Course Code: BIO 073 (Biochemistry/Biomolecules)

Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

Lesson title: PROTEINS Materials:

Lesson Objectives: by the end of this module, you should be Pen, SAS
able to:
1. Classify different amino acids based on its physicochemical References:
properties and functions ▪ stoker, H. S. (2017).Biochemistry
2. Name different peptide formation based on IUPAC Rules (3rd ed.). (M. Finch, Ed.) Belmont
CA, USA,
3. Determine the physicochemical properties of protein ▪ Ferrier, D. (2017). Lippincott's
4. Classify proteins based on the number of peptide chain, Illustrated Biochemistry (7 ed.).
chemical composition, level of structural organization, gross Lippincott Williams & Wilkins,.
structure or shape and functions.
5. Explain the etiology and symptoms of protein related
diseases

Productivity Tip: Start this module by pinning your belief that Biochemistry is a challenging yet very
interesting course to venture. And, one of the best ways to study this course effectively is known as the
PROTÉGÉ’ EFFECT. It means that to understand a concept, one must explain it to someone else or simply
teach someone what you want to learn.

Note for teachers: Later for an in between activities or once the module is done, let the student exercise the
protégé’ effect. Or if not, for dentistry students, please see the suggested oral recitation question.

A. LESSON PREVIEW
Introduction: (2 min)

Next to water, proteins are the most abundant substances in

nearly all cells—they account for about 15% of a cell’s overall mass and
for almost half of a cell’s dry mass. All proteins contain the elements
carbon, hydrogen, oxygen, and nitrogen; most also contain sulfur.
The presence of nitrogen in proteins sets them apart from
carbohydrates and lipids, which most often do not contain nitrogen. The
average nitrogen content of proteins is 15.4% by mass. Other
elements, such as phosphorus and iron, are essential constituents of
certain specialized proteins.
An extraordinary number of different proteins, each with a
different function, exist in the human body. A typical human cell
contains about 9000 different kinds of proteins, and the human body
contains about 100,000 different proteins. As scientists would have to
say that if there are such things being done in a molecular level, it would be done by protein. In this
module you will learn about what constitute a protein, how they are made and their functions and uses.
Novel SARs Cov-2 spike proteins

This document is the property of PHINMA EDUCATION Page |1

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

Activity 2: What I Know Chart, part 1 (2 min)

Instructions: "In this chart, reflect on what you know now. Do not worry if you are sure or not sure of
your answers. This activity simply serves to get you started on thinking about our topic. Answer only
the first column, "What I know" based on the question of the second column. Leave the third column
"What I learned" blank at this time.

What I Know Questions: What I Learned (Activity 5)

1. Proteins, what are they made
of?
2. How are proteins formed?

3. Give example of protein related

disorder?

B.MAIN LESSON
Activity 2: Content Notes (60 mins)
Instructions: Make an outline of the most important information you will encounter in this module.

A protein is a naturally occurring, unbranched polymer in which the monomer units are amino
acids.
Fig. 1: a-amino acid

▪ -amino acid- is an amino acid in which the

amino group, the carboxyl group and the
hydrogen atom are attached to the -carbon
atom. All amino acids are alpha-amino acids
except Proline (an imino acid) since the side
chain is not free but attached to the amino
Protonated Deprotonated Fig. 2: Proline as
group. Amino acids differ from each other
(NH3+) at (COO-) at imino acid
based on their side chain structure.
physiologic pH physiologic pH
▪ group

CLASSIFICATION OF AMINO ACIDS:

Nonpolar amino acid Polar neutral Polar basic Polar acidic

•is an amino acid that
contains one amino
group, one carboxyl
group, and a
nonpolar side chain.
G,A,V,L,I,P,F,M,W
• is an amino acid that • is an amino acid that • is an amino acid that
contains one amino contains two amino contains one amino
group, one carboxyl groups and one group and two
group, and a side carboxyl group, the carboxyl groups, the
chain that is polar but second amino group second carboxyl
neutral. S,C,N,T,Q,Y being part of the side group being part of
chain. H,K,R the side chain. D,E

This document is the property of PHINMA EDUCATION Page |2

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

Fig. 3: Structures of amino acids

Note: These set of

amino acids are
found in the interior
of proteins that
function in an
aqueous
environment and on
the surface of
proteins (such as
membrane proteins)
that interact with
lipids

Note: Polar
uncharged or
neutral, acidic and
basic amino acids
are found on the
outside of proteins
that function in an
aqueous
environment and in
the interior
membrane –
associated proteins.

Aka polar negative AA, side chain Aka polar positive AA, side chain is protonated
dissociates to –COO- at physiologic and generally positive charge at physiologic pH
pH

This document is the property of PHINMA EDUCATION Page |3

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

Selenocysteine (Sec), 21st amino acid, codon (UGA)

Pyrrolysine (Pyr), 22nd amino acid, codon (UAG)

ESSENTIAL AMINO ACIDS NON-ESSENTIAL AMINO ACIDS

•- a standard amino acid needed for protein •Synthesized by the body. These are
synthesis that must be obtained from dietary C,A,N,D,E,Y,S, Q,G,P,
sources because the human body cannot
synthesize it in adequate amount.
R*,H,M,I,L,K,W,T,F,V (R – arginine is essential for
children’s growth but not for adult)

• COMPLETE DIETARY PROTEIN - is a protein that contains all of the essential amino acids in the
same relative amounts in which the body needs them. This may or may not contain all of the
nonessential amino acids
• INCOMPLETE DIETARY PROTEIN - is a protein that does not contain adequate amounts, relative to
the body’s needs, of one or more of the essential amino acids
• LIMITING AMINO ACID - is an essential amino acid that is missing, or present in inadequate amounts,
in an incomplete dietary protein
• COMPLEMENTARY DIETARY PROTEINS- are two or more incomplete dietary proteins that, when
combined, provide an adequate amount of all essential amino acids relative to the body’s needs. Ex.
Rice and beans servings.

