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Groups on the hydrophobic

The examples of substituted piperidines and pyridines show that ctbi depends on position and polarity of the substituents (Table XXI). Apolar groups seem to make the best fit with the receptor at position 3 or 4, while the negative influence of polar groups on the hydrophobic contact seems to be minimal at position 2. [Pg.117]

The fundamental property of a surface active agent, as mentioned before, is that it contains both polar and nonpolar moieties in its structure. This property is termed amphiphilicity or amphipathicity, and the substances that possess it are called amphiphiles. An amphiphile can be anionic or cationic, depending on whether its hydrophobic moiety is an anion or a cation. A zwitterion is an ion that possesses both anionic and cationic groups on the hydrophobic moiety and can behave either as an anionic, cationic or neutral species. An example of an ionic type is sodium dodecyl sulfate a cationic dodecyltrimethylammonium bromide a zwitterionic A-dodecyl-3-aminopropionic acid and a nonionic N, AT-dimethyldodecylamine oxide. [Pg.827]

Heating Kemp s acid with appropriate aromatic diamines yields bis-imides with two convergently oriented carboxylic acid groups on the edges of a hydrophobic pocket. Dozens of interesting molecular complexes have been obtained from such compounds and can be traced in the Journal of the American Chemical Society under the authorship of J. Rebek, Jr., (1985 and later e.g. T. Tjivikua, 1990 B). [Pg.347]

Protein tertiary structure is also influenced by the environment In water a globu lar protein usually adopts a shape that places its hydrophobic groups toward the interior with Its polar groups on the surface where they are solvated by water molecules About 65% of the mass of most cells is water and the proteins present m cells are said to be m their native state—the tertiary structure m which they express their biological activ ity When the tertiary structure of a protein is disrupted by adding substances that cause the protein chain to unfold the protein becomes denatured and loses most if not all of Its activity Evidence that supports the view that the tertiary structure is dictated by the primary structure includes experiments m which proteins are denatured and allowed to stand whereupon they are observed to spontaneously readopt their native state confer matron with full recovery of biological activity... [Pg.1146]

FIG. 1 Self-assembled structures in amphiphilic systems micellar structures (a) and (b) exist in aqueous solution as well as in ternary oil/water/amphiphile mixtures. In the latter case, they are swollen by the oil on the hydrophobic (tail) side. Monolayers (c) separate water from oil domains in ternary systems. Lipids in water tend to form bilayers (d) rather than micelles, since their hydrophobic block (two chains) is so compact and bulky, compared to the head group, that they cannot easily pack into a sphere [4]. At small concentrations, bilayers often close up to form vesicles (e). Some surfactants also form cyhndrical (wormlike) micelles (not shown). [Pg.632]

Alkanesulfonates are the petrochemically derived sulfur analogs of soaps, which are alkane carboxylates based on renewable resources. The main difference between alkanesulfonates and soaps is, however, that alkanesulfonates consist of a rather complex mixture of homologs with different carbon chain lengths and isomers with an almost statistical distribution of the functional group along the hydrophobic carbon chain (Fig. 1), whereas soap is a mixture of homologs of alkane 1-carboxylates with an even number of carbon atoms. [Pg.144]

Comparison of entries 4 and 8 of Table 16 shows that linear IOS 2024 and AOS 2024 adsorption values were the same within a modest experimental error. The major chemical structure difference between them is the position of the sulfonate group on the carbon chain and perhaps the position of the carbon-carbon double bond. These two factors do not appear to have an appreciable effect on adsorption. Therefore, the lower adsorption of IOS 1518 relative to AOS 1618 is probably due to the greater hydrophobe branching of the internal olefin sulfonate or the lower di.monosulfonate ratio. [Pg.399]

