CHEMISTRY GLOSSARY

hydrophobic interaction    →   hidrofobne interakcije

Hydrophobic interaction is the tendency of hydrocarbons (or of lipophilic hydrocarbon-like groups in solutes) to form intermolecular aggregates in an aqueous medium, and analogous intramolecular interactions. The name arises from the attribution of the phenomenon to the apparent repulsion between water and hydrocarbons. Use of the misleading alternative term hydrophobic bond is discouraged.

alanine    →   alanin

Alanine is hydrophobic amino acids with aliphatic side chain. It is the second simplest amino acid, but used the most in proteins. The nonpolar hydrophobic amino acids tend to cluster together within proteins, stabilizing protein structure by means of hydrophobic interactions. Alanine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained directly through the diet.

• Abbreviations: Ala, A
• IUPAC name: 2-aminopropanoic acid
• Molecular formula: C₃H₇NO₂
• Molecular weight: 89.09 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

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

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

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

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

coenzyme    →   koenzim

Coenzyme is an organic nonprotein molecule, such as a vitamin, that associates with an enzyme in catalysing biochemical reactions. Coenzymes usually participate in the substrate-enzyme interaction by donating or acepting certain chemical groups.

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

flotation    →   flotacija

Flotation is a procedure in which hydrophobic solid substances are separated from hydrophilic one using bubbles of air. If air is blow through a suspension, in which substances promoting easier creation of foam are added, bubbles of air are created which stick to the hydrophobic matter and carry it out to the surface.