Physical Science SHS 8.1 Proteins

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Lesson 8.

1
The Structures, Properties, and
Functions of Biomolecules

Proteins
determine the building
1 blocks of proteins;

Objectives know how these


biomolecules are formed
At the end 2 from these building blocks;
of this and
lesson, you
should be explain how the structures
able to: of biomolecules determine
3 their properties and
functions.
What are covalent bonds?
• Covalent bonding is a type of chemical bond formed
by the sharing of electrons between atoms.
• The types of covalent bonds are as follows:
i. In a single bond, a pair of electrons is shared between
two atoms.
ii. In a double bond, two electron pairs are shared
between two atoms.
iii. In a triple bond, three pairs of electrons are shared.
Learn about it!

What are functional groups?

a. A functional group is an atom (or a group of atoms)


that are responsible for the behavior and different
chemical properties of a molecule.
Learn about it!
The following diagram shows the functional groups:
Learn about it!
Proteins were once thought of as biomolecules
representing the “beginning” of life.

The word protein comes from the Greek word


proteious which means first.
Learn about it!

Building Blocks of Proteins


● Amino acids are a protein’s
building blocks.

● They contain two functional


groups: the basic amino
group and the acidic
carboxylic group.
Basic structure of an amino acid
Learn about it!
Properties
● Proteins are chiral molecules.
- Don’t have a plane a plane of
symmetry or a center of symmetry
● In aqueous solutions, an amino acid
usually exists as a dipolar ion called
zwitterion.
○ This usually occur at a physiologically
neutral pH level.
A zwitterion of the amino acid
lysine showing its dipolar
nature
Learn about it!

Essential Amino Acids


● There are 20 amino acids
commonly found in proteins.

● They differ from each other


due to their different R
groups or side chains.

Essential amino acids


Essential Amino
Learn about it! Acids
Essential
Learn Amino
about it!Acids
1. Leucine
Leucine is a type of amino acid that stimulates insulin secretion
and helps body tissues regenerate after injury. It is available in
milk, peanuts, rice, beef, fish, almonds, and many other foods.
2. Tryptophan
Tryptophan is one of the best-known amino acids, and is used to
synthesize both melatonin and serotonin, two important
neurotransmitters in the nervous system. Thus, their presence
contributes to make us experience states of relaxation and sleep.
It is found in foods such as chickpeas, dates, oats, eggs, milk,
and other foods typical of a balanced diet.
Essential
Learn Amino
about it!Acids
3. Histidine
Histidine is an amino acid that is involved in digestion processes that
take place mostly in the stomach.
4. Valina
Valine regulates the use and secretion of other amino acids, and is
also a source of energy for the body’s muscles. It is present in many
sweet fruits, such as bananas or red fruits.
5. Lysine
This is another essential amino acid that intervenes in the
maintenance of connective tissues of the skin in general. Above all, it
contributes to the formation of collagen networks that pass through
the skin
Essential
Learn Amino
about it!Acids
6. Phenylalanine
Phenylalanine has the function of regulating physiological
processes such as the appearance of appetite and the sensation
of pain. It is usually present in good amounts in protein-rich
foods, such as meats or eggs.

