Lesson 5.
Proteins
General Biology 11/2
Science, Technology, Engineering, and Mathematics
Having a source of
protein in our diet is
very important.
Proteins help us grow
faster and stronger.
2
Athletes utilize proteins
more frequently
because their muscles
are prone to tear
during their training
regimen.
3
How would you describe the
structure and functions of
proteins?
4
Learning Competencies
At the end of the lesson, you should be able to do the following:
● Categorize the biological molecules (proteins)
according to their structure and function
(STEM_BIO11/12-Ii-j-15).
5
Learning Objectives
At the end of the lesson, you should be able to do the following:
● Describe the structure and functions of proteins.
● Describe the different classes of proteins.
6
Protein Structure
Amino acid structure
● Amino acids have:
○ Central carbon
○ Amino group
○ Carboxyl group
○ Hydrogen atom
○ R group
The basic structure of an amino acid.
7
Protein Structure
The twenty amino acids in living organisms have different R groups
(highlighted in blue), which give them varying chemical properties in
the cell's physiological conditions. 8
Protein Structure
The twenty amino acids in living organisms have different R groups
(highlighted in blue), which give them varying chemical properties in
the cell's physiological conditions. 9
Protein Structure
The twenty amino acids in living organisms have different R groups
(highlighted in blue), which give them varying chemical properties in
the cell's physiological conditions. 10
Protein Structure
The Classification of Amino Acids Based on their Chemical Nature
Hydrophobic Hydrophilic
Nonpolar Polar Acidic Basic
Glycine Phenylalanine Serine
Alanine Tryptophan Cysteine
Aspartic acid Lysine
Valine Methionine Tyrosine
Glutamic acid Arginine
Leucine Proline Threonine
Histidine
Isoleucine Asparagine
Glutamine
11
Protein Structure
Peptide Bond Formation
● Cells link amino acid
monomers together by
dehydration reactions.
● The bond between
adjacent amino acids is
In the process of a dehydration
called a peptide bond. reaction, one amino acid releases an
H+, and the other releases OH–. Thus,
a water molecule is produced. 12
Levels of Protein Structure
Primary Secondary
Levels of Protein Structure
Tertiary Quaternary
13
Levels of Protein Structure
The primary protein structure refers to the unique sequence
of amino acids. 14
Levels of Protein Structure
Secondary protein structures include the alpha-helices and beta-sheets,
which resulted from amino acid chain coiling or folding. 15
Levels of Protein Structure
Tertiary structures of proteins are formed and maintained by
hydrophobic, hydrophilic, and ionic interactions, as well as by disulfide
bridges. 16
Levels of Protein Structure
Hemoglobin is an example of a protein that can attain a quaternary
structure. It has four polypeptides, wherein each has primary, secondary
and tertiary structures. 17
Protein Structure
Protein Denaturation
● Some conditions can
cause a protein to
unravel and lose its
normal shape.
○ Examples of these
conditions include
The change in the appearance and
pH and temperature. chemical composition of an egg once
cooked is primarily because of protein
denaturation.
18
Why can denatured proteins no
longer perform their normal
functions?
19
Functional Classification of Proteins
Structural Storage Enzymes
Functional Classifications
of Proteins
Transport Messengers Contractile
20
Functional Classification of Proteins
Structural Proteins
The keratin in hair and silk in spider webs are examples of structural
proteins. Keratin can also be found in the horns, claws, hooves, and outer
skin of vertebrates.
21
Functional Classification of Proteins
Enzymes
Enzymes are mostly globular proteins that catalyze reactions. They are very
specific to the substrate molecule or reactants, the reactions of which are
catalyzed.
22
Functional Classification of Proteins
Transport Proteins
Channel and carrier proteins allow the movement of different molecules
across the cell membrane.
23
Functional Classification of Proteins
Immune Proteins
Interactions between antigens and antibodies help trigger immune
responses. 24
Functional Classification of Proteins
Chemical Messengers
Insulin consists of two amino acid chains connected by disulfide bridges (in
yellow color) between cysteine residues. 25
Functional Classification of Proteins
Contractile Proteins
Contractile proteins are present in muscle cells, which helps the body to
initiate various forms of movements. 26
Functional Classification of Proteins
Storage Proteins
Storage proteins provide amino acids for growing organisms, such as
germinating seeds and developing embryos in eggs.
