amino acid An organic molecule possessing both
acidic carboxylic acid (–COOH) and basic amino
(–NH2) groups attached to the same tetrahedral carbon
atom.
Amino acids are the principal building blocks of
proteins and enzymes. They are incorporated into
proteins by transfer RNA according to the genetic
code while messenger RNA is being decoded by ribo-
somes. The amino acid content dictates the spatial
and biochemical properties of the protein or enzyme
during and after the final assembly of a protein.
Amino acids have an average molecular weight of
about 135 daltons. While more than 50 have been dis-
covered, 20 are essential for making proteins, long
chains of bonded amino acids.
Some naturally occurring amino acids are alanine,
arginine, asparagine, aspartic acid, cysteine, glutamine,
glutamic acid, glycine, histidine, isoleucine, leucine,
lysine, methionine, phenylalanine, proline, serine, thre-
onine, tryptophan, tyrosine, and valine.
The two classes of amino acids that exist are
based on whether the R-group is hydrophobic or
hydrophilic. Hydrophobic or nonpolar amino acids
tend to repel the aqueous environment and are located
mostly in the interior of proteins. They do not ionize
or participate in the formation of hydrogen bonds. On
the other hand, the hydrophilic or polar amino acids
tend to interact with the aqueous environment, are
usually involved in the formation of hydrogen bonds,
and are usually found on the exterior surfaces of pro-
teins or in their reactive centers. It is for this reason
that certain amino acid R-groups allow enzyme reac-
tions to occur.
The hydrophilic amino acids can be further subdi-
vided into polar with no charge, polar with negatively
charged side chains (acidic), and polar with positively
charged side chains (basic).