This document is the property of PHINMA EDUCATION Page |4

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

USES/FUNCTIONS OF AMINO ACIDS

AMINO
USES/ FUNCTIONS
ACIDS

Necessary for the synthesis of neurotransmitter serotonin (5-hydroxytryptamine). A natural relaxant, helps
alleviate insomnia by inducing normal sleep; reduces anxiety and depression.
Trp
-Can be metabolized to niacin Vit. B3 if needed
-Used to synthesized melatonin (5-methoxy-N-acetyltryptamine)

Precursor of dopamine, norepinephrine, epinephrine

Tyr
Promotes healthy thyroid functioning

Val, Ile, enhance energy, increase endurance, and aid in muscle tissue recovery and repair.
Leu -lowers elevated blood sugar levels and increases growth hormone production.

precursor for L-carathine which is essential for healthy nervous system function.
Lys
-for adequate absorption of calcium and bone development in children

-Is antioxidant. It helps in breakdown of fats and aids in reducing muscle degeneration. Helps lower cholesterol
levels by increasing the liver's production of lecithin; reduces liver fat and protects the kidneys.
Met -principle supplier of sulfur, which inactivates free radicals. Is a natural chelating agent for heavy metals and
helps detoxify the body of these metals.
-Adequate methionine prevents disorders of the hair, skin and nails;

-Beneficial for healthy nervous system. It may be useful against depression and suppressing appetite.
-Used to produce dopamine and norepinephrine, chemicals that promote alertness, elevate mood, decrease
pain, aid in memory and learning, and reduce hunger and appetite.
Phe -D-phenylalanine - natural form. May improve rigidity, walking disabilities, speech difficulties and depression
associated with Parkinson’s disease.
-L-phenylalanine can be converted into L-tyrosine, which is in turn converted into L-DOPA. L-DOPA is a
precursor for dopamine, norepinephrine (noradrenalin), and epinephrine (adrenaline)

Ala Removes toxic substances released from breakdown of muscle protein during intensive exercise

antioxidant (free radical scavenger), and has synergetic effect when taken with other antioxidants such as
Cys
vitamin E and selenium.

Gln Promotes healthy brain function. It is also necessary for the synthesis of RNA and DNA molecules.

Gly Component of skin and is beneficial for wound healing. It acts as neurotransmitter

Important for the synthesis of red and white blood cells.

His
It is a precursor for histamine which is good for sexual arousal. Improve blood flow.

Thr It helps promote equilibrium in the central nervous system—aids in balancing state of emotion.

Enhances stamina, aids in removal of toxins and ammonia from the body, and beneficial in the synthesis of
Asp
proteins involved in the immune system.

Pro plays role in intracellular signaling.

plays role in blood vessel relaxation, stimulating and maintaining erection in men, production of ejaculate, and
Arg removal of excess ammonia from the body.

This document is the property of PHINMA EDUCATION Page |5

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

ACID – BASE PROPERTIES OF AMINO ACIDS

• In pure form, amino acids are white crystalline solids with relatively high decomposition
points. (Most amino acids decompose before they melt.)
• Also, most amino acids are not very soluble in water because of strong intermolecular
forces within their crystal structures. Such properties are those often exhibited by
compounds in which charged species are present.
• Studies of amino acids confirm that they are charged species both in the solid state and in
solution.

Zwitterion

• is a molecule that has a

positive charge on one atom
and a negative charge on
another atom, but which has
no net charge.
• the net charge on a Amino acid Amino acid in
zwitterion is zero even
Zwitterion form
though parts of the molecule
carry charges

This document is the property of PHINMA EDUCATION Page |6

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

This document is the property of PHINMA EDUCATION Page |7

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

PEPTIDE FORMATION
Illustration 1:
The relationship between
Within a protein, amino acid side chains and
multiple amino acids are protein conformation

linked together by peptide

bonds, thereby forming a
long chain. Peptide bonds
are formed by a biochemical
reaction that extracts a water
(H2O) molecule as it joins
the amino group of one
amino acid to the carboxyl
group of a neighboring
amino acid. Hence,
Peptide bond aka Amide
bond - is a covalent bond
between the carboxyl group
of one amino acid and the
amino group of another
amino acid. However, it
should be noted that proteins
are not only assembled with
different amino acid
sequences, but they also are
held together by different
bonds and folded into a
variety of three-dimensional
structures. The folded shape,
or conformation, depends
directly on the linear amino
acid sequence of the protein.
The linear sequence of
amino acids within a protein
is considered the primary structure of the protein.
Proteins are built from a set of only twenty amino acids, each of which has a unique side chain.
The side chains of amino acids have different chemistries. The largest group of amino acids have
nonpolar side chains. Several other amino acids have side chains with positive or negative charges,
while others have polar but uncharged side chains. The chemistry of amino acid side chains is critical to
protein structure because these side chains can bond with one another to hold a length of protein in a
certain shape or conformation. Charged amino acid side chains can form ionic bonds, and polar amino
acids are capable of forming hydrogen bonds. Hydrophobic side chains interact with each other via
weak van der Waals interactions. The vast majority of bonds formed by these side chains are
noncovalent. In fact, cysteines are the only amino acids capable of forming covalent bonds, which they
do with their particular side chains. Because of side chain interactions, the sequence and location of
amino acids in a particular protein guides where the bends and folds occur in that protein.

