10

Science
Quarter 4-Modules 3 & 4
Chemistry of Biomolecules

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Quarter 4 – Modules 3 & 4 : Chemistry of Biomolecules
Second Edition, Revised 2021

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 Modules
Chemistry of Biomolecules
3&4

Introduction
Think about the food you eat everyday. Different types of food give you
different nutrients for energy, growth and repair. In your Grade 9, you have learned
that the bonding characteristics of carbon result in the formation of large variety of
compounds.

In this module, you will understand the structure of biomolecules which are
made up mainly of carbon, hydrogen and oxygen as well as proteins and nucleic
acids and some derivatives of carbohydrates and lipids which also contain nitrogen.
Also, you will learn why these biomolecules are important to all living things and
what differentiates them from each other.

This module contains activities that will enhance understanding about the
major groups of biomolecules divided into four (4) lessons.

Lesson 1 - Carbohydrates
Lesson 2 - Proteins
Lesson 3 - Lipids
Lesson 4 - Nucleic Acids

Learning competencies/objectives

At the end of this module you are expected to:

1. Identify the major categories of biomolecules such as carbohydrates, proteins,
lipids and nucleic acids
2. Differentiate the biomolecules from each other in terms of their structure and
function
3. Recognize the major categories of biomolecules such as carbohydrates, lipids,
proteins and nucleic acids.

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 What is It

Since food is always part of our lives

it is important that we know the nutrients
found in the food we eat. Figure 1 shows
some foods that are rich in
carbohydrates. Biologically speaking,
carbohydrates are molecules that contain
carbon, hydrogen and oxygen atoms in
specific ratios.

FUNCTIONS OF CARBOHYDRATES
1. It provides your body with energy
One of the primary functions of
carbohydrates is to provide your body
with energy. Most of the carbohydrates in
the foods you eat are digested and broken down into glucose before entering the
bloodstream.
Glucose in the blood is taken up into your body’s cells and used to produce a
fuel molecule called adenosine triphosphate (ATP) through a series of complex
processes known as cellular respiration. Cells can then use ATP to power a variety
of metabolic tasks.

2. They also provide stored energy

If your body has enough glucose to fulfill its current needs, excess glucose can
be stored for later use. This stored form of glucose is called glycogen and is primarily
found in the liver and muscle.
The liver contains approximately 100 grams of glycogen. These stored glucose
molecules can be released into the blood to provide energy throughout the body and
help maintain normal blood sugar levels between meals.
In circumstances in which you have all of the glucose your body needs and
your glycogen stores are full, your body can convert excess carbohydrates into
triglyceride molecules and store them as fat.

3. It helps preserve muscle

Glycogen storage is just one of several ways your body makes sure it has
enough glucose for all of its functions. When glucose from carbohydrates is lacking,
muscle can also be broken down into amino acids and converted into glucose or
other compounds to generate energy.
Obviously, this isn’t an ideal scenario, since muscle cells are crucial for body
movement. Severe losses of muscle mass have been associated with poor health and
a higher risk of death. However, this is one way the body provides adequate energy
for the brain, which requires some glucose for energy even during periods of
prolonged starvation.

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4. They promote digestive health
Unlike sugars and starches, dietary fiber is not broken down into glucose.
Instead, this type of carbohydrate passes through the body undigested. It can be
categorized into two main types of fiber: soluble and insoluble.
Soluble fiber is found in oats, legumes and the inner part of fruits and some
vegetables. While passing through the body, it draws in water and forms a gel-like
substance. This increases the bulk of your stool and softens it to help make bowel
movements easier.
On the other hand, insoluble fiber helps alleviate constipation by adding bulk
to your stools and making things move a little quicker through the digestive tract.
This type of fiber is found in whole grains and the skins and seeds of fruits and
vegetables. Getting enough insoluble fiber may also protect against digestive tract
diseases.

5. They Influence Heart Health and Diabetes

Certainly, eating excessive amounts of refined carbs is detrimental to your
heart and may increase your risk of diabetes. However, eating plenty of dietary fiber
can benefit your heart and blood sugar levels.

CLASSIFICATIONS OF CARBOHYDRATES

1. MONOSACCHARIDES

From the prefix “mono” which means

one, monosaccharide is the simplest sugar
and the basic subunit of a carbohydrate.
These compounds are white solids at room
temperature. Because they have polar,
hydroxyl (-OH) groups in their molecular
structures, they are very soluble in water.
The most common monosaccharides are
Figure 2. Structure of Glucose and Fructose
http://joelbergenerdc.com/tag/glucose-vs-
fructose/

GLUCOSE (also called dextrose) and FRUCTOSE.

Although both of these monosaccharides have the formula C 6H12O6, their

structural formulas differ. As Figure 2 shows, glucose in water solution forms a ring
made up of five carbon atoms and one oxygen atom, and fructose in a water solution
forms a ring made up of four carbon atoms and one oxygen atom. Both compounds
have five-OH groups in their structures.
Fruits like grapes, apple or atis contain a monosaccharide called FRUCTOSE
or fruit sugar. It is considered the sweetest naturally occurring sugar. Due to its
sweetness, fructose is sometimes used as low calories sweetener because less
fructose is needed to produce the same sweetness that table sugar does. Starchy
food that we eat is widely distributed in the plant world. Thus, its main constituent
glucose is found in all plants and in the sap of trees. However, glucose is also found
in glycogen that is produced in animal cells.
Another example of monosaccharide is the GALACTOSE. Galactose is more
commonly found in the disaccharide, lactose or milk sugar. It is found as the
monosaccharide in peas. Galactose is classified as a monosaccharide, an aldose, a
hexose, and is a reducing sugar.

