CHEMISTRY GLOSSARY

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.

vitamin    →   vitamin

The name vitamin is obtained from vital amines as it was originally thought that these substances were all amines. This is now known not to be true as vitamins have a range of structures. The body requires a small amout of vitamins, but any deficiency leads to metabolic and physical disorders.

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

methionine    →   metionin

Methionine is neutral amino acids with polar side chains. It is one of the two sulfur-containing amino acids. Methionine is a fairly hydrophobic amino acid and typically found buried within the interior of a protein. It can form stacking interactions with the aromatic moieties of tryptophan, phenylalanine, and tyrosine. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Met, M
• IUPAC name: 2-amino-4-methylsulfanylbutanoic acid
• Molecular formula: C₅H₁₁NO₂S
• Molecular weight: 149.21 g/mol

oxo compound    →   okso-spoj

Oxo compounds are organic compounds that contain the karbonyl group, C=O. The term thus embraces aldehydes, carboxylic acids, ketones, amides, and esters.

peptide    →   peptid

Peptides are amides derived from two or more amino acids (the same or different) linked by peptide bonds. These bonds are formed by the reaction between adjacent carboxyl (-COOH) and amino (-NH₂) groups with the elimination of water.

peptide bond    →   peptidna veza

Peptide bond emerges when two amino acid join in a way that the carbon atom from one connects with the nitrogen atom from the other (creating a C-N bond).