 11.4 Schematic representation of drug association with polymeric micelles by hydrophobic interaction. (1 - a water-insoluble hydrophobic drug 2 - a drug of intermediate hydrophobicity 3 - a hydrophilic drug).

Figure 14 Proposed interaction of kalata B1 with dodecylphosphocholine membranes. 23 A schematic representation of DPC micelles is shown with a surface representation of kalata Bl. The hydrophobic face of the cyclotide associates with the surface of the micelle.

Figure 3.1 Schematic representations of a) a water molecule orientation near a nonpolar CHs-group, which is optimal if none of the hydrogen atoms or electron pairs is directed toward the nonpolar group ( = 0) b) contour line diagrams of three polar molecules with the first inner line of a solvation energy o/O kcal/mol, the second line of 1 kcal, the third line of 2 kcal/mol e/c and c) of the hydrophobic effect. Upon association of hydrophobic particles water or other solvent molecules are released. Entropy grows.

Figure 10. Schematic representation of hydrophobic associations in aqueous...

Fig. 2. Schematic representation of the retention dependencies for peptides or proteins chromatographed on mixed-mode support media. The figure illustrates four case histories for the dependency of the logarithmic capacity factor (log it ) on the mole fraction, f, of the displacing species. As the contact area associated with the solute-Ugand interaction increases, the slopes of the log k versus f plots increase resulting in a narrowing of the elution window over which the solute will desorb. Cases (a) and (b) are typically observed for the RP-HPLC of polar peptides and small, polar globular proteins whilst cases (c) and (d) are more representative of the RP-HPLC behaviour of highly hydrophobic polypeptides and non-polar globular proteins, respectively.

Schematic Representation of an Equilibrium Between Hydrophobically Associated and Dissociated Tlims of a P-Spiral Held at Fixed Extension...

The amphiphilic character of surfactant molecules is due to the association of two parts with very differing polarities inside the same molecule [2]. One part is highly nonpolar, hydrophobic or lipophilic, usually an alkyl chain. Another part of the surfactant molecule is polar or hydrophilic. It can be a nonionic chain with polar groups, such as ether, alcohol or amine groups, or an ionic (anionic or cationic) group. Figure 2.1 shows the schematic representation of a surfectant molecule. Some surfactants have two nonpolar tails or two polar heads, as illustrated in the figure. The nature of the surfactant polar head is used to classify the molecules. 

Figure 4. CPK molecular model of APC(C2Lys2C24)4, showing the most efficient hydrophobic association of its eight hydrophobic chains in aqueous media, (a) and its schematic representation (b).

Figure 2. A schematic representation of the interactions with the THOM2 potential. THOM2 assigns scores according to two contact shells. As an example we show a sample of contacts to a site and the associated energies for vahne and lysine. As expected, the hydrophobic residue (vaUne) strongly prefers to be at a site with a large number of neighbors in the first and second shells. Lysine is the extreme case on the polar side.

Schematic representation of an HASE associative polymer and the molecular constitution of the HASE polymer used in this study. R refers to the C22H45 hydrophobe, p = 40, and xjylz = 43.6/56.2/0.20 by mole. 

Structure of parallel stripes with respect to the long liber axis with a spacing 3 nm (comparable to the diameter of the thinner fibrils observed in samples with a concentration below 0.25 mM). The 3 nm fibrils correspond quite well to the diameter of a discotic molecule of the gelator and most likely result from the single stacks of the molecules of 9c hydrogen bonded in the z-direction. These thinner fibrils subsequently associate into parallel bundles resulting in 9 nm fibers stabilized by hydrophobic interaction between the aliphatic chains (a schematic representation of the self-assembly is shown in Fig. 6.11). 

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