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2. DISACCHARIDES
Similar to other carbohydrates, disaccharides are comprised
of hydrogen, carbon, and oxygen, and the ratio of hydrogen atoms to oxygen atoms
is often 2:1, which explains why they are referred to as hydrates of carbon. The
general chemical formula of disaccharides is C 12H22O11. Because of the presence of
carbon and C-C and C-H covalent bonds, disaccharides are also organic compounds,
just as the other carbohydrates.
A disaccharide is a carbohydrate or a sugar comprised of two
monosaccharides joined together by a glycosidic bond (or glycosidic linkage).
Glycosidic bonds are covalent bonds that may form between the hydroxyl groups of
two monosaccharides. Thus, even if they have the same chemical formula, there are
different kinds of disaccharides that differ in bond formations, as well as
monosaccharide constituents, and therefore, different properties.
The most common disaccharide is the table sugar also called SUCROSE with
the molecular formula C12H22O11.
CONDENSATION REACTION is a reaction in which two molecules or parts of
the same molecule combine. During the condensation of monosaccharides to form
disaccharides, one molecule of water is lost. When two glucose molecules are
combined, maltose is form and water is lost during the process. A HYDROLYSIS
REACTION occurs when the bond between monosaccharides is broken with the
addition of a water molecule.
Another important disaccharide – Lactose or milk sugar. Lactose is made up
of a sugar called GALACTOSE and GLUCOSE. In our body, a specific enzyme,
LACTACE is necessary to help break the bond between the two monosaccharides
when lactose is digested.

People who cannot

digest milk products are
called “lactose intolerant”
because they do not produce
the enzyme (lactase)
necessary to break the bond
between glucose and
galactose. Since lactose
molecules are too large to be
absorbed into the circulatory
system, they continue
through the digestive system,
where they are eventually
broken down by bacteria in
the large intestine. These
bacteria digest
monosaccharides, producing
carbon dioxide gas in the
process. As a result, a
common symptom of lactose
intolerance is a buildup of intestinal gas along with a bloated feeling, and more often
the passing out of undigested lactose as diarrhea.

Figure 3 shows that when two monosaccharides joint together by combination

reaction, a glycosidic bond will be formed between the two monosaccharide
molecules. The reaction produces water as a side product.

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3. POLYSACCHARIDES
Polysaccharides are characterized by the following chemical properties: (1) not
sweet in taste, (2) many of which are insoluble in water, (3) do not form crystals when
desiccated, (4) compact and not osmotically active inside the cells, (5) can be extracted
to form white powder, and (6) general chemical formula of Cx(H2O)y.
Polysaccharides consist of hydrogen, carbon, and oxygen, just as the other
forms of carbohydrates. The ratio of hydrogen atoms to oxygen atoms is often 2:1,
which is why they are also described as hydrates of carbon. The general chemical
formula of polysaccharides is (C6H10O5)n. Because of the presence of carbon and C-C
and C-H covalent bonds, they are considered as organic compounds similar to other
carbohydrates.
Polysaccharides may be a homopolysaccharide or
a heteropolysaccharide depending on their monosaccharide components.
A homopolysaccharide (also called homoglycan) is made up of only one type of
monosaccharide whereas a heteropolysaccharide (also called heteroglycan) is
composed of different types of monosaccharides.
Based on their function, polysaccharides may be classified
as storage or structural polysaccharides. Storage polysaccharides are those that
are used for storage. For instance, plants store glucose in the form of starch.
Animals store simple sugars in the form of glycogen. Structural polysaccharides
are carbohydrates that have a structural role. Plants have celluloses, which are
polymers of repeated glucose units that are joined by beta-linkages. Certain animals
produce chitin that serves as a structural component, for example, of exoskeleton.
Common examples of polysaccharides are cellulose, starch, glycogen,
and chitin.

a. Cellulose is polysaccharide consisting

of a linear chain of β (1→4) linked D-
glucose units: (C6H10O5) n.
b. Starch is polysaccharide carbohydrate
(C6H10O5)n consisting of a large number
of glucose monosaccharide units joined
together by glycosidic bonds found
especially in seeds, bulbs, and tubers.
c. Glycogen is a branched polymer of
glucose that is mainly produced in liver
and muscle cells, and functions as
secondary long-term energy storage in
animal cells.
d. Chitin is a polymer of nitrogen-
containing polysaccharide (C8H13O5N)n
rendering a tough, protective covering or
structural support in certain organisms.
It makes up the cell walls
of fungi and exoskeleton of insects. Figure 4. Structure of cellulose, starch,
glycogen and chitin
https://www.pinterest.ph/pin/605804587
356684138/

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Figure 5. Hydrolysis (Breakdown of Starch)
https://www.quora.com/How-does-
amylase-break-down-starch-into-glucose
The breakdown of starch
requires a water molecule to provide a
hydrogen atom and a hydroxyl group to
the site where the bond is broken. With
the help of enzymes in the digestive
system, the glucose units can be
separated from one another. When a
glucose molecule is separated from the
rest of the starch polymer; it can be
absorbed and used as fuel by your cells.
Since it takes time for glucose to be
separated from the polysaccharide, it is
released to the cells gradually. Thus,
the glucose from starch reaches muscle
cells over a period of time providing
energy as it is needed. For this reason,
athletes often eat meals rich complex
carbohydrates before an athletic event.

