MODULE IN SCIENCE GRADE 10

Biochemistry Roxane O. Dolim

Practice Teacher

PROTEIN
Think about the food you eat every day. Different
LESSON types of food give you different nutrients for energy,
growth, and repair. These were introduced to you when

1 you were in the elementary grades.

In this quarter, you will learn more about
compounds that are essential to life. These compounds
belclasses of biomolecules: carbohydrates, lipids, proteins,
belong to four main
and nucleic acids. Carbohydrates and lipids are generally made up of
carbon, hydrogen, and oxygen. Proteins and nucleic acids and some
derivatives of carbohydrates and lipids also contain nitrogen.
In this module, we will be focusing first on protein, its structure, and
its other aspects.
At the end of this module, you will be able to:
1. define what is a protein;
2. identify protein’s functions and importance; and
3. describe the level of protein’s structure and its composition.

Proteins are the most abundant biological macromolecules, occurring

in all cells and all parts of cells. Amino acids are the building blocks of
proteins. All proteins, whether from the most ancient lines of bacteria or
the most complex forms of life, are constructed from the same set of 20
amino acids.
What is most remarkable is that cells can produce proteins with
strikingly different properties and activities by joining the same 20 amino
acids in many different combinations and sequences. From these building
blocks, different organisms can make such widely diverse products as
enzymes, hormones, antibodies, transporters, muscle fibers, the lens
protein of the eye, feathers, spider webs, rhinoceros’ horn, milk proteins,
antibiotics, mushroom poisons, and other substances having distinct
biological activities. While proteins contain only L-а-amino acids,
microorganisms elaborate peptides that contain both D- and L-а-amino
acids.
 PRETEST

Multiple choice. Answer the following questions and write your answer on a
piece of paper.

1. Which of the following is NOT a major source of protein

a. fish
b. milk
c. egg
d. meat

2. Which is a correct pair of an example of protein and its function?

a. enzymes: speed up reactions in the body and eventually use up in
the process.
b. collagen: provides strength and flexibility to connective tissues.
c. actin and myosin: supplies amino acids to baby mammals
d. hemoglobin: helps regulate blood sugar levels

3. Which element does NOT make up a protein?

a. Hydrogen
b. Oxygen
c. Carbon
d. None of this

4. Protein is made of how many different amino acids are linked in a

different order?
a. 15
b. 18
c. 20
d. 21

5. What is protein’s main function?

a. supply oxygen throughout the body.
b. helps the growth and maintenance of cells.
c. the framework of the body
d. supply nutrients and the removal of waste in the body.
 DISCUSSION
Proteins
EACH INDIVIDUAL IS
Proteins are made up of the elements info
UNIQUE TO ONE
carbon, hydrogen, oxygen, nitrogen, and bits
ANOTHER.
sulfur. Egg white, fish, meat, and cheese are
foods rich in proteins. Proteins are found in Protein is a polymer.
all living cells. They are the second most Polypeptide is another name for
common molecules found in the human body protein.
(after water) and makeup about 10% to 20%
of the mass of a cell. When a person eats Protein exists in every single cell in
protein-rich foods, the digestive system our body. Without protein, life
breaks the long protein chains into simpler would not exist.
substances called amino acids.

Amino acids are the building blocks of proteins.

Of the 20 amino acids found in human protein, only 11 can be
synthesized by the body, and 9 have to be supplied by the foods we eat.
These 9 amino acids are also called essential amino acids. Adults only need
to obtain eight of them: valine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, and tryptophan. The ninth amino acid - histidine
- is only essential for infants.
Your body doesn’t store amino
acids, so it needs a regular daily supply
of these essential building blocks.
Nonessential is a slightly misleading
label because these amino acids fill
essential roles, but since they’re
synthesized by your body, they’re not an
essential part of your diet. When you’re
sick or under significant stress, your
body may not be able to produce enough
of these amino acids to meet your
needs.
Amino acids are linked together by
‘amide groups’ called peptide bonds.
During protein synthesis, the carboxyl
group of amino acids at the end of the growing polypeptide chain reacts
with the amino group of incoming amino acids, releasing a molecule of
water. The resulting bond between the amino acids is a peptide bond.
An amino acid contains both a carboxylic group and an amino group.
Amino acids that have an amino group bonded directly to the alpha-carbon
are referred to as alpha-amino acids. Every alpha-amino acid has a carbon
atom, called an alpha carbon, Cα; bonded to a carboxylic acid, –COOH
group; an amino, –NH2 group; a hydrogen atom; and an R group that is
unique for every amino acid

