Collagen polypeptide chains

The results showed that while none of the books stored in the clean Welsh environment had deteriorated to any significant extent, nearly all the volumes subjected to London s acidic pollution exhibited evidence of decay, some within less than 10 years. In addition, the superior ageing properties of leathers prepared with hydrolysable tannins were confirmed. Of the various chemical analytical determinations undertaken, the only results to show any correlation with the degree of deterioration observed were those for the number of -terminal amino acid groups on the protein. This figure reflects the amount by which the collagen polypeptide chain had been broken and was considered to be evidence for hydrolytic deterioration. 

The cross-linkages found in collagen and elastin arise from the non-enzymatic interaction of a-amino adipic acid 8-semialdehyde (AL) and 8-hydroxy a-amino adipic acid 8-semialdehyde (HAL) with another residue of the aldehyde or with lysine, hydroxylysine, or histidine residues located at specific positions in the collagen polypeptide chains. Possible relationships among the different compounds in Table II are shown in Figures 4 and 5 for collagen and elastin. 

An individual collagen polypeptide chain has a large number of repeating amino acid sequences, most often glycine-X-Y, where X is often proline and Y is often hydroxyproline. Lysine, in its pure form or modified to hydroxylysine, is also found in collagen. Both hydroxyproline and hydrox-ylysine are formed via the enzyme-catalyzed oxidations of the profine and lysine amino acid side chains, which occur after the collagen polypeptide has been synthesized. These enzymatic reactions reqtiire ascorbic acid (vitamin C) as a cofactor. 

The hydroxylation of proline in nascent collagen polypeptide chains does not require ... 

The collagens are the most abundant proteins found in various connective tissues of all multicellular animals. A typical collagen molecule has a long, flexible, and triple-stranded helical structure, in which three collagen polypeptide chains, so-called a-chains, are coiled in a rope-like helix. Among the 15 types of mature collagen molecules composed of different a-chains, the primary types are I, II, IV, and IX. 

Collagen chains are synthesized as longer precursors, called procollagens, with globular extensions—propeptides of about 200 residues—at both ends. These procollagen polypeptide chains are transported into the lumen of the rough endoplasmic reticulum where they undergo hydroxylation and other chemical modifications before they are assembled into triple chain molecules. The terminal propeptides are essential for proper formation of triple... 

Figure 14.1 Each polypeptide chain in the collagen molecule folds into an extended polyproline type II helix with a rise per turn along the helix of 9.6 A comprising 3.3 residues. In the collagen molecule three such chains are supercoiled about a common axis to form a 3000-A-long rod-like molecule. The amino acid sequence contains repeats of -Gly-X-Y- where X is often proline and Y is often hydroxyproline. (a) Ball and stick model of two turns of one polypeptide chain.

Figure 14.2 Models of a collagen-like peptide with a mutation Gly to Ala in the middle of the peptide (orange). Each polypeptide chain is folded into a polyproline type II helix and three chains form a superhelix similar to part of the collagen molecule. The alanine side chain is accommodated inside the superhelix causing a slight change in the twist of the individual chains, (a) Space-filling model, (b) Ribbon diagram. Compare with Figure 14.1c for the change caused by the alanine substitution. (Adapted from J. Bella et al.. Science 266 75-81, 1994.)...

Collagen, the principal fibrous protein in mammalian tissue, has a tertiary structure made up of twisted a-helices. Three polypeptide chains, each of which is a left-handed helix, are twisted into a right-handed super helix to form an extremely strong tertiary structure. It has remarkable tensile strength, which makes it important in the structure of bones, tendons, teeth, and cartilage. 

Collagen triple helices are stabilized by hydrogen bonds between residues in dijferent polypeptide chains. The hydroxyl groups of hydroxyprolyl residues also participate in interchain hydrogen bonding. Additional stability is provided by covalent cross-links formed between modified lysyl residues both within and between polypeptide chains. 

Collagen, the major component of most connective tissues, constimtes approximately 25% of the protein of mammals. It provides an extracellular framework for all metazoan animals and exists in virmally every animal tissue. At least 19 distinct types of collagen made up of 30 distinct polypeptide chains (each encoded by a separate gene) have been identified in human tissues. Although several of these are present only in small proportions, they may play important roles in determining the physical properties of specific tissues. In addition, a number of proteins (eg, the Clq component of the complement system, pulmonary surfactant proteins SP-A and SP-D) that are not classified as collagens have... 

Proteins, the main constituents of the animals body, are polypeptides, biopolymers consisting of many amino acid molecules (the monomers) combined together (see Chapter 11) collagen, for example, the main component of animal skin, is a complex protein consisting of many molecules of amino acids combined together into polypeptide chains (see Fig. 71). Polysaccharides, the essential constituents of plants, also consist of many monosaccharide molecules combined together. Cellulose, the most abundant biological material on earth, which makes up most of the structural... 

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