This document is the property of PHINMA EDUCATION Page |8

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

TYPES OF PEPTIDE BOND

Dipeptide Tripeptide oligopeptide Polypeptide

•w/ 2 or more amino •w/ 3 or more amino • w/ 10 or 20 amino •w/ longer

acids acids joined together acid residues are unbranched chain of
in a chain present in a chain amino acids

STEP by STEP PEPTIDE FORMATION

FIRST: SECOND: THIRD:

Two amino acids are brought
together. The acid group of the
first is close to the amine group
of the second.
Next, a water molecule is
eliminated, leaving a bond
between the acid carbon of the
first amino acid and the amine
nitrogen of the second
The peptide bond is left
between the two amino acids
and the chain continue.

PEPTIDE NOMENCLATURE (IUPAC)

Peptide Bonds
1. The amino acid naming sequence
begins at the N-terminal amino
acid residue.

2. All of the other amino acid w/ free H3+N w/ free COO-

residues have names that end in – group group
yl. The –yl suffix replaces the –ine
or ic acid ending of the amino acid
name, except for tryptophan
(tryptophyl), cysteine (cysteinyl),
Direction of peptide chain
glutamine (glutaminyl), and
asparagine (asparaginyl). Glycylalanylserine
3. The C-terminal amino acid residue
keeps its full amino acid name.

This document is the property of PHINMA EDUCATION Page |9

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

EXAMPLES OF BIOCHEMICALLY IMPORTANT PEPTIDES:

Oxytocin (9)
Uterus-Contracting Hormone
(also stimulates lactation)
Vasopression (ADH or
antidiuretic hormone)
Enhances reabsorption of free water
and plays a role in Blood pressure
control
Enkephalins (5)
pain killers
neuromodulators
in the brain and spinal cord; involved
with pain perception,
movement, mood, behavior,
and neuroendocrine regulation

TRH (Thyrotropin Releasing Angiotensin II (8)

Glutathione (3) Hormone) (3) Pressor Agent. Can increase blood
Found in most living cells as Hypothalmic Neurohormone pressure by vasoconstriction.; can
antioxidant & promote tissue also trigger thirst or the desire for
(governs release of thyrotropin) or TSH salt. Is responsible for the release of
growth or thyroid-stimulating hormone
the pituitary gland's ADH

Somatostatin (14) Bradykinin (9) Endothelin (21)

Inhibits Growth Hormone Potent Vasoconstrictor
Hypotensive Vasodilator
Release (structurally similar to some
(used to treat ulcers) (acts on smooth muscle) snake venoms)

Mellitin (26) Glucagon (29) Insulin (51)

Honey Bee Venom Hyperglycemic Factor Pancreatic Hormone
(used to treat rheumatism) (used as an anti-diabetic) (used in treatment of diabetes)

• TSH: stimulates the thyroid gland to produce thyroxine (T4), and then triiodothyronine (T3) which
stimulates the metabolism of almost every tissue in the body ) and prolactin or luteotropin (protein that
enable female mammals to produce milk) from the anterior pituitary.

This document is the property of PHINMA EDUCATION P a g e | 10

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

STRUCTURES OF PROTEIN
The primary structure of a protein — its amino acid sequence — drives the folding and
intramolecular bonding of the linear amino acid chain, which ultimately determines the protein's unique
three-dimensional shape. Hydrogen bonding between amino groups and carboxyl groups in
neighboring regions of the protein chain sometimes causes certain patterns of folding to occur. Known
as alpha helices and beta sheets, these stable folding patterns make up the secondary structure of a
protein. Most proteins contain multiple helices and sheets, in addition to other less common patterns.
The ensemble of formations and folds in a single linear chain of amino acids — sometimes called a
polypeptide — constitutes the tertiary structure of a protein. Finally, the quaternary structure of a protein
refers to those macromolecules with multiple polypeptide chains or subunits.
Fig. 5: structures of
proteins

Fig. 5.1: Primary

structure of myoglobin

Held by covalent peptide bonds

β- Fig 5.2. Common structural motifs combining α-helices and/or β-sheets. The
names describe their schematic appearance

Other forms:
1. β-Bends(reverse
turn,
β -turns) α-α (helix-loop-helix) β-α-β β-Meander β-Barrel
2. Nonrepetitive 2nd
structure
3. Supersecondary
structures (motifs)

Fig. 5.3: Tertiary

structure

Electrostatic interaction (salt

bridges)

Fig. 5.4: Hemoglobin

The two or more polypeptide chain may be structurally identical or Human hemoglobin molecule is a
totally unrelated. Subunits are held together by noncovalent tetramer w/ two alpha and two beta
interactions (for example, hydrogen bonds, ionic bonds, and polypeptide chains in which the
hydrophobic interactions). This is also when the protein binding of oxygen to one subunit of the
associates with non-proteic groups like carbohydrates can be tetramer increases the affinity of the
added to form a glycoprotein. other subunits for oxygen

This document is the property of PHINMA EDUCATION P a g e | 11

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

How Do Proteins Arrive at Their Final Shapes?