Starch is the chief storage form of carbohydrates in plants and the most
important source of carbohydrate in human nutrition. A starch molecule is a
polysaccharide assembled from the simple sugar glucose; it can contain anywhere
from five hundred to several hundred thousand glucose molecules joined by covalent
bonds into a single structure. Starch is made up of two types of polysaccharides;
AMYLOSE, which is coiled or helical structure, and AMYLOPECTIN, which is
branched. Plants make starch.

Figure 6. Structure of Amylose and Amylopectin

https://www.researchgate.net/figure/Starch-amylose-and-amylopectin-
structure_fig6_321226776

All individuals whose intake of glucose is excessive will store the excess
glucose as fat for long term storage and some are converted to another
polysaccharide GLYCOGEN. Glycogen is a polysaccharide that is similar to starch
because it is also composed of alpha glucose units. It differs from starch since
glycogen shows a higher degree of branching and is a polysaccharide that is made
by animal.
On the other hand, starch contains both straight chain and branched
polysaccharides with much less branching than that of glycogen, and is made only
by plant.

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 Figure 7. Structure of Glycogen
https://slideplayer.com/slide/9886242

Figure 7 shows the structure of glycogen which consists of long polymer

chains of glucose units connected by an alpha glycosidic linkage. It is a
multibranched polysaccharide of glucose that serves as a form of energy storage in
animals. The polysaccharide structure represents the main storage form of glucose
in the body.
Glycogen is the readily available energy stored in liver and muscles and the
one that is easily metabolized. Fats are stored in adipose tissues but unlike glycogen,
are not as readily metabolized. They are used during prolonged exercise or activity.

What’s More

Copy and fill in the graphic organizer. Choose your answers from the box
below.

Carbohydrates
Monosaccharides
Disaccharides
Polysaccharides
Glucose
Fructose
Galactose
Sucrose
Cellulose
Maltose
Lactose
Glycogen
Starch

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 Lesson
Proteins
2
At the end of the lesson, you are expected to:

1. Describe the general structure of an amino acid.

2. List the twenty common amino acids found in living organisms.
3. Classify the twenty common amino acids
4. Describe how a peptide bond forms.
5. Define a protein and differentiate between the four levels of structure of a protein.
6. Describe the biological functions of proteins in living things

What’s New

Activity 1: MY PLATE OF FOOD GROUPS

Look at the plate below.

To what food group is labelled #3.

What is It

PROTEINS

Proteins are among the most abundant organic molecules in living systems
and are way more diverse in structure and function than other classes of
macromolecules. A single cell can contain thousands of proteins, each with a unique
function. Although their structures, like their functions, vary greatly, all proteins
are made up of one or more chains of amino acids.

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 Types and functions of proteins

Proteins can play a wide array

of roles in a cell or organism.

Figure 8. Foods rich in Proteins
https://www.livescience.com/53044-
protein.html
Enzymes
Enzymes act as catalysts in
biochemical reactions, meaning that
they speed the reactions up. Each
enzyme recognizes one or more
substrates, the molecules that serve
as starting material for the reaction it
catalyzes. Different enzymes
participate in different types of
reactions and may break down, link
up, or rearrange their substrates.

One example of an enzyme found in your body is salivary amylase, which

breaks amylose (a kind of starch) down into smaller sugars. The amylose doesn’t
taste very sweet, but the smaller sugars do. This is why starchy foods often taste
sweeter if you chew them for longer: you’re giving salivary amylase time to get to
work.

Hormones
Hormones are long-distance chemical signals released by endocrine cells (like
the cells of your pituitary gland). They control specific physiological processes, such
as growth, development, metabolism, and reproduction. While some hormones are
steroid-based, others are proteins. These protein-based hormones are commonly
called peptide hormones.
For example, insulin is an important peptide hormone that helps regulate
blood glucose levels. When blood glucose rises (for instance, after you eat a meal),
specialized cells in the pancreas release insulin. The insulin binds to cells in the liver
and other parts of the body, causing them to take up the glucose. This process helps
return blood sugar to its normal, resting level.
Some additional types of proteins and their functions are listed in the table
below:
Table 1. Types and Functions of Proteins

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 Proteins come in many different shapes and sizes. Some are globular (roughly
spherical) in shape, whereas others form long, thin fibers. For example, the
hemoglobin protein that carries oxygen in the blood is a globular protein, while
collagen, found in our skin, is a fibrous protein.

A protein’s shape is critical to its function, and, many different types of

chemical bonds may be important in maintaining this shape. Changes in
temperature and pH, as well as the presence of certain chemicals, may disrupt a
protein’s shape and cause it to lose functionality, a process known as denaturation.

