This is an article I found in my files ,It is taken from med text, hope the info helps !
II. Nutrition
Whether found in humans or in single-celled bacteria, proteins are composed of units of about 20 different amino acids, which, in turn, are composed of carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur. In a protein molecule these acids form peptide bonds—bonds between amino and carboxyl (COOH) groups—in long strands (polypeptide chains). The almost numberless combinations in which the acids line up, and the helical and globular shapes into which the strands coil, help to explain the great diversity of tasks that proteins perform in living matter.
To synthesize its life-essential proteins, each species needs given proportions of the 20 main amino acids. Although plants can manufacture all their amino acids from nitrogen, carbon dioxide, and other chemicals through photosynthesis, most other organisms can manufacture only some of them. The remaining ones, called essential amino acids, must be derived from food. Eight essential amino acids are needed to maintain health in humans: leucine, isoleucine, lysine, methionine, phenylalanine, theonine, tryptophan, and valine. All of these are available in proteins produced in the seeds of plants, but because plant sources are often weak in lysine and tryptophan, nutrition experts advise supplementing the diet with animal protein from meat, eggs, and milk, which contain all the essential acids.
Most diets—especially in the United States, where animal protein is eaten to excess—contain all the essential amino acids. (Kwashiorkor, a wasting disease among children in tropical Africa, is due to an amino acid deficiency.) For adults, the Recommended Dietary Allowance (RDA) for protein is 0.79 g per kg (0.36 g per lb) of body weight each day. For children and infants this RDA is doubled and tripled, respectively, because of their rapid growth
III. Structure of Proteins
The most basic level of protein structure, called the primary structure, is the linear sequence of amino acids. Different sequences of the acids along a chain, however, affect the structure of a protein molecule in different ways. Forces such as hydrogen bonds, disulfide bridges, attractions between positive and negative charges, and hydrophobic ("water-fearing") and hydrophilic ("water-loving") linkages cause a protein molecule to coil or fold into a secondary structure, examples of which are the so-called alpha helix and the beta pleated sheet. When forces cause the molecule to become even more compact, as in globular proteins, a tertiary protein structure is formed. When a protein is made up of more than one polypeptide chain, as in hemoglobin and some enzymes, it is said to have a quaternary structure.
IV. Interaction with Other Proteins
Polypeptide chains are sequenced and coiled in such a way that the hydrophobic amino acids usually face inward, giving the molecule stability, and the hydrophilic amino acids face outward, where they are free to interact with other compounds and especially other proteins. Globular proteins, in particular, can join with a specific compound such as a vitamin derivative and form a coenzyme (see Enzyme), or join with a specific protein and form an assembly of proteins needed for cell chemistry or structure.
V. Fibrous Proteins
The major fibrous proteins, described below, are collagen, keratin, fibrinogen, and muscle proteins.
A. Collagen
Collagen, which makes up bone, skin, tendons, and cartilage, is the most abundant protein found in vertebrates. The molecule usually contains three very long polypeptide chains, each with about 1000 amino acids, that twist into a regularly repeating triple helix and give tendons and skin their great tensile strength. When long collagen fibrils are denatured by boiling, their chains are shortened to form gelatin.
B. Keratin
Keratin, which makes up the outermost layer of skin and the hair, scales, hooves, nails, and feathers of animals, twists into a regularly repeating coil called an alpha helix. Serving to protect the body against the environment, keratin is completely insoluble in water. Its many disulfide bonds make it an extremely stable protein, able to resist the action of proteolytic (protein-hydrolyzing) enzymes. In beauty treatments, human hair is set under a reducing agent, such as thioglycol, to reduce the number of disulfide bonds, which are then restored when the hair is exposed to oxygen.
C. Fibrinogen
Fibrinogen is a blood plasma protein responsible for blood clotting. With the catalytic action of thrombin, fibrinogen is converted into molecules of the insoluble protein fibrin, which link together to form clots.
D. Muscle Proteins
Myosin, the protein chiefly responsible for muscle contraction, combines with actin, another muscle protein, forming actomyosin, the different filaments of which shorten, causing the contracting action.
PART 1
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