Amino acids are compounds containing both a carboxylic acid group (-COOH) and an amino group (-NH2 ). The most important are the α-amino acids, in which the -NH2 group in attached to the C atom adjacent to the -COOH group. In the β-amino acids, there is an intervening carbon atom.
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.
Arginine is an electrically charged amino acids with basic side chains. It is one of the least frequent amino acids. As a group the charged amino acids are important for making proteins soluble. These residues are generally located on the surface of the protein. Arginine is well designed to bind the phosphate anion, and is often found in the active centers of proteins that bind phosphorylated substrates. As a cation, arginine, as well as lysine, plays a role in maintaining the overall charge balance of a protein. Although arginine is considered an essential amino acid (it must be obtained through the diet), this is true only during the juvenile period in humans.
Conjugated proteins are proteins which have a prostetic group as a part of their structure which is bonded with one or more amino acids of the same protein.
Primary structure of proteins is a sequence of defined amino acids in some protein.
Proteins are natural organic compounds of animal or herbal origin, essential in diet. They are natural polymers developed from a crowd of interconnecting monomers of amino acids, with relative molecular masses amounting up to a few million.
Asparagine is neutral amino acids with polar side chains. The polar amino acids are an important class of amino acids since they provide many of the functional groups found in proteins. Asparagine is a common site for attachment of carbohydrates in glycoproteins. In general this is not very reactive residues. Asparagine is amide derivative of aspartic acid. Asparagine is not essential for humans, which means that it can be synthesized from central metabolic pathway intermediates and is not required in the diet.
Aspartic acid is an electrically charged amino acids with acidic side chains. As a group the charged amino acids are relatively abundant and are generally located on the surface of the protein. Aspartic acid and glutamic acid play important roles as general acids in enzyme active centers, as well as in maintaining the solubility and ionic character of proteins. Aspartic acid (sometimes referred to as asparate depending on pH) is non-essential in mammals, being produced from oxaloacetate by transamination.
Carboxylic acids are organic compounds characterized by the presence of one or more RC(=O)OH groups (the carboxyl group). In the systematic chemical nomenclature carboxylic acids names end in the suffix -oic (e.g. ethanoic acids, CH3COOH). The carbon of the terminal group being counted as part of the chain. They are generally weak acids. Carboxylic acids include a large and important class of fatty acids and may be either saturated or unsaturated. There are also some natural aromatic carboxylic acids (benzoic, salicylic).
Generalic, Eni. "Aminokiseline." Croatian-English Chemistry Dictionary & Glossary. 29 June 2022. KTF-Split. {Date of access}. <https://glossary.periodni.com>.
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