Protein folding
Interactions between the side chains of amino acids determine how a linear polypeptide chain
folds into the intricate three-dimensional shape of the functional protein. Protein folding, which occurs
within the cell in seconds to minutes, involves nonramdom, ordered pathways. As a peptide folds,
secondary structures form, driven by the hydrophobic effect (that is hydrophobic groups come together
as water is released). These small structures combined to form larger structures. Additional events
stabilize secondary structure and initiate formation of tertiary structure. Its amino acid side chains are
attracted and repulsed according to their chemical properties. For example, amino acids w/ positively
and negatively charged side chains attract each other, ionic bond. Conversely, similarly charged side
chains repel each other. In addition, interactions involving hydrogen bonds (between polar neutral
amino acids), hydrophobic interactions (between nonpolar amino acids), and disulfide bonds (2
cysteine atoms) all exert an influence on the folding process. This process of trial and error tests many,
but not all, possible configurations, seeking a compromise in which attractions outweigh repulsions The
last stage, the peptide achieves its fully folded, native (functional) form characterized by low energy
state. (Note: Some biologically active proteins or segments thereof lack a stable tertiary structure. They
are referred to as intrinsically disordered proteins.)
Denaturation of proteins
Protein denaturation results in the unfolding and disorganization of the protein’s secondary and
tertiary structures, which are not accompanied by hydrolysis of peptide bonds. Denaturing agents
include heat, organic solvents, mechanical mixing, strong acids or bases, detergents, and ions of heavy
metals such as lead and mercury. Denaturation may, under ideal conditions, be reversible, in which
case the protein refolds into its original native structure when the denaturing agent is removed.
However, most proteins, once denatured, remain permanently disordered. Denatured proteins are often
insoluble and, therefore, precipitate from solution.
Role of chaperones in protein folding
The information needed for correct protein folding is contained in the primary structure of the
polypeptide. However, most denatured proteins do not resume their native conformations under
favorable environmental conditions. This is because, for many proteins, folding is a facilitated process
that requires a specialized group of helper proteins, referred to as molecular chaperones, and ATP
hydrolysis. The chaperones, aka heat shock proteins (HSP), interacts with a polypeptide at various
stages during the folding process. Some chaperone bind to hydrophobic regions of extended
polypeptide and are important in keeping the protein unfolded until its synthesis is completed (example,
Hsp70) or act as catalysts by increasing the rates of the final stages in the folding process. Others
protect proteins as they fold so that their vulnerable, exposed regions do not become tangled in
unproductive interactions.

Illustration A Illustration B

This document is the property of PHINMA EDUCATION P a g e | 12

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

Figure 2.15 Key concept map for protein structure.

This document is the property of PHINMA EDUCATION P a g e | 13

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

PHYSICAL AND CHEMICAL PROPERTIES OF PROTEINS

PHYSICAL PROPERTIES
Color and Taste colorless and usually tasteless; They are
homogeneous and crystalline.
Shape and Size range in shape from simple crystalloid spherical
structures to long fibrillar structures. (will be
discussed more on the “Classification of Proteins:
Based on shape”)
Molecular Weight generally have large molecular weights ranging
between 5 × 103 and 1 × 106. It might be noted
that the values of molecular weights of many
proteins lie close to or multiples of 35,000 and
70,000.
Colloidal Nature Because of their giant size, the proteins exhibit
many colloidal properties, such as; Their
diffusion rates are extremely slow and they
may produce considerable light-scattering in
solution, thus resulting in visible turbidity
(Tyndall effect).
Denaturation Denaturation refers to the changes in the
properties of a protein. In other words, it is the loss
of biologic activity. In many instances the process
of denaturation is followed by coagulation— a
process where denatured protein molecules tend
to form large aggregates and to precipitate from
solution.
Amphoteric Nature Like amino acids, the proteins are amphoteric,
i.e., they act both as acids and bases. These
migrate in an electric field and the direction of
migration depends upon the net charge
possessed by the molecule. The net charge is
influenced by the pH value. Each protein has a
fixed value of isoelectric point (pl) at which it will
move in an electric field.
Ion Binding Capacity The proteins can form salts with both cations and
anions based on their net charge.
Solubility The solubility of proteins is influenced by pH.
Solubility is lowest at isoelectric point and
increases with increasing acidity or alkalinity. This
is because when the protein molecules exist as
either cations or anions, repulsive forces between
ions are high, since all the molecules possess
excess charges of the same sign. Thus, they will
be more soluble than in the isoelectric state.

This document is the property of PHINMA EDUCATION P a g e | 14


Name: _____________________________________________________________
Section: ____________ Schedule:_____________________________________
Optical Activity
CHEMICAL PROPERTIES
Hydrolysis
Reactions involving COOH Group
Reactions involving NH2 Group
Reactions involving both COOH AND NH2
Group
Reactions involving R Group or Side Chain
This document is the property of PHINMA EDUCATION
Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3
Class number: _______
Date: ________________
All protein solutions rotate the plane of polarized
light to the left, i.e., these are levorotatory.
Proteins are hydrolyzed by a variety of hydrolytic
agents.
A. By acidic agents: Proteins, upon hydrolysis
with conc. HCl (6–12N) at 100–110°C for 6 to 20
hrs., yield amino acids in the form of their
hydrochlorides.
B. By alkaline agents: Proteins may also be
hydrolyzed with 2N NaOH.
A. Reaction with alkalies (Salt formation)
B. Reaction with alcohols (Esterification)
C. Reaction with amines
A. Reaction with mineral acids (Salt formation):
When either free amino acids or proteins are
treated with mineral acids like HCl, the acid salts
are formed.
B. Reaction with formaldehyde: With
formaldehyde, the hydroxy-methyl derivatives are
formed.
C. Reaction with benzaldehyde: Schiff ‘s bases
are formed
D. Reaction with nitrous acid (Van Slyke reaction):
The amino acids react with HNO2 to liberate N2
gas and to produce the corresponding α-hydroxy
acids.
E. Reaction with acylating agents (Acylation)
F. Reaction with FDNB or Sanger’s reagent
G. Reaction with dansyl chloride
A. Reaction with triketohydrindene hydrate
(Ninhydrin reaction)
B. Reaction with phenyl isocyanate: With phenyl
isocyanate, hydantoic acid is formed which in
turn can be converted to hydantoin.
C. Reaction with phenyl isothiocyanate or Edman
reagent
D. Reaction with phosgene: With phosgene, N-
carboxyanhydride is formed
E. Reaction with carbon disulfide: With carbon
disulfide, 2-thio-5-thiozolidone is produced
A. Biuret test – test for proteins with peptide
bonds. Positive reaction will be the color change
from blue (color of the biuret reagent) to violet.
P a g e | 15
 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

All peptides and protein give the test positive.