Figure 7. Mechanism of the proton-translocating ubiquinol cytochrome c reductase (complex III) Q cycle. There is a potential difference of up to 150 mV across the hydrophobic core of this complex (potential barrier represented by the vertical broken line). Cytochromes hour and b N are heme groups on the same peptide subunits of complex III which can transfer electrons across the hydrophobic core. The movement of two electrons provides the driving force to transfer two protons from the matrix to the cytosol. Diffusion of UQ and UQHj, which are uncharged, in the hydrophobic core, and lipid bilayer of the inner membrane is not influenced by the membrane potential (see Nicholls and Ferguson, 1992). Figure 7. Mechanism of the proton-translocating ubiquinol cytochrome c reductase (complex III) Q cycle. There is a potential difference of up to 150 mV across the hydrophobic core of this complex (potential barrier represented by the vertical broken line). Cytochromes hour and b N are heme groups on the same peptide subunits of complex III which can transfer electrons across the hydrophobic core. The movement of two electrons provides the driving force to transfer two protons from the matrix to the cytosol. Diffusion of UQ and UQHj, which are uncharged, in the hydrophobic core, and lipid bilayer of the inner membrane is not influenced by the membrane potential (see Nicholls and Ferguson, 1992).
Traditional amphiphiles contain a hydrophilic head group and the hydrophobic hydrocarbon chain(s). The molecules are spread at molecular areas greater (-2-10 times) than that to which they will be compressed. The record of surface pressure (II) versus molecular area (A) at constant temperature as the barrier is moved forward to compress the monolayer is known as an isotherm, which is analogous to P-V isotherms for bulk substances. H-A isotherm data provide information on the molecular packing, the monolayer stability as de-... [Pg.61]

The water structure at the water/surfactant interface depends on the nature of the surfactant head group, whereas the hydrophobic interface plays only a secondary role [91-93],... [Pg.482]

The peripheral substitution with hydrophobic chains on one hemisphere and hydrophilic groups on the other provides the perfect hydrophobic/hydrophilic balance allowing the formation of stable Langmuir films. In addition, a perfect reversibility has been observed in successive compression/decompression cycles (Fig. 18). [Pg.104]

Water-soluble polymeric dyes have been prepared from water-insoluble chromophores, viz., anthraquinone derivatives. Unreacted chromophore and its simple derivatives, which are all water-insoluble, remain in solution due to solubilization by the polymeric dye. A method has been developed to separate and quantitate the polymeric dye and these hydrophobic impurities using Sephadex column packing. The solvent developed has the property of debinding the impiirities from the polymer, and further allows a separation of the imp irities into discrete species. This latter separation is based on the functional groups on the impurity molecules, having a different interaction with the Sephadex surface in the presence of this solvent. The polymer elutes at the void volume... [Pg.301]

Figure 6 WIN52084 bound to HRV-14. The methyl group on the oxazoline ring is pointing toward a hydrophobic pocket formed by Leu106 and Ser107. Figure 6 WIN52084 bound to HRV-14. The methyl group on the oxazoline ring is pointing toward a hydrophobic pocket formed by Leu106 and Ser107.

See other pages where Groups on the hydrophobic is mentioned: [Pg.398]    [Pg.14]    [Pg.110]    [Pg.159]    [Pg.3]    [Pg.131]    [Pg.398]    [Pg.14]    [Pg.110]    [Pg.159]    [Pg.3]    [Pg.131]    [Pg.351]    [Pg.27]    [Pg.256]    [Pg.347]    [Pg.96]    [Pg.130]    [Pg.205]    [Pg.260]    [Pg.279]    [Pg.56]    [Pg.215]    [Pg.19]    [Pg.14]    [Pg.158]    [Pg.1197]    [Pg.891]    [Pg.246]    [Pg.68]    [Pg.894]    [Pg.118]    [Pg.37]    [Pg.153]    [Pg.374]    [Pg.6]    [Pg.288]    [Pg.105]    [Pg.75]    [Pg.335]    [Pg.334]    [Pg.244]   


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Hydrophobic groups

The Hydrophobic Group

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