Amino acids

Amino acids are the monomers that make up

proteins. Specifically, a protein is made up of one or
more linear chains of amino acids, each of which is
called a polypeptide. There are 20 types of amino
acids commonly found in proteins.
Amino acids share a basic structure, which
consists of a central carbon atom, also known as the
alpha (α) carbon, bonded to an amino group (NH 2),
Figure 9. Image of an amino acid, indicating
a carboxyl group (COOH), and a hydrogen atom. the amino group, carboxyl group, alpha
carbon, and R group.
Properties of Amino Acids
A. Physical Properties
1. Amino acids are colorless, crystalline solid.
2. All amino acids have a high melting point greater than 200o
3. Solubility: They are soluble in water, slightly soluble in alcohol and dissolve
with difficulty in methanol, ethanol, and propanol. R-group of amino acids and
pH of the solvent play important role in solubility.
4. On heating to high temperatures, they decompose.
5. All amino acids (except glycine) are optically active.
6. Peptide bond formation: Amino acids can connect with a peptide bond involving
their amino and carboxylate groups. A covalent bond formed between the alpha-
amino group of one amino acid and an alpha-carboxyl group of other forming -
CO-NH-linkage. Peptide bonds are planar and partially ionic.

B. Chemical Properties
1. Zwitterionic property
A zwitterion is a molecule with functional groups, of which at least one
has a positive and one has a negative electrical charge. The net charge of the
entire molecule is zero. Amino acids are the best-known examples of zwitterions.
They contain an amine group (basic) and a carboxylic group (acidic). The -
NH2 group is the stronger base, and so it picks up H+ from the -COOH group to
leave a zwitterion. The (neutral) zwitterion is the usual form amino acids exist
in solution.
2. Amphoteric property
Amino acids are amphoteric in nature that is they act as both acids and
base since due to the two amine and carboxylic group present.
3. Ninhydrin test
When 1 ml of Ninhydrin solution is added to a 1 ml protein solution and
heated, the formation of a violet color indicates the presence of α-amino acids.
4. Xanthoproteic test
The xanthoproteic test is performed for the detection of aromatic amino
acids (tyrosine, tryptophan, and phenylalanine) in a protein solution. The

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 nitration of benzoid radicals present in the amino acid chain occurs due to
reaction with nitric acid, giving the solution yellow coloration.
5. Reaction with Sanger’s reagent
Sanger’s reagent (1-fluoro-2, 4-dinitrobenzene) reacts with a free amino
group in the peptide chain in a mild alkaline medium under cold conditions.
6. Reaction with nitrous acid
Nitrous acid reacts with the amino group to liberate nitrogen and form
the corresponding hydroxyl.
Classification of Amino Acids
A. On the basis of R-group
1. Nonpolar, Aliphatic amino acids: The R groups in this class of amino
acids are nonpolar and hydrophobic. Glycine, Alanine, Valine, leucine,
Isoleucine, Methionine, Proline.
2. Aromatic amino acids: Phenylalanine, tyrosine, and tryptophan, with
their aromatic side chains, are relatively nonpolar (hydrophobic). All can
participate in hydrophobic interactions.
3. Polar, Uncharged amino acids: The R groups of these amino acids are
more soluble in water, or more hydrophilic, than those of the nonpolar amino
acids, because they contain functional groups that form hydrogen bonds
with water. This class of amino acids includes serine, threonine, cysteine,
asparagine, and glutamine.
4. Acidic amino acids: Amino acids in which R-group is acidic or negatively
charged. Glutamic acid and Aspartic acid
5. Basic amino acids: Amino acids in which R-group is basic or positively
charged. Lysine, Arginine, Histidine
B. On the basis of nutrition
1. Essential amino acids (Nine)
Nine amino acids cannot be synthesized in the body and, therefore,
must be present in the diet in order for protein synthesis to occur. These
essential amino acids are histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan, and valine.
2. Non-essential amino acids (Eleven)
These amino acids can be synthesized in the body itself and hence not
necessarily need to be acquired through diet. Arginine, glutamine, tyrosine,
cysteine, glycine, proline, serine, ornithine, alanine, asparagine, and
aspartate.
3. Conditionally
Conditional amino acids are usually not essential, except in times of
illness and stress. It include: arginine, cysteine, glutamine, tyrosine,
glycine, ornithine, proline, and serine.
C. On the basis of metabolic fate
1. Glucogenic amino acids: These amino acids serve as precursors
gluconeogenesis for glucose formation. Glycine, alanine, serine, aspartic
acid, asparagine, glutamic acid, glutamine, proline, valine, methionine,
cysteine, histidine, and arginine.
2. Ketogenic amino acids: These amino acids breakdown to form ketone
bodies. Leucine and Lysine.
3. Both glucogenic and ketogenic amino acids: These amino acids
breakdown to form precursors for both ketone bodies and glucose.
Isoleucine, Phenylalanine, Tryptophan, and tyrosine.

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 Figure 10. Twenty-one Amino Acids

Peptide bonds

Each protein in your cells consists of one or

more polypeptide chains. Each of these polypeptide
chains is made up of amino acids, linked together in
a specific order. A polypeptide is kind of like a long
word that is "spelled out" in amino acid. The
chemical properties and order of the amino acids are
key in determining the structure and function of the
polypeptide, and the protein it is part of. But how
are amino acids actually linked together in chains?
The amino acids of a polypeptide are attached
Figure 11. Illustration of
to their neighbors by covalent bonds known as
Peptide Bond
a peptide bonds. Each bond forms in a dehydration
synthesis (condensation) reaction. During protein synthesis, the carboxyl group of

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the amino acid at the end of the growing polypeptide chain reacts with the amino
group of an incoming amino acid, releasing a molecule of water. The resulting bond
between amino acids is a peptide bond
Peptide bond formation between two amino acids. In a peptide bond, the
carbonyl C of one amino acid is connected to the amino N of another.