Also, Histidine is the only amino acid that give
biuret test positive.

B. Xanthoproteic test - or the detection of amino

acids containing phenolic or indolic groups
like phenylalanine, tyrosine, and tryptophan
(aromatic amino acids). The test allows the
differentiation of aromatic amino acids from
non-aromatic amino acids.

Positive result: The appearance of a dark yellow

or orange-colored solution represents a positive
test. This indicates the presence of aromatic
groups in the proteins and amino acids.
Negative result: The absence of a dark yellow or
orange-colored solution represents a negative
test. This indicates the absence of aromatic
groups in proteins and amino acids.

C. Millon’s test - test used for the detection of the

amino acid tyrosine, which is the only amino acid
containing the phenol group.

Positive result: A positive result in the Millon’s

test is demonstrated by the formation of a red or
pink colored precipitate. This indicates the
presence of tyrosine or tyrosine containing protein.
Negative result: A negative result in the Millon’s
test is demonstrated by the absence of colored
precipitate in the test tube. This indicates the
absence of tyrosine or tyrosine-containing protein.

D. Sullivan and McCarthy’s Test - test for the

detection of the amino acid methionine or
methionine-containing proteins.

Positive result: The positive result is represented

by the appearance of the red color. This indicates
the presence of methionine.
Negative result: The negative result is
represented by the absence of the red color. This
indicates the absence of methionine.

This document is the property of PHINMA EDUCATION P a g e | 16

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

E. Sakaguchi test - test consisting of colorimetric

reaction for the detection and quantification of
guanidinium groups, used as a qualitative test
for arginine that is either free or in protein.

Positive result: A positive result on the

Sakaguchi’s test is demonstrated by the formation
of red color. This indicates the presence of an
arginine or guanidinium compound.
Negative result: A negative result in the
Sakaguchi’s test is demonstrated by the absence
of red color. This indicates an absence of arginine
or a guanidinium compound.

F. Pauly test - test for the detection of tyrosine

and histidine where the reagent couples with
amines, phenols, and imidazole groups.

Positive result: A positive result is demonstrated

by the appearance of a red-colored complex,
indicating the presence of histidine and tyrosine in
the solution.
Negative result: A negative result is
demonstrated by the absence of a red-colored
solution, indicating the absence of histidine and
tyrosine in the sample.

G. Ehrlich test - test used for the detection of

amino acid, tryptophan, in a protein sample.

Positive result: A positive result in the Ehrlich

test is indicated by the appearance of red to
purple or blue-violet color. The color then changes
to blue with the addition of NaNO2. This indicates
that the sample contains tryptophan.
Negative result: A negative result in the Ehrlich
test is indicated by the absence of blue-violet color
on the addition of the Ehrlich reagent. This
indicates that the sample doesn’t contain any
tryptophan.

Reactions involving SH Group A. Nitroprusside test: red color develops with

sodium nitroprusside in dilute NH4OH. The test
is specific for cysteine.

This document is the property of PHINMA EDUCATION P a g e | 17

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

B. Sullivan test: Cysteine develops red color in

the presence of sodium 1, 2-naphthoquinone-
4-sulfonate and sodium hydrosulfite. This test
was pioneered by the American Organic and
Industrial Chemist, Eugene Cornelius Sullivan
(1872–1962).

CLASSIFICATION OF PROTEINS: Proteins are classified based on the number of peptide chain ,
chemical composition, shape and function

I. NUMBER OF PEPTIDE CHAIN

MONOMERIC PROTEIN MULTIMERIC PROTEIN

•is a protein in which only one peptide •is a protein in which more than one
chain is present. peptide chain is present.
•Example: myoglobin •The peptide chains present are called
protein subunits.
•Example: insulin

II. CHEMICAL COMPOSITION

SIMPLE PROTEIN CONJUGATED PROTEIN DERIVED PROTEIN

•is a protein in which only
amino acid residues are
present
•is a protein that has one •These include substances
or more non-amino acid formed from simple
entities present in its conjugated proteins.
structure in addition to
one or more peptide
chains.

EXAMPLES OF SIMPLE PROTEINS

ALBUMINS
Examples:
-Serum albumin (blood)
-Lactalbumin (milk)
-Ovalbumin (eggwhite)
GLOBULINS
PROLAMINES
Examples: GLUTELINS
-Ovoglobulin (eggwhite),
Examples:
Examples:
-Edestin (hempseed), -Gliadin (wheat)
-Legumin (peas)
-Glutenin (wheat)
-Zein (corn)
-Myosinogen (muscles) -Oryzenin (rice)
-Hordein (barley)
-Serum globulin (blood)

This document is the property of PHINMA EDUCATION P a g e | 18

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

SCLEROPROTEINS
(Albuminoids)
HISTONES
PROTAMINES Examples:
Examples:
Examples: -Keratin (epidermal tissues)
--Thymus histones
Salmin (salmon sperm) -Elastins (Ligaments)
-Scobrone of Mackerel
-Collagen (hides, bones and
cartillage)

EXAMPLES OF CONJUGATED PROTEINS

• prosthetic group is a non-amino acid group present in a conjugated protein. These non-amino
acid components, which may be organic or inorganic.

