What Is Protein?
Protein is found throughout the body—in muscle, bone, skin, hair, and virtually every other body part or tissue. It makes up the enzymes that power many chemical reactions and the hemoglobin that carries oxygen in your blood. At least 10,000 different proteins make you what you are and keep you that way.
Proteins are made up of hundreds or thousands of smaller units called amino acids, which are attached to one another in long chains. There are 20 different types of amino acids that can be combined to make a protein. The sequence of amino acids determines each protein’s unique 3-dimensional structure and its specific function. Amino acids are coded by combinations of three DNA building blocks (nucleotides), determined by the sequence of genes.
Examples of protein functions
A protein molecule is very large compared with molecules of sugar or salt and consists of many amino acids joined together to form long chains, much as beads are arranged on a string. There are about 20 different amino acids that occur naturally in proteins. Proteins of similar function have similar amino acid composition and sequence. Although it is not yet possible to explain all of the functions of a protein from its amino acid sequence, established correlations between structure and function can be attributed to the properties of the amino acids that compose proteins.
The common property of all proteins is that they consist of long chains of α-amino (alpha amino) acids. The general structure of α-amino acids is shown in . The α-amino acids are so called because the α-carbon atom in the molecule carries an amino group (―NH2); the α-carbon atom also carries a carboxyl group (―COOH).
In acidic solutions, when the pH is less than 4, the ―COO groups combine with hydrogen ions (H+) and are thus converted into the uncharged form (―COOH). In alkaline solutions, at pH above 9, the ammonium groups (―NH+3) lose a hydrogen ion and are converted into amino groups (―NH2). In the pH range between 4 and 8, amino acids carry both a positive and a negative charge and therefore do not migrate in an electrical field. Such structures have been designated as dipolar ions, or zwitterions (i.e., hybrid ions).
Although more than 100 amino acids occur in nature, particularly in plants, only 20 types are commonly found in most proteins. In protein molecules the α-amino acids are linked to each other by peptide bonds between the amino group of one amino acid and the carboxyl group of its neighbour.
The condensation (joining) of three amino acids yields the tripeptide.
It is customary to write the structure of peptides in such a way that the free α-amino group (also called the N terminus of the peptide) is at the left side and the free carboxyl group (the C terminus) at the right side. Proteins are macromolecular polypeptides—i.e., very large molecules (macromolecules) composed of many peptide-bonded amino acids. Most of the common ones contain more than 100 amino acids linked to each other in a long peptide chain. The average molecular weight (based on the weight of a hydrogen atom as 1) of each amino acid is approximately 100 to 125; thus, the molecular weights of proteins are usually in the range of 10,000 to 100,000 daltons (one dalton is the weight of one hydrogen atom). The species-specificity and organ-specificity of proteins result from differences in the number and sequences of amino acids. Twenty different amino acids in a chain 100 amino acids long can be arranged in far more than 10100 ways (10100 is the number one followed by 100 zeroes).