Protein

I

Introduction

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.

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.

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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. Nine essential amino acids are needed to maintain health in humans: leucine, isoleucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine, and histidine. 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.

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