B. GLYCOPROTEINS
A. NUCLEOPROTEINS (more proteins less carbohydrates)
Examples: Examples:
Ribosomes (site for protein synthesis in cells) Mucin aka mucoproteins – more carbs less proteins (saliva,
mucous secretion of the nose)
Viruses (self-replicating, infectious complex) Tendomucoid (tendons)
Chromatin Osseomucoid (bones)
Products from glandular tissues gamma globulin (antibody)
Germ of grains Interferon (antiviral protection)
Simple proteins like globulins and albumins

This document is the property of PHINMA EDUCATION P a g e | 19

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

D. CHROMOPROTEINS/HEMOPROTEINS
C. PHOSPHOPROTEINS Examples:
Examples: Hemoglobin (blood -carrier of O2 in blood )
Casein (milk) Myoglobin (oxygen binder in muscles)
Vitellin (egg yolk) Cytochromes
Rhodopsin

E. LIPOPROTEINS
D. METALLOPROTEINS
Examples:
Examples:
Lecithin
iron–ferritin (storage complex for iron)
Cephalin
zinc–alcohol dehydrogenase (enzyme in alcohol
low-density lipoprotein (LDL) – lipid carrier
oxidation)
high-density lipoprotein (HDL) – lipid carrier

EXAMPLES OF CONJUGATED PROTEINS

A. Primary Protein derivatives – proteins which have undergone slight intramolecular
rearrangement through the hydrolytic action of certain physical and chemical agents.
- synonymous w/ denatured proteins

METAPROTEINS
PROTEANS Examples: COAGULATED PROTEINS
Examples: Acid metaproteins (acid Examples:
Myosan from myosin albuminate) Cooked egg albumin
Edestan from edestin Alkali metaproteins (alkali Cooked meat
albuminate)

This document is the property of PHINMA EDUCATION P a g e | 20

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

B. Secondary Protein derivatives

▪ Product of more extensive hydrolysis
▪ Mixtures of fragments of original proteins varying in composition and size
▪ Exhibit certain common properties such as solubility in water and non-coagulability by
heat.

1. PRIMARY PROTEOSES
2. SECONDARY PROTEOSES
Properties
Properties
Soluble in water, precipitated by
conc.HNO3 and by half saturation with Precipitated only by complete
(NH4)2SO4 or ZnSO4. saturation with (NH4)2SO4 but nit with
picric acid and HNO3 .
Not coagulated by heat

3. PEPTONES
Properties
Soluble in water
Not coagulated by heat
Not precipitated by saturation with
(NH4)2SO4 but by certain alkaloidal
reagents, such as,phosphotingstic and
tannic acids.
4. PEPTIDES
Are combinations of two or more amino
acids, the carboxyl group of one being
united with the amino group of the
other.
Present properties like peptones
Ex. di, tri,tera,penta etc.

III. BASED ON SHAPE

FIBROUS
•Protein whose molecules have an elongated
shape with one dimension much longer than
the others.
•Properties:
•Tend to have simple, regular and linear
structures.
•Largely insoluble in ordinary aqueous
media
•Molecular weights are high
•Functions is for structural and support
GLOBULAR
•molecules have peptide chains that are folded
into spherical or globular shapes.
•The folding in such that most of amino acids
with hydrophobic side chains (nonpolar R
groups) are in the interior of the molecules
and most of the hydrophilic side chains (polar)
are on the outside of the molecule.
•Properties:
•Soluble in aqeous media
•Have been crystallized and have definite
molecular weights
•Can be denatured

This document is the property of PHINMA EDUCATION P a g e | 21

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

This document is the property of PHINMA EDUCATION P a g e | 22

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

IV. BASED ON FUNCTION

PROTEINS EXAMPLES USES

Catalytic Enzymes biochemical catalyst

Defense Immunoglobulins or antibodies Protect body’s immune system/response

(IgG,IgM,IgA,IgE)
Transport ▪ Hemoglobin • carries oxygen from the lungs to other
organs and tissues.
• carries iron from the liver to the bone
▪ Transferrin marrow

Messenger Insulin transmit signals to coordinate biochemical

Glucagon processes between different cells, tissues,
Human growth hormone and organs

Contractile Actin and myosin necessary for all forms of movement

Structural Collagen confer stiffness and rigidity to otherwise fluid-
Keratin like biochemical

Storage Ferritin
Myoglobin
Regulatory transcription factors (TFs) -
protect their binding DNA sequences
from nuclease cleavage, resulting in
the markedly increased accessibility
surrounding their binding sites and
over neighboring chromatin
Transmembrane Membrane transport proteins (eg.
Glucose transporter)
Ligand gated ion channels
Nutrient Casein
Ovalbumin
bind (and store) small molecules for future use
Act as sites at which messenger molecules,
like insulin, can bind and thereby initiate the
effect that the messenger “carries.”
Are often the molecules that bind to enzymes
(catalytic proteins), thereby turning them “on”
and “off” and thus controlling enzymatic
action.
function as gateways to permit the transport of
specific substances across the membrane
particularly important in the early stages of
life, from embryo to infant.

Buffer Hemoglobin has a buffering role in part of the system by which the acid-base
addition to being an oxygen carrier. balance within body fluids is maintained

Fluid Balance Albumin (serum albumin) help maintain fluid balance between blood
Globulin and surrounding tissue

This document is the property of PHINMA EDUCATION P a g e | 23

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

PROTEIN RELATED DISORDERS:

I. Protein Energy (calorie) Malnutrition (PEM): Kwashiorkor & Marasmus

A.Kwashiorkor: Kwashiorkor occurs when protein deprivation is relatively greater than the reduction in
total calories. Protein deprivation is associated with severely decreased synthesis of visceral protein
(usually albumin). Kwashiorkor is frequently seen in children after weaning at about one year of age,
when their diet consists predominantly of carbohydrates. Typical symptoms include stunted growth,
edema, skin lesions, depigmented hair, anorexia, enlarged fatty liver, and decreased plasma albumin
concentration. Edema results from the lack of adequate plasma proteins (albumin) to
maintain the distribution of water between blood and tissues. Edema may mask muscle
loss.