7. Isoleucine
The isoleucine is basic to be able to create proteins that serve for
the body to form and develop. We can find this amino acid in
cheese, milk, chicken meat, eggs and soy protein.
Essential
Learn Amino
about it!Acids
8. Threonine
Threonine is another amino acid involved in the formation of collagen
and the proper functioning of digestive processes. It is present in
chicken, red meat, lentils, and certain types of cheese.
9. Methionine
Methionine can burn accumulated fat. It is present in eggs, fish and
cereals, among other foods.
10. Arginine
This is another element of the amino acid table that intervenes in the
regeneration of damaged organic tissues and in healing. On the other
hand, it stimulates the secretion of glucagon and insulin, and is a
precursor of one of the most important neurotransmitters: GABA.
Non-Essential
Learn aboutAmino
it! Acids
This list of types of amino acids shows those that are already
synthesized by the human body.
1. Alanine
Alanine allows the generation of antibodies and muscle growth. It
is important to face the challenges of everyday life.
2. Glycine
Glycine is one of the most important amino acids, because on the
one hand it is a neurotransmitter used for communication
between neurons, and also allows the existence of hemoglobin
(red blood cells), because it is part of its cellular architecture.
Non-Essential
Learn aboutAmino
it! Acids
3. Tyrosine
Tyrosine is a precursor of growth hormone and thyroxine, another
hormone, in addition to other substances that act as neurotransmitters as
important as serotonin or adrenaline.
4. Proline
Proline has a very important role in the development of cartilage, so it is
very important in terms of the structure and basic functioning of body
movement.
5. Cysteine
Cysteine is an antioxidant, and regulates various functions of cell
maintenance. Although it is a non-essential amino acid, certain population
groups may have a deficit of it, and in these cases it is advisable to obtain
it from foods such as chicken, eggs, cabbage or broccoli.
Non-Essential
Learn aboutAmino
it! Acids
6. Glutamine
This amino acid is a precursor of glutamate and GABA, and
intervenes in processes of regulation of digestion and the amount
of sugar in the blood.
7. Asparagine
Asparagine participates in many processes linked to the nervous
system, especially in the consolidation of memories by neural
networks.
Non-Essential
Learn aboutAmino
it! Acids
8. Serine
This amino acid allows the myelin sheaths to develop well. These are
layers of myelin that cover the axons of neurons and make the nerve
impulse go faster. It also strengthens the immune system and contributes
to muscle growth.
9. Aspartic acid
Aspartic acid has many functions. Among them is its involvement in the
immune system, and its involvement in states of excitement and alertness
to react quickly to what happens in the environment.
10. Glutamic acid
This is one of the most versatile types of amino acids, and while it affects
many biological processes, the one that stands out most is the immune
system-strengthening factor.
Learn about it!

Essential Amino Acids


● Polypeptides and proteins
are formed when amino
acids are linked together by a
peptide bond.

A peptide bond between two amino


acids.
Learn about it!

Essential Amino Acids


● Polypeptides are formed
from a large number of
amino acids.

● Proteins, on the other hand,


are composed of one or
more polypeptide chain.
A peptide bond between two amino
acids.
Learn about it!

Levels of Protein Organization


● Proteins have different
shapes and sizes.

● How they achieve their


individual structures
depends on four different
levels of protein
organization.
The different levels of protein structure
Learn about it!

Levels of Protein Organization


Primary Structure

● This refers to the amino acid


sequence that comprises a
polypeptide chain.

● The properties of the amino


acids determine the The primary structure shows the
properties of the sequence. amino acids that are linked together
by peptide bonds
Learn about it!

Levels of Protein Organization


Secondary Structure

● This refers to the localized


folding of protein chains.
○ This is due to the
hydrogen bonding
between the amino and
carboxyl groups of
Secondary structure of proteins include
neighboring amino acids. the alpha helix and beta sheets
Learn about it!

Levels of Protein Organization


Secondary Structure

● An α-helix is a right-handed coil stabilized by the hydrogen


bonds between the amino group of one amino acid and
carbonyl group of another amino acid.

● A β-pleated sheet has hydrogen bonds that are between


adjacent amino acids resulting in extended rather than
coiled polypeptide chains.
Learn about it!

Levels of Protein Organization


Tertiary Structure

● This level of organization describes the three-dimensional


structure of the protein.
○ This structure refers to the positioning of the protein’s
atoms and side chains.
○ Tertiary structure can either be fibrous (long parallel
coils) or globular (compact and almost spherical).
Learn about it!

Levels of Protein Organization

Tertiary Structures. Collagen (left) is an example of a fibrous protein,


while myoglobin (right) is an example of a globular protein.
Learn about it!

Levels of Protein Organization


Quaternary Structure

● The quaternary structure


describes how proteins
come together to form
large aggregates.

Hemoglobin is a protein with


quaternary structure consisting of
two alpha and two beta chains.
Learn about it!
Learn about it!

Functions of Proteins
● Proteins perform the function of transporting different
molecules through the different parts of organism.
- An example of an important group of transport proteins
are lipoproteins, which are used for transporting cholesterol.
● Enzymes are biological catalysts that act to make the
reaction take place more rapidly.
- An example of an enzyme is chymotrypsin, an enzyme of
the digestive system for breaking down proteins.
Learn about it!

Functions of Proteins
● Structure: There are some proteins that organisms and
cells use for mechanical support. Keratin is an example of
a structural protein.

