Amino acid collagen

The major organic component in hone is collagen, which constitutes some 90 to 96% of the dry fat-free organic matter Collagen is a long fibrous protein, two-thirds of which is formed of only four amino acids Collagen is about 33% glycine, 11% alanine, and 22% proline and hydroxyproline (13) ... 

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.

Fibrous proteins are long-chain polymers that are used as structural materials. Most contain specific repetitive amino acid sequences and fall into one of three groups coiled-coil a helices as in keratin and myosin triple helices as in collagen and p sheets as in silk and amyloid fibrils. 

Collagen Collagen is an extracellular structural protein 1052 amino acid residues. Collagen has an minsnal amino acid composidon it is about one-third glycine and is rich in proline. Note diat it also lacks Cys and Trp and is deficient in aromadc amino acid residues in general. 

The amino acid sequence of the collagen type I (bone, skin, tendon) is nearly completely known6. The sequence of the different tripeptides in the archain shows a more or less statistic distribution. The content of the tripeptides in the archain of type I collagen, however, is quite different (Table 1). 

The part of non-imino acid-containing tripeptides amounts to nearly 50%. It is astonishing that at some places in the collagen chain, containing 1044 amino acid units, such sequences are accumulated, forming imino add-free ranges of remarkable length. 

Table 2 shows a list of collagen model peptides which have teen prepared. Many efforts have been made to prevent racemization. The polycondensation reaction seemed to be more sensitive to racemization than the coupling steps preparing the monomeric tripeptide. Therefore, the sequence of the monomer was selected with Gly or Pro at the C-terminal chain end, because racemization is mostly favored at the carboxy-activated amino acid, and these amino acids cannot racemize. 

The amino acids proline and hydroxyproline exert a stabilizing influence on the triple helix as described in detail in Sect. 4.5. By examining the CB peptides of collagen, a structural stability which is directly proportional to the itnino acid content may thus be found. It has, however, not been possible to synthesize model peptides displaying structural stability comparable to that of the native peptides having corresponding amino acid contents. 

It is known that native collagen contains tripeptide sequences which, because of being homopolypeptides, are not able to give rise to triple-helical tertiary structures (e.g. Gly-Pro-Leu, Gly-Pro-Ser). The reason for this and for the above-mentioned low thermostability of the synthetic homopolypeptides is presumably to be found in the fact that in the case of the model peptides with their monotonously repeated tripeptide sequences, special interactions between the side chains of the different amino acid residues as postulated by Ward and Mason are no more possible157). 

Model peptides that could build up quarternary fibrillar structures are not yet known. Though complete explanation of the interdependence between the primary structure and the stability of the quarternary structure has not yet been possible, i.e. the role of the different amino acids in collagen could be understood completely only in correlation with the fibril formation (formation of polar and hydrophobic clusters ). 

Collagen forms a triple helix, where three chains of connected amino acids form weak hydrogen bonds between the double-bonded oxygen atoms and the hydrogen atoms attached to the adjacent chain s nitrogens. The three chains then twist together like three cords in a rope. 

The fifteen samples analyzed for amino acid composition were compared to a human type 1 collagen standard. There are no significant differences in amino acid composition among these samples, which range in age from stillbirth to adult. Analytical error is 10%. All samples show the typical composition of type 1 collagen (Table 1.1). Based on these results there is no reason to suspect differential preservation of specific amino acids in the small bones of infants in comparison to bones of adults and older children. 

Tabic 1.1. Amino acids per thousand residues for standard type 1 collagen and 15 human bone collagen samples from St. Thomas Church cemetery. Samples are identified by burial numlter (Bx) followed by age midpoint for subadults and age range for adults in parentheses. For example, B17(0) refers to burial 17 who was aged as a newborn. 

Van Klinken, GJ. 1991 Dating and Dietary Reconstruction by Isotopic Analysis of Amino Acids in Fossil Bone Collagen—with Special Reference to the Caribbean. Ph.D. dissertation. University of Groningen, The Netherlands. 

In comparison with values from the literature, the majority of the amino acid values for our collagen standard (3 replicates) are within acceptable... 

Figure 7.4. Amino acid profiles for seven aliquots from collagen of Burial 8.

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