Because of the
structure of the amino acids,
a polypeptide chain
has directionality, meaning
that it has two ends that are
chemically distinct from one
another. At one end, the
polypeptide has a free amino
group, and this end is called
the amino terminus (or N-
Figure 12. Polypeptide Chain terminus). The other end, which
has a free carboxyl group, is known
as the carboxyl terminus (or C-terminus). The N-terminus is on the left and the C-
terminus is on the right for the very short polypeptide shown above.

Levels of protein structure

Primary Structure

The primary protein structure refers to

the sequence of amino acids and the location of
disulfide bonds.
The amino acids, when linked by peptide
bonds, are referred to as residues. Short chains
of amino acid residues are often called (oligo-)
peptides.

Secondary Structure

Secondary structure refers to regular,

local structure of the protein backbone,
Figure 12. Primary Structure stabilized by intramolecular and sometimes
intermolecular hydrogen bonding of amide
groups.

Types of Secondary Structure

1. The alpha helix (α-helix) has a right-handed spiral conformation, in which every
backbone N-H group donates a hydrogen bond to the backbone C=O group of the
amino acid four residues before it in the sequence.
2. The other common type of secondary structure is the beta strand. A Beta strand
(β-strand) is a stretch of polypeptide chain, typically 3 to 10 amino acids long,

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 with its backbone in an almost fully extended
conformation. Two or more parallel or anti-
parallel adjacent polypeptide chains of beta
strand stabilized by hydrogen bonds form a beta
sheet. For example, the proteins in silk have a
beta sheet structure. Those local structures are
stabilized by hydrogen bonds and connected by
tight turns and loose, flexible loops.

Tertiary Structure
The spatial arrangement of secondary
Figure 13. Alpha helix (blue) and anti- structure elements results in the formation of
parallel beta sheet composed of three beta the tertiary structure, or fold, of a protein. The
strands (yellow and red).
tertiary structure is held together by non-
covalent interactions (hydrogen bonding, ionic interactions, van der Waals forces,
and hydrophobic packing), disulphide bonds and metal ion coordination.
An example of tertiary structure is a
single-domain globular protein. Globular
proteins (are sphere-like proteins that are more
or less soluble in aqueous solutions (the other
two protein classes are membrane and fibrous
proteins)

Quaternary Structure

Some proteins form assemblies (units)

with other molecules – this is called the
quaternary structure.
Figure 14. Tertiary Structure
Two examples are: hemoglobin which is
an assembly of four globular proteins and the
actin microfilament, composed of many
thousands of actin molecules.
Assemblies of different proteins or
macromolecules are also referred to as the
quaternary structure; for example,
the ribosome, a combination of different RNA
and protein molecules, is a form of quaternary
structure.

Figure 15. Quaternary Structure

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 What’s More

A. Classify these amino acids as ACIDIC, BASIC, NEUTRAL POLAR

or NEUTRAL NONPOLAR. Write your answers on your answer sheet.

1 2 3 4 5
B. Identify which of the diagrams below represents a proteins primary structure,
secondary structure, tertiary structure or quaternary structure. Write your
answer on your answer sheet.

6 7 8 9

1. Explain the importance of lipids in the body

2. compare the structure of saturated and unsaturated fatty acids,
3. describe the properties of triglyceride, phospholipid, and cholesterol molecules
and relate them to their functions in organisms,
4. recall that lipids can be classified into simple, complex, and derived lipids.

What’s New

WORD SEARCH
Instructions: Find the word in the word search puzzle. Words only run across and
down. Write your answer in your answer sheet. Use the picture on the side as your
hint or clue.

17 | Page
 What is It

LIPIDS

Lipids are molecules that contain hydrocarbons and make up the building
blocks of the structure and function of living cells. Examples of lipids include fats,
oils, waxes, certain vitamins (such as A, D, E and K), hormones and most of the cell
membrane that is not made up of protein.

Lipids are not soluble in water as they are non-polar, but are thus soluble in
non-polar solvents such as chloroform.

Lipids are mainly composed of hydrocarbons

in their most reduced form, making them an
excellent form of energy storage, as when
metabolized the hydrocarbons oxidize to release
large amounts of energy. The type of lipid found in
fat cells for this purpose is a triglyceride, an ester
created from glycerol and three fatty acids.

Excess carbohydrates in the diet are

converted into triglycerides, which involves the
synthesis of fatty acids from acetyl-CoA in a
Figure 16. Food rich in Lipids process known as lipogenesis and takes place in
https://examples.yourdictionary.c
the endoplasmic reticulum. In animals and fungi,
om/examples-of-lipids.html
a single multi-functional protein handles most of
these processes, while bacteria utilize multiple separate enzymes. Some types of
unsaturated fatty acids cannot be synthesized in mammalian cells, and so must be
consumed as part of the diet, such as omega-3.

Acetyl-CoA is also involved in the mevalonate pathway, responsible for

producing a wide range of isoprenoids, which include important lipids such as
cholesterol and steroid hormones.

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Properties of Lipids

Lipids are a family of organic compounds, composed of fats and oils. These
molecules yield high energy and are responsible for different functions within the
human body. Listed below are some important characteristics of Lipids.