27
How are proteins involved in
the different metabolic
processes?
28
Check Your Understanding
Write true if the statement is correct and false if it is
otherwise.
1.The twenty 20 amino acids can be grouped according to
whether their R group is hydrophobic or hydrophilic.
2.Tertiary protein structure consists of more than one
polypeptide.
3.An unfavorable change in the condition of the
environment cannot affect the shape of proteins.
29
Check Your Understanding
Briefly explain the possible consequences should the
following events take place.
1.All amino acids have the same side groups.
2.Some gene mutations resulted in an impaired urea
cycle.
3.The body does not produce ammonium ions.
30
Let’s Sum It Up!
● Proteins are biological compounds composed of
chains of amino acid monomers. Proteins, given
the variety of their structures, have diverse
functions in living organisms.
31
Let’s Sum It Up!
● Each amino acid consists of a central carbon that
is bonded to four covalent groups. Three of these
four attachments are common to all 20 amino
acids—an amino group (—NH2), a carboxyl
group (—COOH), and a hydrogen atom. The
variable component of amino acids, the R group
(radical group), is attached via the fourth bond of
the central carbon.
32
Let’s Sum It Up!
● A peptide consists of two or more amino acids
bonded together, and the resulting longer chain of
amino acids joined by peptide bonds is called a
polypeptide. A protein is a polymer consisting of
one or more polypeptides.
33
Let’s Sum It Up!
● The overall shape of a protein has at least three
levels of structure, which are primary, secondary,
and tertiary structures. Proteins with more than
one polypeptide chain have a fourth level called the
quaternary structure.
34
Let’s Sum It Up!
● Protein shape is sensitive to the surrounding
environment. Any unfavorable change in
temperature, pH, salt, or some other cellular
conditions may result in denaturation or loss of
normal protein function.
35
Let’s Sum It Up!
● Proteins are, in many ways, important to living
organisms. Proteins may function to provide
structure, storage, catalysis, transport,
chemical signaling, motility, and immunity.
36
Let’s Sum It Up!
● Protein digestion involves various enzymes
produced by the stomach, pancreas, and small
intestine. After absorption, amino acids are
transported to the liver and other body tissues for
further metabolism.
37
Let’s Sum It Up!
● One byproduct of amino acid metabolism is
ammonium. The urea cycle in the liver allows the
processing of ammonium ions so that they can be
excreted in the urine.
38
Let’s Sum It Up!
Graphical representation of structure, functions, and metabolic
activities involving proteins 39
Photo Credit
● Slide 19: This photo, Protein Denaturation by RMADLA, is licensed under CC-BY SA 3.0 via
Wikimedia Commons.
40
Bibliography
Hoefnagels, Marielle. Biology: The Essentials. 2nd ed. McGraw-Hill Education. 2016.
Mader, Sylvia S., and Michael Windelspecht. Biology. 11th ed. McGraw-Hill Education. 2014.
“Protein Metabolism.” BC Campus. Accessed April 17, 2020.
https://opentextbc.ca/anatomyandphysiology/chapter/24-4-protein-metabolism/.
Reece, Jane B, Martha R. Taylor, Eric J. Simon, Jean L. Dickey, and Kelly Hogan. Biology Concepts and
Connections. 8th ed. Pearson Education South Asia, Pte Ltd., 2016.
Simon, Eric J., and Jane B. Reece. Campbell Essential Biology. 5th ed. Pearson Education Inc., 2013.
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Bibliography
Starr, Cecie, Christine A. Evers, and Lisa Starr. Biology Applications and Concepts. 8th ed. Cengage
Learning Asia Pte. Ltd., 2012.
Starr, Cecie, Christine A. Evers, and Lisa Starr. Biology: Today and Tomorrow. 4th ed. Cengage Learning
Asia Pte. Ltd., 2014.
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