ALL BIOMOLECULES ARE “MACRO” OR

LARGE MOLECULES
The four biomolecules and their monomers
Proteins
Nucleic Acids (DNA & RNA)
Carbohydrates (Polysaccharide)
Lipids
Note: Strictly speaking Lipids are
not macromolecules because they
are not polymers.
CLASSIFICATION OF
MONOSACCHARIDES
Structures of some common
carbohydrates
 Condensation reaction

Note: the condensation reaction occurs in the polymerization or synthesis of all the
biomolecules. Compare example above – polysaccharide synthesis- to other
biomolecule synthesis reactions.
PROTEINS
Proteins (a polymer) are macromolecules composed of amino acid
subunits (the monomers ).

These amino acids are covalently attached to one another to form long
linear chains called polypeptides, which then fold into a specific three-
dimensional shape.

Sometimes these folded polypeptide chains are functional by

themselves. Other times they combine with additional polypeptide
chains to form the final protein structure.

Sometimes non-polypeptide groups are also required in the final

protein. For instance, the blood protein hemogobin is made up of four
polypeptide chains, each of which also contains a heme molecule,
which is ring structure with an iron atom in its center.
Because form determines function, any slight change to a protein’s
shape may cause the protein to become dysfunctional.
 THE AMINO ACID
Amino acids are the monomers that make up
proteins.

Each amino acid has the same fundamental

structure, which consists of a central carbon atom,
also known as the alpha (α) carbon, bonded to an
amino group (NH2), a carboxyl group (COOH),
and to a hydrogen atom.

In the aqueous environment of the cell, both the

amino group and the carboxyl group are ionized
under physiological conditions, and so have the
structures -NH3+ and -COO–, respectively.

Every amino acid also has another atom or group of

atoms bonded to the central atom known as the R
 THE AMINO ACID
The name “amino acid” is derived from the amino group and carboxyl-acid-group in their basic structure.
There are 21 amino acids present in proteins, each with a specific R group or side chain. Ten of these are
considered essential amino acids in humans because the human body cannot produce them and they must
be obtained from the diet. All organisms have different essential amino acids based on their physiology.
The chemical composition of the side chain determines the characteristics of the amino acid.
The essential amino acids are
arginine (required for the young, but not for adults),
histidine,
isoleucine,
leucine,
lysine,
methionine,
phenylalanine,
threonine,
tryptophan,
valine.
 THE PEPTIDE BOND
Each amino acid is attached to another amino acid by a covalent bond, known as
a peptide bond. When two amino acids are covalently attached by a peptide
bond, the carboxyl group of one amino acid and the amino group of the incoming
amino acid combine and release a molecule of water.
 THE N AND C TERMINALS

The resulting chain of amino acids is called a polypeptide chain. Each polypeptide
has a free amino group at one end. This end is called the N terminus, and the other
end has a free carboxyl group, also known as the C terminus.
The shape of a protein is critical to its function because it determines
whether the protein can interact with other molecules.

Early structural biochemists conceptually divided protein

structures into four “levels” to make it easier to get a handle on
the complexity of the overall structures. To determine how the
protein gets its final shape or conformation, we need to
understand these four levels of protein structure: primary,
secondary, tertiary, and quaternary.
PRIMARY STRUCTURE
A protein’s primary
structure is the unique
sequence of amino acids
in each polypeptide chain
that makes up the
protein. Really, this is
just a list of which amino
acids appear in which
order in a polypeptide
chain, not really a
structure. But, because
the final protein structure
ultimately depends on
this sequence, this was
called the primary
structure of the
polypeptide chain.
IMPORTANCE OF THE SEQUENCE

The Rules of Protein Structure.

