Protein, any of a large number of organic compounds that make up living organisms and are essential to their functioning. First discovered in 1838, proteins are now recognized as the predominant ingredients of cells, making up more than 50 percent of the dry weight of animals. The word protein is coined from the Greek proteios, or “primary.”
Protein molecules range from the long, insoluble fibers that make up connective tissue and hair to the compact, soluble globules that can pass through cell membranes and set off metabolic reactions. They are all large molecules, ranging in molecular weight from a few thousand to more than a million, and they are specific for each species and for each organ of each species. Humans have an estimated 30,000 different proteins, of which only about 2 percent have been adequately described. Proteins in the diet serve primarily to build and maintain cells, but their chemical breakdown also provides energy, yielding close to the same 4 calories per gram as do carbohydrates (see Metabolism).
Besides their function in growth and cell maintenance, proteins are also responsible for muscle contraction. The digestive enzymes are proteins, as are insulin and most other hormones. The antibodies of the immune system are proteins, and proteins such as hemoglobin carry vital substances throughout the body.
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 (see Nutrition, Human).
|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.
The major fibrous proteins, described below, are collagen, keratin, fibrinogen, and muscle proteins.
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.
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.
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.
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.
Unlike fibrous proteins, globular proteins are spherical and highly soluble. They play a dynamic role in body metabolism. Examples are albumin, globulin, casein, hemoglobin, all of the enzymes, and protein hormones. The albumins and globulins are classes of soluble proteins abundant in animal cells, blood serum, milk, and eggs. Hemoglobin is a respiratory protein that carries oxygen throughout the body and is responsible for the bright red color of red blood cells. More than 100 different human hemoglobins have been discovered, among which is hemoglobin S, the cause of sickle-cell anemia, a hereditary disease suffered mainly by blacks.
All of the enzymes are globular proteins that combine rapidly with other substances, called substrate, to catalyze the numerous chemical reactions in the body. Chiefly responsible for metabolism and its regulation, these molecules have catalytic sites on which substrate fits in a lock-and-key manner to trigger and control metabolism throughout the body.
These proteins, which come from the endocrine glands, do not act as enzymes. Instead they stimulate target organs that in turn initiate and control important activities—for example, the rate of metabolism and the production of digestive enzymes and milk. Insulin, secreted by the islands of Langerhans, regulates carbohydrate metabolism by controlling blood glucose levels. Thyroglobulin, from the thyroid gland, regulates overall metabolism; calcitonin, also from the thyroid, lowers blood calcium levels. Angiogenin, a protein structurally determined in the mid-1980s, directly induces the growth of blood vessels in tissues.
Also called immunoglobulins, antibodies (see Antibody) make up the thousands of different proteins that are generated in the blood serum in reaction to antigens (body-invading substances or organisms). A single antigen may elicit the production of many antibodies, which combine with different sites on the antigen molecule, neutralize it, and cause it to precipitate from the blood.
Globular proteins can also assemble into minute, hollow tubes that serve both to structure cells and to conduct substances from one part of a cell to another. Each of these microtubules, as they are called, is made up of two types of nearly spherical protein molecules that pair and join onto the growing end of the microtubule, adding on length as required. Microtubules also make up the inner structure of cilia, the hairlike appendages by which some microorganisms propel themselves.
Mary Lynn Hendrix