CHEMISTRY GLOSSARY

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

glutamine    →   glutamin

Glutamine is neutral amino acids with polar side chains. It serves as an important carrier of ammonia and contributes it to the formation of urea and purines. Glutamine is not recognized as an essential amino acid but may become conditionally essential in certain situations, including intensive athletic training or certain gastrointestinal disorders. It is synthesized by the enzyme glutamine synthetase from glutamate and ammonia.

• Abbreviations: Gln, Q
• IUPAC name: 2,5-diamino-5-oxopentanoic acid
• Molecular formula: C₅H₁₀N₂O₃
• Molecular weight: 146.14 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

glycogen    →   glikogen

Glycogen (animal starch) is a polysaccharide that serves the same energy storage function in animals that starch serves in plants. Dietary carbohydrates not needed for immediate energy are converted by the body to glycogen for long term storage (principally in muscle and liver cells). Like amylopectin found in starch, glycogen is a polymer of α(1→4)-linked subunits of glucose, with α(1→6)-linked branches. Glycogen molecules are larger than those of amylopectin (up to 100 000 glucose units) and contain even more branches. Branch points occur about every 10 residues in glycogen and about every 25 residues in amylopectin. The branching also creates lots of ends for enzyme attack and provides for rapid release of glucose when it is needed.

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

ionic radius    →   ionski radijus

Ionic radius is the radius of anions and cations in crystalline ionic compounds, as determined by consistently partitioning the center-to-center distance of ions in those compounds. In general, negative ions have larger ionic radii than positive ions.

ionisation    →   ionizacija

Ionisation is the process of producing ions. Certain molecules ionise in a solution; for example, acids ionise when dissolved in water.

Electron transfer also causes ionisation in certain reactions, for example sodium and chlorine react by transfer of a valence electron from the sodium atom to the chlorine atom to form the ions that constitute a sodium chloride crystal.

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

lysine    →   lizin

Lysine is an electrically charged amino acids with basic side chains. Lysine is a base, as are arginine and histidine. The amino group is highly reactive and often participates in reactions at the active centers of enzymes. Lysine plays an important role in coordinating negatively charged ligands. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Lys, K
• IUPAC name: 2,6-diaminohexanoic acid
• Molecular formula: C₆H₁₄N₂O₂
• Molecular weight: 146.19 g/mol