1. Lipids are oily or greasy nonpolar molecules, stored in the adipose tissue of
the body.
2. Lipids are a heterogeneous group of compounds, mainly composed of
hydrocarbon chains.
3. Lipids are energy-rich organic molecules, which provide energy for different
life processes.
4. Lipids are a class of compounds characterised by their solubility in nonpolar
solvents and insolubility in water.
5. Lipids are significant in biological systems as they form a mechanical barrier
dividing a cell from the external environment known as the cell membrane.

Lipid Structure
Lipids are the polymers of fatty acids
that contain a long, non-polar hydrocarbon
chain with a small polar region containing
oxygen. The lipid structure is explained in
the diagram:
Classification of Lipids

Figure 17. Lipid Structure Lipids can be classified into two main
classes:

• Nonsaponifiable lipids

A nonsaponifiable lipid cannot be disintegrated into smaller molecules

through hydrolysis. Nonsaponifiable lipids include cholesterol, prostaglandins,
etc.

• Saponifiable lipids

A saponifiable lipid comprises one or more ester groups, enabling it to

undergo hydrolysis in the presence of a base, acid, or enzymes, including waxes,
triglycerides, sphingolipids and phospholipids.

Further, these categories can be divided into non-polar and polar lipids.

• Nonpolar lipids, namely triglycerides, are utilized as fuel and to store energy.
• Polar lipids, that could form a barrier with an external water environment,
are utilized in membranes. Polar lipids comprise sphingolipids and
glycerophospholipids.

Types of Lipids

Within these two major classes of lipids, there are numerous specific types of
lipids important to live, including fatty acids, triglycerides, glycerophospholipids,

19 | Page
sphingolipids and steroids. These are broadly classified as simple lipids and complex
lipids.

A. Simple Lipids

Esters of fatty acids with various alcohols.

1. Fats: Esters of fatty acids with glycerol. Oils are fats in the liquid state. They
are the most abundant lipids. The presence of double bonds in the fatty acids
lowers its melting point. At room temperature, lauric acid is solid while
linoleic acid is liquid. The table below shows the structures of common fatty
acids.
Table 2. Structure of Some Common Fatty Acis

Sometimes we prefer to buy a product in solid form rather than in

liquid. Which do you prefer? Spreading margarine on a pandesal or pouring
oil on it? Of course, margarine is more acceptable to consumers when it is
solid because it looks more like butter. However, margarine is made from
vegetable oils that are liquid at room temperature. The oils can be processed
to form solid margarine.

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 Can we consider fats good or bad? It depends. If you eat in moderation,
fats are good sources of body fuel. They are considered good emergency food
and are efficient energy storage system. However, an excess quantity of fats
is not good for the heart. The reason why fats are not good for the heart is
because they tend to clog arteries and overwork the heart. While
carbohydrates are the main source of energy in your body, your system turns
it to fats as a backup energy source when carbohydrates are not available.
Vitamins A, D, E and K cannot function without adequate daily fat intake
since they are fat soluble vitamins. If you don’t meet your daily fat intake or
follow a low-fat diet, absorption of these vitamins may be limited resulting in
impaired functioning.

2. Waxes: Esters of fatty acids with higher molecular weight monohydric alcohols

B. Complex Lipids

Esters of fatty acids containing groups in addition to alcohol and a fatty acid.
1. Phospholipids: These are lipids containing, in addition to fatty acids and
alcohol, a phosphoric acid residue. They frequently have nitrogen-containing
bases and other substituents, e.g., in glycerophospholipids the alcohol is
glycerol and in sphingophospholipids the alcohol is sphingosine.
2. Glycolipids (glycosphingolipids): Lipids containing a fatty acid, sphingosine
and carbohydrate.
3. Other complex lipids: Lipids such as sulfolipids and amino lipids.
Lipoproteins may also be placed in this category.

C. Precursor and Derived Lipids

These include fatty acids, glycerol, steroids, other alcohols, fatty aldehydes,
and ketone bodies, hydrocarbons, lipid-soluble vitamins, and hormones. Because
they are uncharged, acylglycerols (glycerides), cholesterol, and cholesteryl esters are
termed neutral lipids. These compounds are produced by the hydrolysis of simple
and complex lipids.

Some of the different types of lipids are described below in detail.

Fatty Acids

Fatty acids are carboxylic acids

(or organic acid), usually with long
aliphatic tails (long chains), either
unsaturated or saturated.

A. Saturated fatty acids

Lack of carbon-carbon double

Figure 18. Structure of Fatty Acids
bonds indicate that the fatty acid is
saturated. The saturated fatty acids
have higher melting points compared
to unsaturated acids of the
corresponding size due to their
ability to pack their molecules

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 together thus leading to a straight rod-like shape.

B. Unsaturated fatty acids

Unsaturated fatty acid is indicated when a fatty acid has more

than one double bond. “Often, naturally occurring fatty acids possesses
an even number of carbon atoms and are unbranched.” On the other
hand, unsaturated fatty acids contain a cis-double bond(s) which
create a structural kink that disables them to group their molecules in
straight rod-like shape.

Role of Fats

Fats play several major roles in our body. Some of the important roles of fats
are mentioned below:

• Fats in the correct amounts are necessary for the proper functioning of our
body.
• Many fat-soluble vitamins need to be associated with fats in order to be
effectively absorbed by the body.
• They also provide insulation to the body.
• They are an efficient way to store energy for longer periods.

Waxes
Waxes are “esters” (an
organic compound made by
replacing the hydrogen with
acid by an alkyl or another
organic group) formed from
long-alcohols and long-chain
carboxylic acids.

