Fibrous proteins collagens and

The main constituents are the mineral hydroxyapatite, the fibrous protein collagen, and water. There is some non-collagenous organic material. 

The pleural tissue is a typical connective tissue that consists mostly of matrix the fibrous proteins (collagen, elastin), and mucopolysaccharides, and a few scattered mesothelial cells, capillaries, venules, and ducts. Anatomists have defined several layers (Fig. 3.4) for each of the pleura. Layers 3 and 5 in Fig. 3.4 contain an abundance of fibrous protein, especially elastin. Both the interstitial (Layer 4) and mesothelial (1 and 2) layers contain capillaries of the vascular system and lymphatic channels. The matrix (ground substance) gives the pleura structural integrity and is responsible for its mechanical properties such as elasticity and distensibility. 

Gelatin is derived from the fibrous protein collagen, which is the principal constituent of animal skin, bone, and connective tissue. Fish skin waste could be used as a potential source to isolate collagen and gelatin. Zhu et al. (2010) evaluated the effect of collagen peptides on markers of metabolic nuclear receptors. 

Natural polymers polysaccharides (celullose, starch, pectins, dextrans, agar, agarose, alginate, chitine, chitosan, etc.) and fibrous proteins (collagen, keratine, etc.). 

In Nature, there are many examples of protein and peptide molecular self-assembly. Of the genetically engineered fibrous proteins, collagen, spider silks, and elastin have received attention due to their mechanical and biological properties which can be used for biomaterials and tissue engineering. 

The fibrous protein collagen, the major constituent of skin and bone, is derived from procollagen, a soluble precursor. 

The use of chemiluminescence technique has expanded to others natural polymers. Recently, Millington et al. reported studies on polymers such as the fibrous proteins wool and feather keratin, silk fibroin, and reconstituted collagen from bovine skin, which revealed new information about their degradation [81]. The potential of CL to analyze the effectiveness of treatments to protect the polymer during processing could contribute to diminish the loss of properties of the types of polymers widely used in textile industry. 

Basically, there are three major groups of proteins in muscle tissue (a) the sarcoplasmic proteins of the muscle cell cytoplasm, (b) the myofibrillar proteins, soluble at high ionic strengths, that make up the myofibril or contractile part of the muscle, and (c) the stromal proteins comprised largely of the connective tissue proteins, collagen, and elastin. The myofibrillar proteins and the stromal proteins are fibrous and elongated they form viscous solutions with large shear resistance. These properties coupled with other lines of indirect evidence indicate that the physical properties of the myofibrillar and stromal proteins are directly related to the texture and tenderness of meat (34). 

Most structural proteins have a fibrous structure. Collagen and elastin are such fibrous structures and are important components of cormective tissues such as cartilage, and keratin that forms hair, nails, hooves, arri-mal shells, etc. Structural proteins can also generate mechanical forces for cellular mobility and muscle contraction. Examples are myosin and kinesin, two globular proteins (Figure 3.3) that are crucial for cellular... 

Fibrous proteins can serve as structural materials for the same reason that other polymers do they are long-chain molecules. By cross-linking, interleaving and intertwining the proper combination of individual long-chain molecules, bulk properties are obtained that can serve many different functions. Fibrous proteins are usually divided in three different groups dependent on the secondary structure of the individual molecules coiled-coil a helices present in keratin and myosin, the triple helix in collagen, and P sheets in amyloid fibers and silks. 

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 is a rigid, inextensible fibrous protein that is a principal constituent of connective tissue in animals, including tendons, cartilage, bones, teeth, skin, and blood vessels. The high tensile strength of collagen fibers in these struc-... 

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. 

Mithieux SM, Weiss AS (2005) Elastin. In Parry DAD, Squire JM (eds) Fibrous proteins coiied-coiis, collagen and elastomers. Advances in protein chemistry, vol 70. Elsevier Academic, San Diego, pp 437-461... 

Collagen is the most abundant animal protein in the body of animals, where it makes up as much as one-quarter of all the proteins. It is a fibrous protein that provides structure to and protects and supports soft tissues it also connects tissues to the skeleton. Collagen forms, for example, most of the resilient layers that make up the skin and the filaments that support the internal organs. Interwoven with bioinorganic components, collagen also makes up the bones and teeth of vertebrate animals (see Chapter 15). 

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