Classification of Amino Acid

All the amino acids except proline have both free amino and free
carboxyl groups. The classifications of amino acids are based on the polarity
of the side chains. Thus, the structures are grouped into the following
categories: (1) nonpolar or hydrophobic amino acids, (2) neutral
(uncharged) but polar amino acids, (3) acidic amino acids (which have a
net negative charge at pH 7.0),
and (4) basic amino acids
(which have a net positive
charge at neutral pH).
Nonpolar Amino Acids.
The nonpolar amino acids
include all those with alkyl
chain R groups (alanine, valine,
leucine, and isoleucine), as
well as proline (with its unusual
cyclic structure), methionine
(one of the two sulfur-
containing amino acids), and
two aromatic amino acids, phenylalanine and tryptophan. Tryptophan is
sometimes considered a borderline member of this group because it can
interact favorably with water via the N–H moiety of the indole ring. Proline,
strictly speaking, is not an amino acid but rather an α-amino acid.
Polar, Uncharged Amino Acids. The polar, uncharged amino acids
except for glycine contain R groups that can form hydrogen bonds with
water. Thus, these amino acids are usually more soluble in water than
nonpolar amino acids. Tyrosine displays the lowest solubility in water of the
20 common amino acids. Glycine, the simplest amino acid, has only single
hydrogen for an R group, and this hydrogen is not a good hydrogen bond
former. Glycine’s solubility properties are mainly influenced by its polar
amino and carboxyl groups, and thus glycine is best considered a member
of the polar, uncharged group. It should be noted that tyrosine has
significant nonpolar characteristics due to its aromatic ring and could
arguably be placed in the nonpolar group.
Acidic Amino Acids. There are two acidic amino acids – aspartic acid
and glutamic acid – whose R groups contain a carboxyl group. Aspartic acid
and glutamic acid thus have a net negative charge at pH 7. Many proteins
that bind metal ions for structural or functional purposes possess metal-
binding sites containing one or more aspartate and glutamate side chains.
Basic Amino Acids. Three of the common amino acids have side
chains with net positive charges at neutral pH: histidine, arginine, and
lysine. The ionized group of histidine is an imidazolium, arginine is a
guanidinium, and lysine contains a protonated alkylamino group. Arginine
and lysine side chains, which are protonated under physiological conditions,
participate in electrostatic interactions in proteins.

BASIC AMINO ACIDS

Three of the common amino acids have side chains with net positive
charges at neutral pH: histidine, arginine, and lysine. The ionized group of
histidine is an imidazolium, arginine is a guanidinium, and lysine contains
a protonated alkylamino group. Arginine and lysine side chains, which are
protonated under physiological conditions, participate in electrostatic
interactions in proteins.
Functions of Proteins

1. Enzymes: Enzymes mostly carry out numerous chemical reactions

which take place within a cell. They also help in regenerating and
creating DNA molecules and carrying out complex processes.
2. Hormones: Proteins are involved in the creation of various types of
hormones that help in balancing the components of the body. For
example, hormones like insulin help in regulating blood sugar and
secretin. It is also involved in the digestion process and the formation
of digestive juices.
3. Antibody: Antibody is also known as an immunoglobulin. It is a type
of protein that is majorly used by the immune system to repair and
heal the body from foreign bacteria. They often work together with
other immune cells to identify and separate the antigens from
increasing until the white blood cells destroy them completely.
4. Energy: Proteins are the major source of energy that helps in the
movements of our body. It is important to have the right amount of
protein to convert it into energy. Protein, when consumed in excess
amounts, gets used to create fat and becomes part of the fat cells.
THE LEVELS OF PROTEIN STRUCTURE
In general, there are two types of protein molecules fibrous proteins and
globular proteins. Fibrous proteins are insoluble and elongated. Globular
proteins are soluble and compact. Fibrous and globular proteins may
comprise one or four types of protein structures and they include primary,
secondary, tertiary, and quaternary structures.
Primary Structure. It is a specific sequence of amino acids. The order of
amino acids bonded together is detected by information stored in genes.
The simplest level of protein structure, the primary structure is simply
the sequence of amino acids in a polypeptide chain. • The hormone insulin
has two polypeptide chains A, and B. The sequence of the A chain and the
sequence of the B chain can be considered as an example of a primary
structure.

