PROPERTIES OF AMINO ACIDS

The Genetic Code Specifies

20 l-`-Amino Acids
Although more than 300 amino acids occur in nature, proteins
are synthesized almost exclusively from the set of 20 l-a-
amino acids encoded by nucleotide triplets called codons
(see Table 37�1). While the three-letter genetic code could
potentially accommodate more than 20 amino acids, the
genetic code is redundant since several amino acids are
specified by multiple codons. Scientists frequently represent
the sequences of peptides and proteins using one- and threeletter
abbreviations for each amino acid (Table 3�1). These
amino acids can be characterized as being either hydrophilic
or hydrophobic (Table 3�2), properties that affect their location
in a protein�s mature folded conformation (see Chapter 5).
Some proteins contain additional amino acids that arise by
the post-translational modification of an amino acid already
present in a peptide. Examples include the conversion of
peptidyl proline and peptidyl lysine to 4-hydroxyproline and
5-hydroxylysine; the conversion of peptidyl glutamate to
g-carboxyglutamate; and the methylation, formylation, acetylation,
prenylation, and phosphorylation of certain aminoacyl
residues. These modifications significantly extend the biologic
diversity of proteins by altering their solubility, stability, catalytic
activity, and interaction with other proteins.
Selenocysteine, the 21st
Protein l-`-Amino Acid
Selenocysteine (Figure 3�1) is an l-a-amino acid found in
proteins from every domain of life. Humans contain approximately
two dozen selenoproteins that include certain peroxidases
and reductases, selenoprotein P, which circulates in
the plasma, and the iodothyronine deiodinases responsible
for converting the prohormone thyroxine (T4) to the thyroid
hormone 3,3'5-triiodothyronine (T3) (see Chapter 41). As its
name implies, a selenium atom replaces the sulfur of its elemental
analog, cysteine. Selenocysteine is not the product of
a posttranslational modification, but is inserted directly into
a growing polypeptide during translation. Selenocysteine thus
TABLE 3�1 l-`-Amino Acids Present in Proteins
Name Symbol Structural Formula pK1 pK2 pK3

Posttranslational Modifications
onfer Additional Properties
While some prokaryotes incorporate pyrrolysine into proteins,
and plants can incorporate azetidine-2-carboxylic acid, an analog
of proline, a set of just 21 l-a-amino acids clearly suffices
for the formation of most proteins. Posttranslational modifications
can, however, generate novel R-groups that impart further
properties. In collagen, for example, protein-bound proline
and lysine residues are converted to 4-hydroxyproline and
5-hydroxylysine (Figure 3�2). The carboxylation of glutamyl
residues of proteins of the coagulation cascade to g-carboxyglutamyl
With Aliphatic Side Chains `-COOH `-NH3
+ R Group
Glycine Gly [G] H CH
NH3
+
COO� 2.4 9.8
Alanine Ala [A] CH3 CH
NH3
+
COO� 2.4 9.9
Valine Val [V]
CH
H3C
H3C
CH
NH3
+
COO�
2.2 9.7
Leucine Leu [L]
CH
H3C
H3C
NH3
+
CH2 CH COO�
2.3 9.7
Isoleucine Ile [I]
CH
CH2
CH3
CH
NH3
+
COO�
CH3 2.3 9.8
With Side Chains Containing Hydroxylic (OH) Groups
Serine Ser [S] CH
NH3
+
CH2 COO�
OH
2.2 9.2 about 13
Threonine Thr [T]
See below.
CH
NH3
+
CH COO�
OH
CH3
2.1 9.1 about 13
Tyrosine Tyr [Y] See below.
(continued )
vip.persianss.