CHEMISTRY GLOSSARY

electrophoresis    →   elektroforeza

Electrophoresis is a technique for the analysis and separation of colloids, based on the movement of charged colloidal particles in an electric field. The migration is toward electrodes of charge opposite to that of the particles. The rate of migration of the particles depends on the field, the charge on the particles, and on other factors, such as the size and shape of the particles.

Electrophoresis is important in the study of proteins. The acidity of the solution can be used to control the direction in which a protein moves upon electrophoresis.

enzyme    →   enzim

Enzyme is a protein that acts as a catalyst in biochemical reactions. Each enzyme is specific to a particular reaction or a group of similar reactions. Many require the association of certain nonprotein cofactors in order to function. The molecule undergoing a reaction (the substrate) binds to a specific active site on the enzyme molecule to form a short-lived intermediate: this greatly increases (by a factor of up to 10²⁰) the rate at which the reaction proceeds to form the product.

glutamic acid    →   glutaminska kiselina

Glutamic acid is an electrically charged amino acids. It is one of the two amino acids that contain a carboxylic acid group in its side chains. These acids play important roles as general acids in enzyme active centers, as well as in maintaining the solubility and ionic character of proteins. Glutamic acid is commonly referred to as glutamate, because its carboxylic acid side chain will be deprotonated and thus negatively charged in its anionic form at physiological pH. Glutamic acid is referred to as a non-essential amino acid because a healthy human can synthesize all the glutamic acid needed for normal body function from other amino acids.

• Abbreviations: Glu, E
• IUPAC name: 2-aminopentanedioic acid
• Molecular formula: C₅H₉NO₄
• Molecular weight: 147.13 g/mol

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.

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

macromolecule    →   makromolekule

Macromolecule is a molecule of high relative molecular mass (molecular weight), the structure of which essentially comprises the multiple repetitions of units derived, actually or conceptually, from molecules of low relative molecular mass. The types of macromolecules are natural and synthetic polymers, carbohydrates, lipids, proteins etc. Cellulose is a polysaccharide that is made up of hundreds, even thousands of glucose molecules strung together.

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