CHEMISTRY GLOSSARY

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

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.

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.