B.Marasmus: Marasmus occurs when calorie deprivation is relatively greater than the
reduction in protein. It usually occurs in children younger than 1 year of age when breast
milk is supplemented with watery gruels of native cereals that are usually deficient in
protein and calories. Typical symptoms include arrested growth, extreme muscle wasting
(emaciation), weakness, and anemia (Figure 27.22). Victims of marasmus do not show the
edema or changes in plasma proteins observed in kwashiorkor.

II. Protein misfolding: Amyloidosis, Prion disease (human, sheep, cow)

A. Amyloidosis: accumulation of insoluble, long, fibrillar protein assemblies consisting of β-pleated sheets
caused by abnormal proteolytic cleavage.
a. Alzheimer disease. amyloid plaque caused by accumulation of amyloid β (Aβ), a peptide containing
40–42 amino acid residues, which are nonbranching fibrils of Beta pleated sheet. These peptides are
neurotoxic, and is the central pathogenic event leading to the cognitive impairment characteristic of the
disease. A second biologic factor is the accumulation of neurofibrillary tangles inside neurons. A key
component of these tangled fibers is an abnormal form of the tau (τ) protein, which in its healthy version
helps in the assembly of the microtubular structure. The defective τ, however, appears to block the
actions of its normal counterpart.
B. Prion disease: The prion protein (PrP or PRNP) has been strongly implicated as the causative agent of
transmissible spongiform encephalopathies (TSEs) (group of rare degenerative brain disorders characterized
by tiny holes that give the brain a "spongy" appearance) , including Creutzfeldt-Jakob disease in humans,
scrapie in sheep, and bovine spongiform encephalopathy in cattle (popularly called “mad cow disease”). CJD
– Creutzfeldt-Jakob disease - An increased concentration of 14-3-3 protein in cerebrospinal fluid supports
the diagnosis of Creutzfeldt Jakob disease (CJD ), Types of CJD: (1) Familia CJD- mutation in PRNP gene at
the 200th codon, causing conversion of glutamic acid to lysine.(2) Variant CJD – eating cow’s meat with prion

This document is the property of PHINMA EDUCATION P a g e | 24

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

protein.(3) Iatrogenic CJD – caused by medical procedure (exx. Corneal transplant).(4) Sporadic CJD – no
clear cause. Spontaneous mutation in the 129 th codon of the PRNP gene causing replacement of valine to
methionine. Another TSE, kuru disease, cannibalism of infected flesh (like fatal familial insomnia caused by
mutation of PRNP gene at the 178th codon replacing aspartic acid with asparagine)
III. Hemoglobinopathies

IV. Collagenopathies
V. Alpha-1-Antitrypsin Deficiency

This document is the property of PHINMA EDUCATION P a g e | 25

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

This document is the property of PHINMA EDUCATION P a g e | 26

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

Activity 3: Skill-building Activities (with answer key) (25 mins + 3 mins checking). Check your answer in
the key to correction

A. FILL IN THE TABLE BELOW: Using the clues, fill in the table below with the needed three (3)
letter abbreviation, symbol, polarity, classification as essential or nonessential, and function (1) of
the amino acids being asked.

3 letter Symbol Polarity Essential or Function (1 only)

nonessential

Gln

Increases calcium absorption

Essential for baby
but not for adult

B. PEPTIDE FORMATION and NOMENCLATURE:

1. Name the peptides based on the IUPAC rules. 2. Identify the amino acids in the peptide
and name it using the IUPAC rules.

Ans. Ans:

This document is the property of PHINMA EDUCATION P a g e | 27

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

C. MATCHING TYPE: Write only the letter of the correct answer

C.1 LEVEL OF STRUCTURAL ORGANIZATION: Using the phrases, statement and examples, fill in the table
that corresponds to the structural characteristics of proteins. Answers may be repeated.

A. Hydrophobic interactions G. Electrostatic interactions M. Haemoglobin

D.
B. Alpha- helix H. Disulphide bond N. Order in which amino acids are
E.
C. Sequence of amino acids I. Presence of non-protein linked together in a protein
D.
F. Beta-sheet component O. Backbone portions of proteins
E. Beta-bends J. Glycoproteins P. Overall 3D structure of proteins
F. Hydrogen bond K. Oligopeptides from attractive forces
L. Polypeptide formation

PRIMARY SECONDARY TERTIARY QUATERNARY

C.2 BONDS OF PEPTIDE: Identify the possible type of bonds possessed by the following pair of amino
acids as they may be involved in the folding of proteins.

Write
A- hydrophobic bond, B – hydrogen bond, C- Disulfide bond , D – ionic bond

_____ 1. Ala + Leu _____ 6. H + E

_____ 2. Ser + Thr _____ 7. K + D
_____ 3. His + Asp _____ 8. C + C
_____ 4. Glu + Asn _____ 9. T + Y
_____ 5. Val + Phe _____ 10. M + W

This document is the property of PHINMA EDUCATION P a g e | 28

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

C.3 CLASSIFICATION OF PROTEINS based on their chemical composition.