Waxes are found almost

everywhere. Fruits and leaves of
many plants possess waxy
Figure 20. Structure of Waxes coatings, that can safeguard
them from small predators and
dehydration.

Fur of a few animals and the feathers of birds possess same coatings
serving as water repellants.

Carnauba wax is known for its water resistance and toughness

(significant for car wax).

Phospholipids

Membranes are primarily composed of phospholipids that are

Phosphoacylglycerols.

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 Triacylglycerols and
phosphoacylglycerols are the same,
but, the terminal OH group of the
phosphoacylglycerol is esterified with
phosphoric acid in place of fatty acid
which results in the formation of
phosphatidic acid. The name
phospholipid is derived from the fact
that phosphoacylglycerols are lipids
containing a phosphate group.
Figure 20. Structure of
Phospholipids

Steroids
Our bodies possess chemical
messengers known as hormones, that are
basically organic compounds synthesized in
glands and transported by the bloodstream
to various tissues in order to trigger or
hinder the desired process.

Steroids are a kind of hormone that is

typically recognized by their tetracyclic
Figure 21. Structure of Steroids skeleton, composed of three fused six-
membered and one five-membered ring, as
seen above.

Cholesterol

Cholesterol is a wax-like
substance, found only in animal source
foods. Triglycerides, LDL, HDL, VLDL
are different types of cholesterol
found in the blood cells.

Cholesterol is an important lipid

found in the cell membrane. It is a
sterol, which means that cholesterol is
Figure 20. Structure of a combination of steroid and alcohol. In
Cholesterol the human body, cholesterol is
synthesized in the liver.

These compounds are biosynthesized by all living cells and

are essential for the structural component of the cell membrane. In the
cell membrane, the steroid ring structure of cholesterol provides a rigid
hydrophobic structure that helps boost the rigidity of the cell membrane.
Without cholesterol, the cell membrane would be too fluid.

It is an important component of cell membranes and is also the basis

for the synthesis of other steroids, including the sex hormones estradiol
and testosterone, as well as other steroids such as cortisone and vitamin
D.

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 What’s More

Copy and fill in the concept map below. Choose your answers from the
box.

1. Define nucleic acids.

2. Illustrate structure of nucleotides.
3. List functions of nucleotides.

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 . What’s New

Matching Type: Match the first half of the sentences with the second half. Write
only the letters in your answer sheet.

1. Two examples of nucleic acids are a. carbohydrates, lipids, proteins,

2. All living things have nucleic acids, and nucleic acids.
so when you eat them you also b. the structure and functions of our
consume body.
3. We find the DNA in the c. their DNA.
4. Nucleic acids contain genetic d. DNA and RNA.
information that gives e. are made of very small parts which
5. The information contained we call monomers, they are like
in nucleic acids is used for building blocks
6. The building blocks (monomers) f. instructions for the activities of
that made nucleic acids are called of our cells.
7. The four organic biomolecules are: g. nucleus of cells.
8. Monomers: the substances that we h. nucleotide.
obtain with food ….

What is It

NUCLEIC ACIDS

Nucleic acids are molecules that code for

Figure 21. Chemical
Structure of a nucleotide
hereditary traits by controlling the production of
protein. Like proteins, nucleic acids are long
chain of polymers consisting of simpler units or
monomers. The monomers of nucleic acids are
NUCLEOTIDES. A nucleotide is an organic
molecule that is the building block of DNA and
RNA. They also have functions related to cell
signaling, metabolism, and enzyme reactions.
They are made up of three parts: a five carbon
sugar (pentose), a phosphate group, and a
ring-shaped base containing nitrogen.

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Parts of a Nucleotide

1. Nitrogenous Base. Purines and pyrimidines are the two categories of

nitrogenous bases. Adenine and guanine are purines. Cytosine, thymine, and
uracil are pyrimidines. In DNA, the bases are adenine (A), thymine (T), guanine
(G), and cytosine (C). In RNA, the bases are adenine, guanine, uracil, and
cytosine.

2. Pentose Sugar. In DNA,

the sugar is 2'-deoxyribose.
In RNA, the sugar is ribose.
Both ribose and deoxyribose
are 5-carbon sugars. The
carbons are numbered
sequentially, to help keep
track of where groups are
attached. The only
difference between them is
that 2'-deoxyribose has one Figure 23. Chemical Structure of Pentose
less oxygen atom attached Sugars
to the second carbon.
3. Phosphate Group. A single phosphate group is PO43-. The phosphorus
atom is the central atom. One atom of oxygen is connected to the 5-carbon in
the sugar and to the phosphorus atom. When phosphate groups link together
to form chains, as in ATP (adenosine triphosphate), the link looks like O-P-O-
P-O-P-O, with two additional oxygen atoms attached to each phosphorus, one
on either side of the atom.

Functions of Nucleic Acids

Broadly speaking, DNA stores information, while RNA transfers information.

You might thus think of DNA as a computer hard drive or set of files, and RNA as
a flash drive or jump drive.
RNA can serve as a messenger to build proteins using information coded by
DNA, migrating from the nucleus where DNA "lives" to other parts of the cell to
carry this out. This is, fittingly, mRNA (m stands for "messenger"). A different kind
of RNA, transfer RNA (tRNA) helps in the assembly process of proteins from amino
acids, and ribosomal RNA (rRNA) makes up most of the organelles called
ribosomes, which also participate in protein synthesis.
Many single-stranded RNA molecules form three-dimensional structures
that include weak hydrogen bonds between nucleotides. As with proteins, the three-
dimensional structure of an RNA molecule specifies a unique function in cells,
including the degradation of enzymes.

