CHEMISTRY GLOSSARY

cysteine    →   cistein

Cysteine is neutral amino acids with polar side chains. Because of its high reactivity, the thiol group of cysteine has numerous biological functions. It serves as a potent nucleophile and metal ligand (particularly for iron and zinc), but is best known for its ability to form disulfide bonds, which often make an important contribution to the stability of extracellular proteins. Cysteine is a non-essential amino acid, which means that it is biosynthesized in humans.

• Abbreviations: Cys, C
• IUPAC name: 2-amino-3-sulfanylpropanoic acid
• Molecular formula: C₃H₇NO₂S
• Molecular weight: 121.16 g/mol

deoxyribonucleic acid    →   dezoksiribonukleinska kiselina

Deoxyribonucleic acid (DNA) is a nucleic acid with 2-deoxy-D-ribose as the sugar in its nucleotides. DNA contains encoded genetic information, specifically templates for the synthesis of all of an organism’s proteins and enzymes.

DNA was first identified in the 1869 by Swiss chemist Friedrich Miescher (1844-1895). In 1953, American biologist James Dewey Watson (1928-) and English physicist Francis Harry Compton Crick (1916–2004) had discovered that DNA occurs in the cell as a double helix, with two long strands of the molecule wound around each other, and further that the chemical structure of the molecule dictates that adenine (A) always aligns or pairs with thymine (T), and cytosine (C) always pairs with guanine (G). It is this base pairing that allows DNA in a cell to copy itself, and transfer its information to a new cell. The diameter of the helix is 2.0 nm and there is a residue on each chain every 0.34 nm in the z direction. The angle between each residue on the same strand is 36°, so that the structure repeats after 10 residues (3.4 nm) on each strand.

glutamic acid    →   glutaminska kiselina

Glutamic acid is an electrically charged amino acids. It is one of the two amino acids that contain a carboxylic acid group in its side chains. These acids play important roles as general acids in enzyme active centers, as well as in maintaining the solubility and ionic character of proteins. Glutamic acid is commonly referred to as glutamate, because its carboxylic acid side chain will be deprotonated and thus negatively charged in its anionic form at physiological pH. Glutamic acid is referred to as a non-essential amino acid because a healthy human can synthesize all the glutamic acid needed for normal body function from other amino acids.

• Abbreviations: Glu, E
• IUPAC name: 2-aminopentanedioic acid
• Molecular formula: C₅H₉NO₄
• Molecular weight: 147.13 g/mol

glutamine    →   glutamin

Glutamine is neutral amino acids with polar side chains. It serves as an important carrier of ammonia and contributes it to the formation of urea and purines. Glutamine is not recognized as an essential amino acid but may become conditionally essential in certain situations, including intensive athletic training or certain gastrointestinal disorders. It is synthesized by the enzyme glutamine synthetase from glutamate and ammonia.

• Abbreviations: Gln, Q
• IUPAC name: 2,5-diamino-5-oxopentanoic acid
• Molecular formula: C₅H₁₀N₂O₃
• Molecular weight: 146.14 g/mol

glycine    →   glicin

Glycine is the smallest amino acid and is unique because it lacks a side chain. This gives it more conformational freedom than any other amino acid. Glycine is often found in turns and loops where other amino acids would be sterically unacceptable. Although it is formally nonpolar, it’s very small side chain makes no real contribution to hydrophobic interactions. Glycine is not essential to the human diet, as it is biosynthesized in the body from the amino acid serine.

• Abbreviations: Gly, G
• IUPAC name: 2-aminoacetic acid
• Molecular formula: C₂H₅NO₂
• Molecular weight: 75.07 g/mol

histidine    →   histidin

Histidine is an electrically charged amino acids with basic side chains. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested. Histidine is perhaps the most common and versatile catalytic residue in proteins. The imidazole sidechain of histidine has a pKa of approximately 6.0. This means that, at physiologically relevant pH values, relatively small shifts in pH will change its average charge. The unprotonated imidazole is nucleophilic and can serve as a general base, while the protonated form can serve as a general acid. In addition, it is often a ligand for transition metal ions such as iron and zinc.

• Abbreviations: His, H
• IUPAC name: 2-amino-3-(1H-imidazol-5-yl)propanoic acid
• Molecular formula: C₆H₉N₃O₂
• Molecular weight: 155.15 g/mol

isoelectric point    →   izoelektrična točka

Isoelectric point (pI or IEP) is the pH of a solution or dispersion at which the net charge on the molecules or colloidal particles is zero. In electrophoresis there is no motion of the particles in an electric field at the isoelectric point. The net charge (the algebraic sum of all the charged groups present) of any amino acid, peptide or protein, will depend upon the pH of the surrounding aqueous environment. For example, alanine can have a charge of +1, 0, or -1, depending on the pH of the solution in which it is dissolved.

isoleucine    →   izoleucin

Isoleucine is hydrophobic amino acids with aliphatic side chain. It is one of the three amino acids having branched hydrocarbon side chains. The side chains of these amino acids are not reactive but, these residues are critically important for ligand binding to proteins, and play central roles in protein stability. Isoleucine is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Ile, I
• IUPAC name: 2-amino-3-methylpentanoic acid
• Molecular formula: C₆H₁₃NO₂
• Molecular weight: 131.12 g/mol

leucine    →   leucin

Leucine is hydrophobic amino acids with aliphatic side chain. It has one additional methylene group in its side chain compared with valine. The nonpolar hydrophobic amino acids tend to cluster together within proteins, stabilizing protein structure by means of hydrophobic interactions. Leucine is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Leu, L
• IUPAC name: 2-amino-4-methylpentanoic acid
• Molecular formula: C₆H₁₃NO₂
• Molecular weight: 131.17 g/mol

lysine    →   lizin

Lysine is an electrically charged amino acids with basic side chains. Lysine is a base, as are arginine and histidine. The amino group is highly reactive and often participates in reactions at the active centers of enzymes. Lysine plays an important role in coordinating negatively charged ligands. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Lys, K
• IUPAC name: 2,6-diaminohexanoic acid
• Molecular formula: C₆H₁₄N₂O₂
• Molecular weight: 146.19 g/mol