Republic of the Philippines

Department of Education
REGION XII
DIVISION OF SULTAN KUDARAT
Bagumbayan Municipality High Schools

LEARNING ACTIVITY SHEET

Name: Grade & Section:

Subject: SCIENCE 10 Teacher:
Quarter: 4 Week: 4 LAS: 1 MELC Code: S10MT-IVc-d-22 Score:

Biomolecules: Proteins
Learning Objectives:
At the end of the doing the Learning Activity Sheet, the learners will be able to:
1. describe proteins;
2. recognize amino acids as monomers of proteins;
3. identify the four levels of structures of proteins; and
4. identify examples of proteins in the body and their functions.

A. What’s New?
Biomolecules are any of numerous substances that are produced by cells and living organisms. They
are very important to life. They have a wide range of sizes and structures and perform a vast array of
functions. The four major types of biomolecules are carbohydrates, lipids, nucleic acids, and proteins.
Combined, these molecules make up the majority of a cell’s mass. Biological macromolecules are organic,
meaning that they contain carbon. Proteins and nucleic acids and some derivatives of carbohydrates and
lipids contain nitrogen N.

B. What Is It?
Proteins are very important to our
nutrition since they are common in our body
and can be taken from eggs, milk and meat
sources or the grow foods. They have diverse
range of functions like being structural,
regulatory, contractile, or protective; they may
serve in transport, storage, or membranes; or
they may be toxins or enzymes. Each cell in a
living system may contain thousands of
different proteins, each with a unique function.
Their structures, like their functions, vary
greatly. They are all, however, polymers of
amino acids, arranged in a linear sequence.
Figure 1: Samples of proteins in the body and their functions
Image Source: https://alevelbiology.co.uk/notes/functions-of-proteins/

Amino acids make up each protein. Proteins are made by a particular sequence of amino acids. There
are 20 amino acids in the body, only 11 can be made by our body and 9 of them should be taken from the
food we eat.

Figure 2: 20 types of amino acids Figure 3: A specific protein is made up of a specific

order of amino acids
Images Taken from https://www.genome.gov/genetics-glossary/Amino-Acids

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Structure of Amino Acids. 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. Every amino acid also has another atom or group of atoms
bonded to the central atom known as the R group (Figure 4).

Figure 4. Structure of Amino Acid

Image Source: ttps://courses.lumenlearning.com/suny- wmopen-biology1/chapter/proteins/

Peptide Bond, Peptides, and Polypeptides. Each amino acid is attached to another amino acid by a
covalent bond, known as a peptide bond, which is formed by a dehydration reaction. The carboxyl group
of one amino acid and the amino group of the incoming amino acid combine, releasing a molecule of
water. The products formed by such linkages are called peptides. Longer chains are called polypeptides
and chains of 50 or more amino acids are known as proteins.

Figure 5. Amino Acid 1 links with amino acid 2 through Figure 6. An amino acid, a polypeptide, and a protein
peptide bond producing a peptide and a water molecule Image Source: https://slideplayer.com/slide/16140209/
Image Source: https://byjus.com/jee/peptide-bond/

Protein Structure. The shape of a protein is critical to its function. There are four levels of protein
structure to understand its shape and characteristics: primary, secondary, tertiary, and quarternary
structures (Figure 7).

Primary structure is the unique sequence and

number of amino acids in a polypeptide chain.

Secondary structure is the folding, coiling, or

twisting of the protein resulting from interactions
between the non-R group portions of amino acids.
The most common are the alpha (α)-helix and beta
(β)-pleated sheet structures. Both structures are
held in shape by hydrogen bonds. 

Tertiary structure is a unique three-dimensional

structure of a polypeptide caused by chemical
interactions between various amino acids and
regions of the polypeptide. It looks like a coil
folded on its sides.

Quarternary structure involves the clustering of

several individual polypeptides into final specific
shape. Weak interactions between the subunits
help to stabilize the overall structure. For example,
hemoglobin is a combination of four polypeptide
subunits.
Figure 7. Structures of a Protein
Image Source: https://courses.lumenlearning.com/biology1/chapter/biological-molecules/

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 Enzymes, which are produced by living cells, are catalysts in biochemical reactions (like digestion)
and are usually complex or conjugated proteins. Each enzyme is specific for the substrate (a reactant that
binds to an enzyme) it acts on. The enzyme may help in breakdown, rearrangement, or synthesis
reactions. Enzymes that break down their substrates are called catabolic enzymes, enzymes that build
more complex molecules from their substrates are called anabolic enzymes, and enzymes that affect the
rate of reaction are called catalytic enzymes. An example of an enzyme is salivary amylase, which
hydrolyzes its substrate amylose, a component of starch.

Hormones are chemical-signaling molecules, usually small proteins or steroids, secreted by

endocrine cells that act to control or regulate specific physiological processes, including growth,
development, metabolism, and reproduction. For example, insulin is a protein hormone that helps to
regulate the blood glucose level.
C. Learning Activities

I. Multiple Choice. Write the letter of your answer on the space provided before the number.

_____ 1. Which is not a component of a protein?

a. Carbon
b. Hydrogen
c. Magnesium
d. Oxygen
_____2. How many different kinds of amino acids are in our bodies?
a. 4
b. 9
c. 11
d. 20
_____3. All amino acids are produced in our body.
a. True
b. False
c. I don’t know
d. Maybe
_____4. Proteins are made up of
a. a short chain of amino acids
b. weak peptide bonds
c. a very long chain of amino acids
d. two peptides called dipeptide
_____5. Why proteins are important?
a. Proteins are essential for survival.
b. Proteins have diverse functions in the body.
c. Every cell in the body uses proteins.
d. All of the above.
_____6. Antibodies are examples of what type of proteins?
a. Contractile
b. Regulatory
c. Structural
d. Protective
_____7. Proteins that are used as catalysts to break down substances in our body are called?
a. Enzymes
b. Hormones
c. Fluids
d. Waste
____8. A protein structure due to coiling or twisting of a protein
a. Primary
b. Secondary
c. Tertiary
d. Quarternary

II. The figure below shows a dehydration reaction in the formation of a dipeptide. Locate and label the
(a) Peptide Bond and (b) Water molecule in the figure.

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Answer Key for Part C. Learning Activities

I. Multiple Choice. 1 point each.

1. c
2. d
3. b
4. c
5. d
6. d
7. a
8. b

II. 1 point each

Peptide Bond

Water Molecule

D. References
Acosta, H.D,. et al. Science-Grade 10 Learner’s Material First Edition 2015, pp 462-469 Department of
Education. Printed by REX Book Store, Inc

Rogers, Kara. Biomolecule. Brittanica. Retrieved from https://www.britannica.com/science/ biomolecule

https://courses.lumenlearning.com/biology1/chapter/biological-molecules/

https://courses.lumenlearning.com/suny-wmopen-biology1/chapter/proteins/

LAS Development Team

Writer: Ian Neil M. Gardose, T-II (Busok NHS)

Editor: CerilaT. Lelim, MT-I
Evaluator: Rene P. Canto, Principal-I
Illustrator:
Municipality: Municipality of Bagumbayan

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