26 | Page
 Type of Nucleic Acids

1. Deoxyribonucleic Acid (DNA)

DNA is the chemical name for the
molecule that carries genetic
instructions in all living things. The
DNA molecule consists of two strands
that wind around one another to form a
shape known as a double helix. Each
strand has a backbone made of
alternating sugar (deoxyribose) and
phosphate groups. Attached to each
sugar is one of four bases--adenine (A),
Figure 24. DNA and RNA Structure cytosine (C), guanine (G), and
thymine (T). The two strands are held
together by bonds between the bases; adenine bonds with thymine, and cytosine
bonds with guanine. The sequence of the bases along the backbones serves as
instructions for assembling protein and RNA molecules.
DNA, or deoxyribonucleic acid, is the central information storage system of
most animals and plants, and even some viruses. The name comes from its
structure, which is a sugar and phosphate backbone which have bases sticking out
from it--so-called bases. So that "deoxyribose" refers to the sugar and the nucleic
acid refers to the phosphate and the bases.
DNA is organized structurally into chromosomes and then wound around
nucleosomes as part of those chromosomes. Functionally, it's organized into genes,
of which are pieces of DNA, which lead to observable traits. And those traits come
not from the DNA itself, but actually from the RNA that is made from the DNA, or
most commonly of proteins that are made from the RNA which is made from the DNA.
So, the central dogma so-called of molecular biology, is that genes, which are made
of DNA, are made into messenger RNAs, which are then made into proteins. But for
the most part, the observable traits of eye color or height or one thing or another of
individuals come from individual proteins.

2. Ribonucleic Acid
Ribonucleic acid (RNA) is a molecule similar to DNA. Unlike DNA, RNA is
single-stranded. An RNA strand has a backbone made of alternating sugar (ribose)
and phosphate groups. Attached to each sugar is one of four bases--adenine (A),
uracil (U), cytosine (C), or guanine (G). Different types of RNA exist in the cell:
messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA).
RNA, or ribonucleic acid, is a nucleic acid that is similar in structure to DNA
but different in subtle ways. The cell uses RNA for a number of different tasks, one
of which is called messenger RNA, or mRNA. And that is the nucleic acid information
molecule that transfers information from the genome into proteins by translation.
Another form of RNA is tRNA, or transfer RNA, and these are non-protein encoding
RNA molecules that physically carry amino acids to the translation site that allows
them to be assembled into chains of proteins in the process of translation

27 | Page
 What’s More

Read each term or phrase in the left hand column of the following table.
If the term or phrase applies to DNA, place a check mark in the column
labeled DNA. If it applies to RNA, place a check mark in the column
labeled RNA. If it applies to both nucleic acids, place a check mark in
both columns. Copy the table and answer in your answer sheet.
Term / Phrase Both DNA RNA
Deoxyribose
Ribose
Single stranded
Double stranded
Thymine
Uracil
Nucleotides
Cytosine
Guanine
Adenine
Double Helix
Nitrogen base
Sugar
Phosphate
Nucleic Acids

What I Have Learned

Copy and complete the following chart in your answer sheet.

Food
Biomolecules Monomer Functions Examples
Source
Monosaccharide

• Energy storage
• Membranes’
component
• Steroids
Proteins • Insulin
• Actin and
Myosin

Nucleotides
None

28 | Page
 What I Can Do

FOOD LABELS

Examine the following nutrition labels and answer the questions in your answer
sheet.

1. How many calories would you take in if you ate the whole box of crackers in one
sitting?
2. If you ate 2 servings of crackers, how many grams of carbohydrates would you
get?
3. If each gram of carbohydrates provides 4 calories, how many calories would you
take in by eating 2 servings of crackers?
4. If fat provides 9 calories per gram, how many calories would you get by eating 2
servings?
5. If you were to eat the entire can of soup, how much sodium would you
consume?
6. If the recommended amount of sodium for someone with high blood pressure is
1500 mg/day, how much more than the recommended amount is present in
this entire can?
7. How many servings of soup would I need to consume 20% of my daily
requirement of fiber?
8. How many calories would that be?

29 | Page
30 | Page
31 | Page
References and Links

Printed Materials:

Lehninger, A. L., Nelson, D. L., & Cox, M. M. (2000). Lehninger principles of

biochemistry. New York: Worth Publishers.
Smith, C. M., Marks, A. D., Lieberman, M. A., Marks, D. B., & Marks, D. B.
(2005). Marks’ basic medical biochemistry: A clinical approach. Philadelphia:
Lippincott Williams & Wilkins.
Rodwell, V. W., Botham, K. M., Kennelly, P. J., Weil, P. A., & Bender, D. A.
(2015). Harper’s illustrated biochemistry (30th ed.). New York, N.Y.: McGraw-
Hill Education LLC.
John W. Pelley, Edward F. Goljan (2011). Biochemistry. Third edition. Philadelphia:
USA.

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structures/proteins/levels-of-protein-structure-primary/levels-of-protein-structure-
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https://www.biologyexams4u.com/2012/09/amino-acids
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