The function of a protein is
determined by its shape. The
shape of a protein is determined
by its primary structure
(sequence of amino acids).
SECONDARY STRUCTURE
A protein’s secondary structure is
whatever regular structures arise from
interactions between neighboring or near-
by amino acids as the polypeptide starts to
fold into its functional three-dimensional
form. Secondary structures arise as H
bonds form between local groups of amino
acids in a region of the polypeptide chain.
Rarely does a single secondary structure
extend throughout the polypeptide chain.
It is usually just in a section of the chain.
The most common forms of secondary
structure are the α-helix and β-pleated
sheet structures and they play an important
structural role in most globular and fibrous
 SECONDARY STRUCTURE
The α-helix and β-
pleated sheet form
because of hydrogen
bonding between
carbonyl and amino
groups of neighbouring
amino acids in the
peptide backbone.
Certain amino acids
have a propensity to
form an α-helix, while
others have a
 TERTIARY STRUCTURE

The tertiary structure of a

polypeptide chain is its overall
three-dimensional shape, once all
the secondary structure elements
have folded together among each
other. It is stabilized by
interactions between the R groups.
When a protein loses its three-
dimensional shape, it will no
longer be functional.
 One important amino acid - cysteine
Because it has a very
reactive sulfhydryl
group at its side chain
(the R group). This puts
cysteine in special
position that cannot be
replaced or substituted
by any other amino
acid. Because disulfide
bridges formed by
cysteine residues are
permanent component
of protein primary
structure.
Example of the importance of disulfide bonds in proteins – the antibody which
is a protein which operates in the immune system of animals is stabilized by
disulfide bond resulting in it’s characteristic shape .
 QUATERNARY STRUCTURE
The quaternary structure of a
protein is how its subunits are
oriented and arranged with
respect to one another. As a result,
quaternary structure only applies
to multi-subunit proteins; that is,
proteins made from more than
one polypeptide chain. Proteins
made from a single polypeptide
will not have a quaternary
structure. This level of protein
Structure of Haemoglobin, 4
structure is stabilized by subunits
intermolecular forces of the
subunits
LIPIDS
FATS, OILS, WAXES AND PHOSPHOLIPIDS
Lipids-Role in living things
Lipids are non-polar covalent molecules and are therefore
insoluble in water.

Although some lipids are very large they are not, strictly
speaking, macromolecules because they are not formed by the
polymerization of monomers.

Roles of lipid in living organisms include:

• Energy storage
• Electrical insulation
• Water conservation
• Digestion
• Structural function
• Waterproofing etc.
 FATS and OILS
A fat molecule consists of two main components:
• glycerol
• fatty acids.

Glycerol is an alcohol with three carbons, five hydrogens, and three hydroxyl (OH) groups.
Fatty acids have a long chain of hydrocarbons with a carboxyl group attached. In a fat molecule, the fatty
acids are attached to each of the three carbons of the glycerol molecule with an ester bond through the
oxygen atom. During the ester bond formation, three molecules of water are released. Since fats consist of
three fatty acids and a glycerol, they are also called triacylglycerols or triglycerides.

Note: this is a
condensation
reaction
 Fatty Acid - Saturated or unsaturated?

Fatty acids may be saturated or unsaturated. In a fatty

acid chain, if there are only single bonds between
neighboring carbons in the hydrocarbon chain, the fatty
acid is said to be saturated. Stearic acid and palmitic acid,
which are commonly found in meat, are examples of
saturated fats.
When the hydrocarbon chain contains a double bond, the
fatty acid is said to be unsaturated. Oleic acid is an
example of an unsaturated fatty acid.
 Unsaturated Fatty Acid - Monounsaturated or
Polyunsaturated
If there is only one double
bond in the molecule, then it
is known as a
monounsaturated fat; e.g.
olive oil. If there is more than
one double bond, then it is
known as a polyunsaturated
fat; e.g. canola oil.
 Fatty Acid – ‘Cis’ or ‘trans’

Cis and trans indicate the configuration

of the molecule around the double bond.
If hydrogens are present in the same
plane, it is referred to as a cis fat; if the
hydrogen atoms are on two different
planes, it is referred to as a trans fat.
 Solid or liquid?
Most unsaturated fats
are liquid at room
temperature and are
called oils
 Essential fatty acids
Essential fatty acids are fatty acids required for
biological processes, but not synthesized by the human
body. Consequently we get them from our diet and
they are nutritionally very important. only two fatty
acids known to be essential for humans
• Omega-3 fatty acid, or alpha-linoleic acid (ALA
• omega-6 fatty acid, or linoleic acid).

