Ionic interactions, intramolecular

Anionic polymerization Initiated by electron transfer (e.g., sodium-naphthalene and styrene In THF) usually produces two-ended living polymers. Such species belong to a class of compounds called bolaform electrolytes (27) In which two Ions or Ion pairs are linked together by a chain of atoms. Depending on chain length, counterion end solvent, Intramolecular Ionic Interactions can occur which in turn may affect the dissociation of the ion pairs Into free ions or the llgand-lon pair complex formation constants. 

When dealing with the water solubility of ionized molecules, one also must consider the possibility of intramolecular ionic interactions. Compounds with ionizable functional groups that produce opposite charges have the potential to interact with each other rather than with water molecules. When this occurs, such compounds often become very insoluble in water. A classic example is the amino acid tyrosine (Fig. 2.11). Tyrosine contains three very polar functional groups, with two of these groups (the alkylamine and carboxylic acid) capable of being ionized, depending on the pH of the solution. The phenolic hydroxyl also is ionizable (pKg 9-10), but it... 

Instead, the conformational characteristics are explained by the stringent requirement of the ionic interaction between the carboxylate/imidazolium ion pair coupled with the attempt of the former group to maintain as many H-bonds as possible (e.g. four H-bonds, cf. Ref. 75c). Such an attempt is obviously supported by the intramolecular H-bond in 1 Im 2 H20. The geometry of the corresponding moieties indicates the presence of strongly interacting ionic species (Fig. 42). 

In organic reactions, ionic interactions may serve as intermolecular or intramolecular forces. In some cases, these may involve metal cations, such as Na% or anions, such as Cl. Cations may include an ammonium ion from an amino group, such as RNH3. The anion may be from a carboxylic acid, such as RCOO. The oppositely charged ions attract each other very strongly. 

These interactions are frequently ionic in character. The coulombic forces of interaction between macroions and lower molecular weight ionic species are central to the life processes of the cell. For example, intermolecular interactions of nucleic acids with proteins and small ions, of proteins with anionic lipids and surfactants and with the ionic substrates of enzyme catalyzed reactions, and of ionic polysaccharides with a variety of inorganic cations are all improtant natural processes. Intramolecular coulombic interactions are also important for determining the shape and stability of biopolymer structures, the biological function of which frequently depends intimately on the conformational features of the molecule. 

More recently, in addition to random ionomers, telechelic ionomers in which ionic groups are located only at the chain end(s) became available and were used for the study of polyelectrolyte behavior [26-29]. Discussion was made from the point of view that the behavior of telechelic ionomers in nonaqueous solutions is basically similar to that of polyelectrolytes in aqueous/nonaqueous solutions (including random ionomers in nonaqueous solutions). Also, the study of fundamental aspects of polyelectrolytes was made possible because of the simplicity of the structure of telechelic ionomers. For example, telechelic ionomers with only one ionic group at the chain end can be used to study the role of intermolecular interactions, since there is no intramolecular electrostatic interaction available for this type of ionomer [27]. Due to space limitations, this chapter will only cover polyelectrolyte behavior of random ionomers in polar solvents. Some results on telechelic ionomers can be found elsewhere [26-29]. 

Elevated pressures can induce functional and structural alterations of proteins. The effects of pressure are governed by Le Chatelier s principle. According to this principle, an increase in pressure favours processes which reduce the overall volume of the system, and conversely increases in pressure inhibit processes which increase the volume. The effects of pressure on proteins depend on the relative contribution of the intramolecular forces which determine their stability and functions. Ionic interactions and hydrophobic interactions are disrupted by pressure. On the other hand, stacking interactions between aromatic rings and charge-transfer interactions are reinforced by pressure. Hydrogen bonds are almost insensitive to pressure. Thus, pressure acts on the secondary, tertiary, and quaternary structure of proteins. The extent and the reversibility, or irreversibility, of pressure effects depend on the pressure range, the rate of compression, and the duration of exposure to increased pressures. These effects are also influenced by other environmental parameters, such as the temperature, the pH, the solvent, and the composition of the medium. 

Figure 2. Conceptual representation of intramolecular entropically driven hydrophobic associations (A) and enthalpic ionic interactions (B) in solution.

Secondary structure in water-soluble polymers is related to configuration, conformation, and intramolecular effects such as hydrogen bonding and ionic interactions. Tertiary structure involves intermolecular and water-polymer interactions quaternary structure requires multiple chain aggregation or complexation. 

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