Amino acid is a compound that contains both a carboxyl group and an

amino group. Although many types of amino acids are known, the a-amino acids
are the most signifi cant in the biological world because they are the monomers
from which proteins are constructed. We have already introduced amino acids
(see Connections to Biological Chemistry: “Amino Acids” in Section 3.9). A
general structural formula of an a-amino acid is shown in Figure 27.1. Although
Figure 27.1(a) is a common way of writing structural formulas for amino acids, it
is not accurate because it shows an acid (-COOH) and a base (-NH2) within the
same molecule. These acidic and basic groups react with each other to form a
dipolar ion or internal salt [Figure 27.1(b)]. The internal salt of an amino acid is
given the special name zwitterion. Note that a zwitterion has no net charge; it
contains one positive charge and one negative charge (Brown, 2012: 1098).
According to Timberlake (2012: 559) proteins are composed of molecular
building blocks called amino acids. However, there are only 20 different amino
acids present in human proteins. Every amino acid consists of a central carbon
atom called the -carbon bonded to two functional groups: an amino group and a
carboxylic acid group The -carbon is also bonded to a hydrogen atom and an R
group. It is the R group, which differs in each of the 20 amino acids, that provides
unique characteristics to each type of amino acid. For example, alanine has a
methyl –CH3 as its R group. amino acid with uncharged amino ( and carboxylic
acid ( groups, these groups are ionized for amino acids in most body fluids. At
physiological pH, the group gains to give its ionized form and the group loses to
give its ionized form An ionized amino acid,

Reversing this reaction makes an amino acid stereo specifically out of an

α-keto-acid. In fact, a complete cycle is usually set up whereby one amino acid is
converted to the equivalent α-keto-acid while another α-keto-acid is converted
into its equivalent amino acid. This is true transamination. Amino acids get used
up (making proteins, for example) so, to keep life going, ammonia must be
brought in from somewhere. The key amino acid in this link is glutamic acid. A
true reductive amination using NADPH and ammonia builds glutamic acid from
α-keto-glutaric acid. The other amino acids can now be made from glutamic acid
by transamination. At the end of their useful life they are transaminated back to
glutamic acid which, in mammals at least, gives its nitrogen to urea for excretion
(Clayden, 2001: 1386).
Peptide is the name given to a short polymer of amino acids. Peptides are
classi
 fi ed by the number of amino acid units in the chain. A molecule
containing 2 amino acids joined by an amide bond is called a dipeptide. Those
containing 3 to 10 amino acids are called tripeptides, tetrapeptides, pentapeptides,
and so on. Molecules containing more than 10 but fewer than 20 amino acids are
called oligopeptides. Those containing several dozen or more amino acids are
called polypeptides. Proteins are biological macromolecules of molecular weight
5000 or greater, consisting of one or more polypeptide chains. The distinctions in
this terminology are not precise (Brown, 2012: 1107).