Salmon, trout, and tuna are good sources of omega-3

fatty acids. Plant sources of Linoleic acid include
seeds, nuts, grains and legumes. Alpha-linolenic acid
is found in the green leaves of plants, including
phytoplankton and algae, and in selected seeds, nuts
and legumes (flax, canola, walnuts and soy).
Carotenoids and steroids

The next two lipid classes we’ll discuss

—the carotenoids and the steroids—have
chemical structures very different from
those of triglycerides and phospholipids
and from each other. Both carotenoids
and steroids are synthesized by covalent
linking and chemical modification of
isoprene to form a series of isoprene
units.
 carotenoids
The carotenoids are a family of light-
absorbing pigments found in plants and
animals. They are synthesized by
covalent linking of and chemical
modification of isoprene to for a series
of isoprene units. Beta-carotene is one of
the pigments that traps light energy in
leaves during photosynthesis. In humans,
a molecule of beta-carotene can be
broken down into two vitamin A
molecules, from which we make the
pigment rhodopsin, which is required for
vision. Carotenoids are responsible for
the colors of carrots, tomatoes,
pumpkins, egg yolks and butter.
 STEROID
S
The steroids are a family of organic compounds whose
multiple rings share carbons. The steroid cholesterol is an
important constituent of membranes. Other steroids function
as hormones, chemical signals that carry messages from one
part of the body to another. Testosterone and the estrogens
are steroid hormones that regulate sexual development in
vertebrates. Cortisol and related hormones play many
regulatory roles in the digestion of carbohydrates and
proteins, in the maintenance of salt balance and water
balance and in sexual development. Cholesterol is
synthesized in the liver and is the starting material for
making testosterone and other steroid hormones, as well as
the bile salts that help break down dietary fats so that they
can be digested. Cholesterol is absorbed from foods such as
Waxes
All waxes have the same basic structure: They are formed
by an ester linkage between a saturated, long-chain fatty
acid and a saturated, long-chain alcohol. The result is a
very long molecule, with 40–60 CH2 groups.

Plants use waxes as a protective coating to control

evaporation and hydration and to prevent them from
drying out. Waxes are valuable to both plants and animals
because of their hydrophobic nature. This makes them
water resistant, which prevents water from sticking on
surfaces.
waxes
The sheen on human hair is not
there only for cosmetic purposes.
Glands in the skin secrete a waxy
coating that repels water and
keeps the hair pliable. Birds that
live near water have a similar
waxy coating on their feathers.
The shiny leaves of holly plants,
familiar during winter holidays,
also have a waxy coating. Finally,
bees make their honeycombs out
of wax For example, here is the
structure of beeswax: This highly
nonpolar structure accounts for
Commercial uses of waxes
 PHOSPOLIPIDS

Phospholipids Like triglycerides, are composed

of

fatty acid chains

a glycerol backbone.
Unlike triglycerides, which have three fatty
acids, phospholipids have two fatty acids and
third carbon of the glycerol backbone is
occupied by a modified phosphate group.
 PHOSPHOLIP
IDS
A phospholipid is an amphipathic molecule which means
it has both a hydrophobic and a hydrophilic component.
A single phospholipid molecule has a phosphate group on
one end, called the “head,” and two side-by-side chains
of fatty acids that make up the lipid “tails. ” The
phosphate group is negatively charged, making the head
polar and hydrophilic, or “water loving.” The phosphate
heads are thus attracted to the water molecules in their
environment.

The lipid tails, on the other hand, are uncharged,

nonpolar, and hydrophobic, or “water fearing.” A
hydrophobic molecule repels and is repelled by water.
Some lipid tails consist of saturated fatty acids and some
contain unsaturated fatty acids. This combination adds to
the fluidity of the tails that are constantly in motion.
Phospholipid Bilayer: The phospholipid bilayer consists of two
adjacent sheets of phospholipids, arranged tail to tail. The
hydrophobic tails associate with one another, forming the
interior of the membrane. The polar heads contact the fluid
inside and outside of the cell.
The cell membrane consists of two adjacent layers of
phospholipids, which form a bilayer. The fatty acid tails of
phospholipids face inside, away from water, whereas the
phosphate heads face the outward aqueous side.

Because of the phospholipds’ chemical and physical

characteristics, the lipid bilayer acts as a semipermeable
membrane; only lipophilic (easily dissolved in lipids)
solutes can easily pass the phospholipd bilayer. As a result,
there are two distinct aqueous compartments on each side
of the membrane. This separation is essential for many
biological functions, including cell communication and
metabolism.