Proteins polysaccharides polymers

Whereas conventional poly (amino acids) are probably best grouped together with proteins, polysaccharides, and other endogenous polymeric materials, the pseudopoly (amino acids) can no longer be regarded as "natural polymers." Rather, they are synthetic polymers derived from natural metabolites (e.g., a-L-amino acids) as monomers. In this sense, pseudopoly (amino acids) are similar to polylactic acid, which is also a synthetic polymer, derived exclusively from a natural metabolite. 

We generally describe the structure of both synthetic and natural polymers in terms of four levels of structure primary, secondary, tertiary, and quaternary. The primary structure describes the precise sequence of the individual atoms that compose the polymer chain. For polymers that have only an average structure, such as proteins, polysaccharides, and nucleic acids, a representative chain structure is often given. 

Dickinson, E. (1993). Protein-polysaccharide interactions. In Dickinson, E., Walstra, P. (Eds). Food Colloids and Polymers Stability and Mechanical Properties, Cambridge, UK Royal Society of Chemistry, pp. 77-93. 

Unlike proteins, polysaccharides generally do not have definite molecular weights. This difference is a consequence of the mechanisms of assembly of the two types of polymers. As we shall see in Chapter 27, proteins are synthesized on a template (messenger RNA) of defined sequence and length, by enzymes that follow the template exactly. For polysaccharide synthesis there is no template rather, the program for polysaccharide synthesis is intrinsic to the enzymes that catalyze the polymerization of the monomeric units, and there is no specific stopping point in the synthetic process. 

One of the main advantages of these soft ionisation techniques is that they lead to the formation of multiply charged, pseudomolecular ions (z can be greater than 30). Hence the mass range of the spectrometer can be extended to over 105 Da (to include proteins, polysaccharides and other polymers) (Fig. 16.20). These ionisation devices are often coupled to the mass spectrometer through a heated capillary transmitting the ions. 

In Section III, it was mentioned that cell wall is a complex structure formed by different polysaccharides connected to glycoproteins. Hydroxy-L-proline-rich glycoproteins, such as extensin, have been found in almost all plants surveyed, and in some algae.203,281 A network of protein, pectic polymers, and xyloglucan, serving to cross-link the cellulose fibers of the cell wall, has been proposed.282,283 However, covalent links between the different components have not been demonstrated moreover, some of them can be extracted separately,284 and some associations may be artificial.285 Nevertheless, results are consistent with interactions through dipole-dipole (such as hydrogen bonds) or hydrophobic bonds. 

The DOC/enzyme/microbe interaction (DEMI) model divides bacterioplankton into two functional guilds, opportunists and decomposers, and DOC into two pools, labile and recalcitrant. In the context of the model, labile DOC is defined as directly assimilable monomers (saccharides, amino acids, and organic acids) and readily hydrolyzed polymers (polysaccharides, proteins, and nucleic acids). Because these substrates turn over rapidly, thus are unlikely to be transported far, most of the carbon in this pool will be autochthonous lysates and exudates, or allochthonous leachates from storms or seasonal litter fall. Recalcitrant DOC is defined as humic substances created by oxidative reactions among proteins, polysaccharides, hydrocarbons, and phenolic molecules. For inland waters, recalcitrant DOC is largely of allochthonous origin. 

A large number of macromolecules possess a pronounced amphiphilicity in every repeat unit. Typical examples are synthetic polymers like poly(l-vinylimidazole), poly(JV-isopropylacrylamide), poly(2-ethyl acrylic acid), poly(styrene sulfonate), poly(4-vinylpyridine), methylcellulose, etc. Some of them are shown in Fig. 23. In each repeat unit of such polymers there are hydrophilic (polar) and hydrophobic (nonpolar) atomic groups, which have different affinity to water or other polar solvents. Also, many of the important biopolymers (proteins, polysaccharides, phospholipids) are typical amphiphiles. Moreover, among the synthetic polymers, polyamphiphiles are very close to biological macromolecules in nature and behavior. In principle, they may provide useful analogs of proteins and are important for modeling some fundamental properties and sophisticated functions of biopolymers such as protein folding and enzymatic activity. 

Dickinson, E., and Galazka, V. B. (1991). Bridging flocculation in emulsions made with a mixture of protein + polysaccharide. In Food Polymers, Gels and Colloids, Dickinson, E. (Ed.), pp. 494-497. Royal Chem. Soc., London. 

The repair and replication of cells involves metabolism - interconversions of hundreds of low molecular weight metabolites that ultimately yield the precursors for much larger, more complex macromolecules such as phospholipids (based on phosphatidic. acids or long chain fatty acid esters of glycerol phosphate), polynucleotides such as RNA and DNA (polymers of nucleotide monomers), proteins (polypeptides or amino acid monomers linked by peptide bonds) and polysaccharides (polymers of simple sugars or monosaccharides). 

Food polymers and the behaviour of their mixtures are mainly responsible for the structure-properties relationship in both food and chyme. The two basic features of food are that its biopolymers, proteins and polysaccharides are its main construction materials and water is the main medium, solvent and plasticizer. In other words, three components— protein, polysaccharide and water—are the main elements of food structure that are principally responsible for quality of foods (see also Chapter 13). 

More detailed discussion of food polymers and their functionality in food is now difficult because of the lack of the information available on thermodynamic properties of biopolymer mixtures. So far, the phase behaviour of many important model systems remains unstudied. This particularly relates to systems containing (i) more than two biopolymers, (ii) mixtures containing denatured proteins, (iii) partially hydrolyzed proteins, (iv) soluble electrostatic protein-polysaccharide complexes and conjugates, (v) enzymes (proteolytic and amylolytic) and their partition coefficient between the phases of protein-polysaccharide mixtures, (vi) phase behaviour of hydrolytic enzyme-exopolysaccharide mixtures, exopolysaccharide-cell wall polysaccharide mixtures and exopolysaccharide-exudative polysaccharide mixtures, (vii) biopolymer solutes in the gel networks of one or several of them, (viii) enzymes in the gel of their substrates, (ix) virus-exopolysaccharide, virus-mucopolysaccharides and virus-exudative gum mixtures, and so on. 

Polymer solutions figure in a vast array of practical materials and processes in the modern world. Ideas about polymers are also relevant to understanding solutions of DNA, proteins, polysaccharides, and other solutions of biological interest. Because of the size and complexity of the chain molecule solutes, polymer solutions present challenging problems in solution theory, and a great deal of work has been directed toward a theoretical understanding of these solutions over the last century. 

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