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External Websites
- Healthline - Essential Amino Acids: Definition, Benefits, and Food Sources
- National Library of Medicine - Biochemistry, Essential Amino Acids
- Biology LibreTexts - Structure & Function - Amino Acids
- Cleveland Clinic - Amino Acid
- WebMD - Foods High in Amino Acids
- Purdue University - Chemical Education Division Groups - Amino Acids
- Khan Academy - Amino acid structure
- Mustansiriyah University - Amino Acid: Structure and Classification
- Nature Education - Scitable - Amino Acids, Evolution
- Open Oregon Educational Resources - Structure and Function – Amino Acids
- Roger Williams University Open Publishing - Introduction to Molecular and Cell Biology - Amino Acids and Proteins
Britannica Websites
Articles from Britannica Encyclopedias for elementary and high school students.
- amino acid - Student Encyclopedia (Ages 11 and up)
Written by
Michael K. Reddy
Fact-checked by
The Editors of Encyclopaedia Britannica
Last Updated: •Article History
- Key People:
- James P. Allison
- Carl Sagan
- Dorothy Maud Wrinch
- Charles Yanofsky
- Related Topics:
- creatine
- glutamic acid
- tryptophan
- alanine
- tyrosine
See all related content
Amino acids via their various chemical functionalities (carboxyls, amino, and R groups) can undergo numerous chemical reactions. However, two reactions (peptide bond and cysteine oxidation) are of particular importance because of their effect on protein structure.
Peptide bond
Amino acids can be linked by a condensation reaction in which an ―OH is lost from the carboxyl group of one amino acid along with a hydrogen from the amino group of a second, forming a molecule of water and leaving the two amino acids linked via an amide—called, in this case, a peptide bond. At the turn of the 20th century, German chemist Emil Fischer first proposed this linking together of amino acids. Note that when individual amino acids are combined to form proteins, their carboxyl and amino groups are no longer able to act as acids or bases, since they have reacted to form the peptide bond. Therefore, the acid-base properties of proteins are dependent upon the overall ionization characteristics of the individual R groups of the component amino acids.
Amino acids joined by a series of peptide bonds are said to constitute a peptide. After they are incorporated into a peptide, the individual amino acids are referred to as amino acid residues. Small polymers of amino acids (fewer than 50) are called oligopeptides, while larger ones (more than 50) are referred to as polypeptides. Hence, a protein molecule is a polypeptide chain composed of many amino acid residues, with each residue joined to the next by a peptide bond. The lengths for different proteins range from a few dozen to thousands of amino acids, and each protein contains different relative proportions of the 20 standard amino acids.
Cysteine oxidation
The thiol (sulfur-containing) group of cysteine is highly reactive. The most common reaction of this group is a reversible oxidation that forms a disulfide. Oxidation of two molecules of cysteine forms cystine, a molecule that contains a disulfide bond. When two cysteine residues in a protein form such a bond, it is referred to as a disulfide bridge. Disulfide bridges are a common mechanism used in nature to stabilize many proteins. Such disulfide bridges are often found among extracellular proteins that are secreted from cells. In eukaryotic organisms, formation of disulfide bridges occurs within the organelle called the endoplasmic reticulum.
In extracellular fluids (such as blood), the sulfhydryl groups of cysteine are rapidly oxidized to form cystine. In a genetic disorder known as cystinuria, there is a defect that results in excessive excretion of cystine into the urine. Because cystine is the least soluble of the amino acids, crystallization of the excreted cystine results in formation of calculi—more commonly known as “stones”—in the kidney, ureter, or urinary bladder. The stones may cause intense pain, infection, and blood in the urine. Medical intervention often involves the administration of d-penicillamine. Penicillamine works by forming a complex with cystine; this complex is 50 times more water-soluble than cystine alone.
In summary, it is the sequence of amino acids that determines the shape and biological function of a protein as well as its physical and chemical properties. Thus, the functional diversity of proteins arises because proteins are polymers of 20 different kinds of amino acids. For example, a “simple” protein is the hormone insulin, which has 51 amino acids. With 20 different amino acids to chose from at each of these 51 positions, a total of 2051, or about 1066, different proteins could theoretically be made.
Other functions
Amino acids are precursors of a variety of complex nitrogen-containing molecules. Prominent among these are the nitrogenous base components of nucleotides and the nucleic acids (DNA and RNA). Furthermore, there are complex amino-acid derived cofactors such as heme and chlorophyll. Heme is the iron-containing organic group required for the biological activity of vitally important proteins such as the oxygen-carrying hemoglobin and the electron-transporting cytochrome c. Chlorophyll is a pigment required for photosynthesis.
Several α-amino acids (or their derivatives) act as chemical messengers. For example, γ-aminobutyric acid (gamma-aminobutyric acid, or GABA; a derivative of glutamic acid), serotonin and melatonin (derivatives of tryptophan), and histamine (synthesized from histidine) are neurotransmitters. Thyroxine (a tyrosine derivative produced in the thyroid gland of animals) and indole acetic acid (a tryptophan derivative found in plants) are two examples of hormones.
Several standard and nonstandard amino acids often are vital metabolic intermediates. Important examples of this are the amino acids arginine, citrulline, and ornithine, which are all components of the urea cycle. The synthesis of urea is the principal mechanism for the removal of nitrogenous waste.