Secondary Structure. It is a three-dimensional form of a local segment

of proteins. They are formed by hydrogen bonds between the atoms along
the backbone of the polypeptide chain.
Refers to local folded structures that form within a polypeptide due to
interactions between atoms. • The most common types of secondary
structures are the α helix and the β pleated sheet. Both structures are held
in shape by hydrogen bonds, which form between the carbonyl O of one
amino acid and the amino H of another.

Tertiary Structure. It is determined by R-groups. It is a three-

dimensional shape of a protein. Many numbers of tertiary structures fold to
form Quaternary Structure.
 The tertiary structure is primarily due to interactions between the R
groups of the amino acids that make up the protein. • Important to the
tertiary structure are hydrophobic interactions, in which amino acids with
nonpolar, hydrophobic R groups cluster together on the inside of the
protein, leaving hydrophilic amino acids on the outside to interact with
surrounding water molecules. • Also, Disulfide bonds, covalent linkages
between the sulfur-containing side chains of cysteines, are much stronger
than the other types of bonds.

Quaternary Structure. It is the arrangement of multiple folded protein

subunits in a multi-subunit complex.
When multiple polypeptide chain subunits come together, then the
protein attains its quaternary structure. • An example of a quaternary
structure is hemoglobin. The hemoglobin carries oxygen in the blood and
is made up of four subunits, two each of the α and β types.

ACTIVITY
Complete the jumble words! Each item has a hint for you!
Write your answer on a piece of paper.

1. CYLINGE
the simplest amino acid
2. SNMOOHRE
a function of a protein that helps in balancing the components of
the body.

3. TELPPOYDIEP
another name for protein.

4. TEUQRANRYAR
It is the arrangement of multiple folded protein subunits in a multi-
subunit complex. A protein structure.

5. EPPIEDT OBDN
Amino acids are linked together by ‘amide groups’ called _______.

6. EIRPTON
the second most common molecule found in the human body

7. SYRIETON
displays the lowest solubility in water of the 20 common amino
acids.

8. YEEZNMS
the function of a protein mostly carries out numerous chemical
reactions which take place within a cell.

9. IMOAN IDAC
the building block of proteins.

10. MIYRPRA
The simplest level of protein structure.

RESOURCES

• DepEd Learner’s Material in Science 10 pp. 465-468

• https://byjus.com/biology/proteins/
• BIOLOGICAL SCIENCE (Sixth Edition) by James L. Gould & William T,
Keeton, C & E Publishing, Inc. pp. 58-68.
• https://nios.ac.in/media/documents/dmlt/Biochemistry/Lesson-
04.pdf
• https://www.michigan.gov/documents/explorelabscience/Introducti
on_to_proteins_and_amino_acids_571576_7.pdf
________________________________________________________________

ASSESSMENT
I. IDENTIFICATION. Read and answer the following questions. Write your answer
on a piece of paper.

1. These are the amino acids that you need through your diet because your
body cannot make them.
2. These are the amino acids that are not an essential part of your diet
because they can be synthesized by your body.
3. Refers to local folded structures that form within a polypeptide due to
interactions between atoms.
4-5. Name two elements that made up a protein.

TRUE OR FALSE

6. Proteins are the major source of energy that helps in the movements of
our body.
7. Protein is a polymer.

8. Without protein, life would still exist.

9. Proteins are involved in the creation of various types of hormones that

help in balancing the components of the body.
10. Protein does not exist in every single cell in our body.

II. Enumerate and differentiate the four levels of protein structure. (5pts)