18 MHR • Unit 1 Metabolic Processes
Figure 1.14BNotice that each amino acid has an amine at one end and a carboxyl
group at the other.
C
H
H
C
O
electrically charged
polar
non-polar
H 3 N+
CH 3
O−
C
H
C
O
H 3 N+
O−
CH
CH 3 CH 3
C
H
C
O
H 3 N+
O−
C
H
CH
CH 3
CH 2
CH 3
C
O
H 3 N+
O−
C
H
CH
CH 2
CH 3
C
O
H 3 N+
O−
H 2 C
H 3 C
NH 3 +
glycine alanine
valine
leucine isoleucine
C
H
CH 2
CH 2
S
CH 3
C
O
H 3 N+
O−
C
H
CH 2
CH 2
CH 2
CH 2
C
O
H 3 N+
O−
methionine
C
H
OH
CH 2
C
O
H 3 N+
O−
serine
CH
OH CH 3
C
H
C
O
H 3 N+
O−
threonine
C
H
SH
CH 2
C
O
H 3 N+
O−
cysteine
C
H
CH 2
C
O
H 3 N+
O−
phenylalanine
O
C
H
C
O
H 3 N+
O−
NH 2
asparagine
CH 2
C
O
C
H
C
O
H 3 N+
O−
aspartic acid
CH 2
C
glutamine
O
C
H
C
O
H 3 N+
O−
NH 2
CH 2
CH 2
C
glutamic acid
acidic
lysine
C NH 2 +
C
H
CH 2
CH 2
CH 2
NH
NH 2
C
O
H 3 N+
O−
arginine
O
C
H
C
O
H 3 N+
O−
CH 2
CH 2
C
tyrosine
C
H
CH 2
OH
C
O
H 3 N+
O−
C
H
CH 2
C
O
H 3 N+
O−
C
H
CH 2
CH 2
C
O
H 3 N+
O−
tryptophan
proline
NH
C
H
CH 2
C
O
H 3 N+
O−
histidine
NH
NH+
basic
O−
O−
The 20 major amino acids, the subunits for proteins. Notice
that each amino acid has one carbon that is bonded to
both an amino group and a carboxyl group. Notice also that
bonded to this same carbon atom is a molecular group that
is highlighted in colour. Biologists refer to this group as a
side-chain or an R-group. The R-group is different for each
amino acid, and is responsible for its chemical properties.