● Movement: The body uses proteins like actin and myosin


to allow muscles to contract and generate movement.
Learn about it!
Functions of Proteins
● Some of the most notable proteins used for immunity
are the antibodies.
○ Antibodies are proteins produced by the cells of the
immune system, and are used for defence against
pathogens.
Receptor proteins are used for many purposes, most
of which involve the reception of signals in the form of
other molecules.
i. Multiple receptor proteins are found in the cell
membrane.
Key Points

Amino acids are the building blocks of proteins. They


1 contain the amino group and the carboxylic group.

There are 20 amino acids commonly found in


2 proteins. They differ from each other due to their
different R groups or side chains.

How proteins achieve their individual structures


3 depend on the different levels of protein
organization.
Check Your Understanding
Identify the terms being described by the statements below.
1. These are the building blocks of proteins.
2. It is a term used to refer to amino acids where both
carboxylic acid and amino groups are charged.
3. This dictates the main difference between the essential
amino acids.
4. These are the bonds that hold amino acids together.
5. It is one of the secondary structures of proteins where
amino acids are stabilized by hydrogen bonds in a coil-like
structure.
Check Your Understanding

4. These are the bonds that hold amino acids together.


5. It is one of the secondary structures of proteins where
amino acids are stabilized by hydrogen bonds in a coil-like
structure.
6. These are a type of proteins that have long coils aligned
in an almost parallel fashion to form water-insoluble fibers.
7. These are a type of proteins that are compact and
Check Your Understanding

8. It is a level of protein structural organization that


describes how proteins come together to form large
aggregates.

9. These proteins are known to transport cholesterol.

10. These are proteins produced by the cells of the immune


system and are used for defense against pathogens.
Check Your Understanding
Identify the terms being described by the statements below.
1. These are the building blocks of proteins. amino acids
2. It is a term used to refer to amino acids where both
carboxylic acid and amino groups are charged.
Zwitterions
3. This dictates the main difference between the essential
amino acids. R-group
4. These are the bonds that hold amino acids together.
peptide bonds
5. It is one of the secondary structures of proteins where
amino acids are stabilized by hydrogen bonds in a coil-like
Check Your Understanding

4. These are the bonds that hold amino acids together.


peptide bonds
5. It is one of the secondary structures of proteins where
amino acids are stabilized by hydrogen bonds in a coil-like
structure. α-helixes
6. These are a type of proteins that have long coils aligned
in an almost parallel fashion to form water-insoluble fibers.
fibrous proteins
7. These are a type of proteins that are compact and
roughly spherical in shape. globular proteins
Check Your Understanding

8. It is a level of protein structural organization that


describes how proteins come together to form large
aggregates. quaternary
9. These proteins are known to transport cholesterol.
lipoproteins 10. These are proteins produced by the cells
of the immune system and are used for defense against
pathogens. antibodies
Check Your Understanding

Identify the terms being described by the statements below.

1. These are the building blocks of proteins.


2. It is a term used to refer to amino acids where both carboxylic
acid and amino groups are charged.
3. This dictates the main difference between the essential amino
acids.
4. These are the bonds that hold amino acids together.
5. It is one of the secondary structures of a proteins where
amino acids are stabilized by hydrogen bonds in a coil-like
structure.
Challenge Yourself

Describe the primary and secondary structures


of a protein. What is the difference between the
two structural organizations of proteins?
Bibliography

Boyer, Rodney. 2006. Concepts in Biochemistry Third Edition. Danvers: John Wiley & Sons Inc.

Brown, T.L. et al. 2003. Chemistry, The Central Science. New Jersey: Pearson Education, Inc.

Collins, Caylee. BUILDING AND RUNNING A HOMEMADE AGAROSE GEL


ELECTROPHORESIS.https://www.instructables.com/id/Building-and-Running-a-Homemade-Agarose-
Gel-Electr/

McMurry, J. 2008. Organic Chemistry. Brooks Cole/CENGAGE Learning.

Nelson, D. L. and Cox, M.M. 2005. Lehninger Principles of Biochemistry. New York: W.H. Freeman and
Company.
Nature Education. “Protein Structure”. Accessed June 4, 2017.
https://www.nature.com/scitable/topicpage/protein-structure-14122136.

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