CHEMISTRY GLOSSARY

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

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).

phenylalanine    →   fenilalanin

Phenylalanine is hydrophobic amino acids with aromatic side chain. It is quite hydrophobic and even the free amino acid is not very soluble in water. Phenylalanine is large aromatic residue that is normally found buried in the interior of a protein and is important for protein stability. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Phe, F
• IUPAC name: 2-amino-3-phenylpropanoic acid
• Molecular formula: C₉H₁₁NO₂
• Molecular weight: 165.19 g/mol

polypeptide    →   polipeptid

Polypeptides are peptides containing ten or more amino acid residues. The properties of a polypeptide are determined by the type and sequence of its constituent amino acids.

proline    →   prolin

Proline has an aliphatic side chain with a distinctive cyclic structure. It is unusual because it is conformationally restricted. The secondary amino (imino) group of proline residues is held in a rigid conformation that reduces the structural flexibility of polypeptide regions containing proline. It is not an essential amino acid, which means that the human body can synthesize it.

• Abbreviations: Pro, P
• IUPAC name: pyrrolidine-2-carboxylic acid
• Molecular formula: C₅H₉NO₂
• Molecular weight: 115.13 g/mol

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.

serine    →   serin

Serine is neutral amino acids with polar side chains. It is one of two hydroxyl amino acids. Both are commonly considered to by hydrophilic due to the hydrogen bonding capacity of the hydroxyl group. Serine often serves as a nucleophile in many enzyme active sites, and is best known for its role in the serine proteases. Serine is a site of phosphorylation and glycosylation which is important for enzyme regulation and cell signaling. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine.

• Abbreviations: Ser, S
• IUPAC name: 2-amino-3-hydroxypropanoic acid
• Molecular formula: C₃H₇NO₃
• Molecular weight: 105.09 g/mol

threonine    →   treonin

Threonine is neutral amino acids with polar side chains. It differs from serine by having a methyl substituent in place of one of the hydrogens on the β carbon. Threonine is a site of phosphorylation and glycosylation which is important for enzyme regulation and cell signaling. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Thr, T
• IUPAC name: 2-amino-3-hydroxybutanoic acid
• Molecular formula: C₄H₉NO₃
• Molecular weight: 119.12 g/mol

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.