Muscle proteins, fibrous

Fibrous proteins provide the structural material of many tissues in the body. They are the chief constituents of hair, cartilage, and muscles. Fibrous proteins consist of lengthwise bundles of polypeptide chains (a fiber). Globular proteins consist of polypeptide chains folded into a spherical shape they are found in the bloodstream where they transport and store various substances, act as antibodies (fight infections), act as enzymes (catalysts), and participate in the body s various regulatory systems. 

Proteins can be broadly classified into fibrous and globular. Many fibrous proteins serve a stmctural role (11). CC-Keratin has been described. Fibroin, the primary protein in silk, has -sheets packed one on top of another. CoUagen, found in connective tissue, has a triple-hehcal stmcture. Other fibrous proteins have a motile function. Skeletal muscle fibers are made up of thick filaments consisting of the protein myosin, and thin filaments consisting of actin, troponin, and tropomyosin. Muscle contraction is achieved when these filaments sHde past each other. Microtubules and flagellin are proteins responsible for the motion of ciUa and bacterial dageUa. 

Alpha helices are sufficiently versatile to produce many very different classes of structures. In membrane-bound proteins, the regions inside the membranes are frequently a helices whose surfaces are covered by hydrophobic side chains suitable for the hydrophobic environment inside the membranes. Membrane-bound proteins are described in Chapter 12. Alpha helices are also frequently used to produce structural and motile proteins with various different properties and functions. These can be typical fibrous proteins such as keratin, which is present in skin, hair, and feathers, or parts of the cellular machinery such as fibrinogen or the muscle proteins myosin and dystrophin. These a-helical proteins will be discussed in Chapter 14. 

The natural polymers known as proteins make up about 15% by mass of our bodies. They serve many functions. Fibrous proteins are the main components of hair, muscle, and skin. Other proteins found in body fluids transport oxygen, fats, and other substances needed for metabolism. Still others, such as insulin and vasopressin, are hormones. Enzymes, which catalyze reactions in the body, are chiefly protein. 

The major types of cytoskeletal filaments are 7-nm-thick microfilaments. 25-nm-thick microtubules, and 10-nm-thick intermediate filaments (IPs). These are respectively composed of actin, tubulin, and a variety of interrelated sparsely soluble fibrous proteins termed intermediate filament proteins. In addition, thick myosin filaments are present in large numbers in skeletal and heart muscle cells and in small numbers in many other types of eukaryotic cells. 

In addition to the 20 common amino acids, proteins may contain residues created by modification of common residues already incorporated into a polypeptide (Fig. 3-8a). Among these uncommon amino acids are 4-hydroxyproline, a derivative of proline, and 5-hydroxylysine, derived from lysine. The former is found in plant cell wall proteins, and both are found in collagen, a fibrous protein of connective tissues. 6-N-Methyllysine is a constituent of myosin, a contractile protein of muscle. Another important uncommon amino acid is y-carboxyglutamate, found in the bloodclotting protein prothrombin and in certain other proteins that bind Ca2+ as part of their biological function. More complex is desmosine, a derivative of four Lys residues, which is found in the fibrous protein elastin. 

The alpha helix represents the second major structural element of soluble proteins108 128 and is also found in many fibrous proteins, including those of muscle... 

In many cases there are important interactions between protein molecules that may lead to highly organized structures such as the pleated sheet of silk fibroin (Figure 25-13) or the coiling of a helices, as found in a-keratins, the fibrous proteins of hair, horn, and muscles (Figure 25-17). This sort of organization of protein molecules is called quaternary structure and is an important feature of many proteins that associate into dimers, tetramers, and so on. The tetrameric structure of hemoglobin is an important example. 

Fibrous proteins - these have linear molecules, are insoluble in water and resistant to alkalis and acids. Collagen (in tendons and muscles), keratin (in nails, hair, horn and feathers) and elastin (in arteries) are all fibrous proteins. 

Fibrous proteins represent a substantial subset of the human proteome. They include the filamentous structures found in animal hair that act as a protective and thermoregulatory outer material. They are responsible for specifying much of an animal s skeleton, and connective tissues such as tendon, skin, bone, cornea and cartilage all play an important role in this regard. Fibrous proteins are frequently crucial in locomotion and are epitomised by the muscle proteins myosin and tropomyosin and by elastic structures like titin. Yet again the fibrous proteins include filamentous assemblies, such as actin filaments and microtubules, where these provide supporting structures and tracks for the action of a variety of molecular motors. 

Conversely, the connective tissues and cartilage are much more resistant to proteolysis and will survive for a longer period of time, although they too will eventually succumb to the effects of putrefaction. Reticulin, epidermis, and muscle protein will resist breakdown for some time, whereas collagen and keratin may survive for longer periods (Linch and Prahlow 2001). Keratin is an insoluble fibrous protein found in the skin, hair, and nails, and its resistance to attack by most proteolytic enzymes (Gupta and Ramnani 2006) is the reason it is often found intact amongst skeletal remains, particularly in burial environments (Macko et al. 1999). 

Many of the familiar cells in your body use fibrous proteins to carry out important tasks. Skin, bones, muscles, tendons, and hair cells all rely on molecules in this class. 

Scleroproteins. Insoluble in water and neutral solvents and resistant to enzymic hydrolysis. These are fibrous proteins serving structural and binding purposes. Collagen of muscle tissue is included in this group, as is gelatin, which is derived from it. Other examples include elastin, a component of tendons, and keratin, a component of hair and hoofs. 

Proteins are needed in the body for amino acids. Proteins are broken down in the digestive system to form amino acids which are then absorbed by the rest of the body to form new proteins in the form of vital body tissues such as muscle, connective tissue, and skin. There are two types of protein, fibrous and globular proteins. Fibrous protein is insoluble and goes into making the structural tissues of the body. Globular protein forms amino acids that become enzymes and hormones and other vital parts of cellular functioning within the body. 

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