CHEMISTRY GLOSSARY

ribonucleic acid    →   ribonukleinska kiselina

Ribonucleic acid is a complex organic compound in living cells that is concerned with protein synthesis. Plays an intermediary role in converting the information contained in DNA into proteins. RNA carries the genetic information from DNA to those parts of the cell where proteins are made. Some viruses store their genetic information as RNA not as DNA.

Ribonucleic acid is a similar molecule to DNA but with a slightly different structure.

The structural difference with DNA is that RNA contains a -OH group both at the 2' and 3' position of the ribose ring, whereas DNA (which stands, in fact, for deoxy-RNA) lacks such a hydroxy group at the 2' position of the ribose. The same bases can be attached to the ribose group in RNA as occur in DNA, with the exception that in RNA thymine does not occur, and is replaced by uracil, which has an H-group instead of a methyl group at the C-5 position of the pyrimidine. Unlike the double-stranded DNA molecule, RNA is a single-stranded molecule.

The three main functionally distinct varieties of RNA molecules are: (1) messenger RNA (mRNA) which is involved in the transmission of DNA information, (2) ribosomal RNa (rRNA) which makes up the physical machinery of the synthetic process, and (3) transfer RNA (tRNA) which also constitutes another functional part of the machinery of protein synthesis.

toxin    →   toksin

Toxins are effective and specific poisons produced by living organisms. They usually consist of an amino acid chain which can vary in molecular weight between a couple of hundred (peptides) and one hundred thousand (proteins). They may also be low-molecular organic compounds. Toxins are produced by numerous organisms, e.g., bacteria, fungi, algae and plants. Many of them are extremely poisonous, with a toxicity that is several orders of magnitude greater than the nerve agents. Botulinum toxin, produced by the bacteria Clostridium botulinum, is the most poisonous substance known.

tryptophan    →   triptofan

Tryptophan is hydrophobic amino acids with aromatic side chain. Tryptophan is large aromatic residue that is normally found buried in the interior of a protein and is important for protein stability. Tryptophan has the largest side chain and is the least common amino acid in proteins. It has spectral properties that make it the best inherent probe for following protein folding and conformational changes associated with biochemical processes. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Trp, W
• IUPAC name: 2-amino-3-(1H-indol-3-yl)propanoic acid
• Molecular formula: C₁₁H₁₂N₂O₂
• Molecular weight: 204.23 g/mol

tyrosine    →   tirozin

Tyrosine is hydrophobic amino acids with aromatic side chain. Tyrosine is large aromatic residue that is normally found buried in the interior of a protein and is important for protein stability. Tyrosine has special properties since its hydroxyl side chain may function as a powerful nucleophile in an enzyme active site (when ionized) and is a common site for phosphorylation in cell signaling cascades. Tyrosine absorbs ultraviolet radiation and contributes to the absorbance spectra of proteins. It is not essential (or semi-essential) to the human diet, since it is synthesized in the body from other metabolites.

• Abbreviations: Tyr, Y
• IUPAC name: 2-amino-3-(4-hydroxyphenyl)propanoic acid
• Molecular formula: C₉H₁₁NO₃
• Molecular weight: 181.19 g/mol

valine    →   valin

Valine is hydrophobic amino acids with aliphatic side chain. It is a member of the branched-chain amino acid family, along with leucine and isoleucine. Valine differs from threonine by replacement of the hydroxyl group with a methyl substituent, but they are of roughly the same shape and volume. The nonpolar hydrophobic amino acids tend to cluster together within proteins, stabilizing protein structure by means of hydrophobic interactions. Valine is an essential amino acid, which means that it cannot be synthesized in the body and must be obtained through dietary sources.

• Abbreviations: Val, V
• IUPAC name: 2-amino-3-methylbutanoic acid
• Molecular formula: C₅H₁₁NO₂
• Molecular weight: 117.15 g/mol

zwitterion    →   dipolarni ion

Zwitterion, also known as inner salt or dipolar ion, is an ion with a positive and a negative electrical charge at different locations within a molecule. As the molecule contains two opposite charges, it is electrically neutral. The term zwitterion is derived from the German word zwitter, meaning a hybrid, hermaphrodite. Zwitterions can be formed from compounds that contain both acid groups and base groups in their molecules (ampholytes).

All of the common amino acids found in proteins are ampholytes because they contain a carboxyl group (-COOH) that acts as an acid and an amino group (-NH₂) that acts as a base. In the solid state, amino acids exist in the dipolar or zwitterion form. If acid is added to a solution containing the zwitterion, the carboxylate group captures a hydrogen (H⁺) ion, and the amino acid becomes positively charged. If base is added, ion removal of the H⁺ ion from the amino group of the zwitterion produces a negatively charged amino acid.