CHOICES: _____ 1. Serum albumin ____ 6. Collagen

A. _ Simple _____ 2. Ferritin ____ 7. Proteans
B. _ Conjugated _____ 3. Vitellin ____ 8. Peptones
C._ Derived _____ 4. Glutenin ____ 9. Coagulated proteins
_____ 5. Histones ____ 10. Lecithin

C.4 CLASSIFICATION OF PROTEINS based on the type of conjugated protein

CHOICES:
A. Hemoprotein _____ 1. Glycogen phosphorylase
B. Lipoprotein _____ 2. Myoglobin
C. Glycoprotein _____ 3. Interferon
D. Phosphoprotein _____ 4. HDL
E. Nucleoprotein _____ 5. Ferritin
F. Metalloprotein

C.5 CLASSIFICATION OF PROTEINS based on their shape

CHOICES:
A- Fibrous _____ 1. Collagen
B- Globular _____ 2. Transferrin
_____ 3. Fibrin
_____ 4. Immunoglobulin
_____ 5. Keratin

C.6 CLASSIFICATION OF PROTEINS based on their function.

Column A Column B
CHOICES: _____ 1. Collagen _____ 1. Moves muscle
A. Structural _____ 2. Myosin _____ 2. Stores nutrients
B. Defense _____ 3. Lipoproteins _____ 3. Regulates body metabolism
C. Messenger _____ 4. Casein _____ 4. Catalyze biochemical reactions in cells
D. Contractile _____ 5. Ferritin _____ 5. Recognize and destroy foreign substances.
E. Transport _____ 6. Insulin _____ 6. Provide structural components
F. Storage _____ 7. Sucrase _____ 7. Carry essential substances throughout the body
G. Catalytic _____ 8. Antibody _____ 8. Provides nutrition
H. Nutrient _____ 9. IgE _____ 9. Deliver oxygen from lungs to the body tissue
_____ 10. Keratin _____ 10. Regulates sugar level

This document is the property of PHINMA EDUCATION P a g e | 29

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

C.7 protein related disorder

DISORDERS: _______1. Aka brittle bone disorder

A. Alzheimer’s disease
B. Sporadic CJD
C. Kuru disease
D. Sickle cell disease
E. Alpha-Thalassemia
F. Scurvy
G. Osteogenesis
imperfecta
H. Ehler-danlus
_______2. product of cannibalism in Papua New Guinea.
_______3. Accumulation of neurotoxic amyloid β peptide
aggregates.
_______4. HbS, mutation of β6 from glutamic acid to valine
_______5. No known cause or the 129th codon of PRNP
gene replacement of valine to methionine.
_______6. Caused by decreased synthesis of α-globin
chains of hemoglobin

D. CASE ANALYSIS: Provide short answers

Score: _______

A 3-year old boy was examined at the Out Patient Department of the SWU Medical Center.
During the check up, the boy’s body weight is reduced to less than 60% of the normal
(expected) body weight for the age. The mother of the boy told to the doctors at that time
that he has good appetite despite of his weight condition but his mood is always irrititable
during eating time. Further physical checkup that there’s no edema present.

1. What possible disorder is represented in this case? (2 pt)

_________________________________________________
2. List at least 3 signs and symptoms that will justify possible diagnosis. (3pts)
__________________________________________________________________________

This document is the property of PHINMA EDUCATION P a g e | 30

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

Activity 4: What I Know Chart, part 2 (2 mins)

Instruction: To review what was learned from this session, please go back to Activity 1 and answer
the “What I Learned” column. Notice and reflect on any changes in your answers.

Activity 5: Check for Understanding (15 mins)

Instructions: Now it’s time for you to figure this one out on your own! Take time to read, analyze, and
understand the following scenarios. For this instance, you will not have the chance to check if you have
the correct answers since there are no more keys to correction.

MULTIPLE CHOICE: Check ALL that applies. WRITE the letter of your choice before each number.
Good luck.

1. Which of the following has the correct pairing?

a. Glutathione: Pancreatic hormone
b. Bradykinin: Hypotensive vasodilator
c. Oxytocin: Neuromodulator in the brain and spinal cord
d. Insulin: Potent vasoconstrictor
2. This amino acid is important in the synthesis of red and white blood cells.
a. Met
b. Gln
c. His
d. Asp
3. Which set of the following amino acids are all nonpolar?
a. W K Q
b. H M N
c. T N Y
d. G A P
4. Glycoprotein is a protein with what prosthetic group attach to it?
a. Phosphate group
b. Metal ion
c. Lipid
d. Carbohydrate
5. It carries the oxygen from the lungs to other organs and tissues
a. Hemoglobin
b. Transferrin
c. White blood cell
d. Insulin

This document is the property of PHINMA EDUCATION P a g e | 31

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

6. Debie just gave birth to a healthy baby. However, she was having hard time secreting milk.
Which of this small peptide hormone is associated in low level with Debie’s condition?
a. Enkephalins
b. Vasopressin
c. Oxytocin
d. Both Enkephalins & Vasopressin
7. One customer has bought Vitamin E and selenium in the Pharmacy and the Pharmacist
advised the costumer to also use this amino acid to have synergistic effect with the 2
mentioned supplements. What is the amino acid mentioned by the Pharmacist?
a. Asparagine
b. Cysteine
c. Glutamic acid
d. Glycine
8. The 21st amino acid
a. Selenocysteine
b. Selenicysteine
c. Carbocysteine
d. Pyrrolysine
9. His+Asp+Arg will engage this specific interaction
a. Hydrogen Bonding
b. Disulfide Bonds
c. Non-Polar Hydrophobic
d. Salt Bridges
10. Name the peptide

A. Methionyl-leucynyl- cysteine
B. Methionyl-leucinyl- cysteine
C. Leucyl- methionyl- cysteinyl
D. Methionyl-leucyl- cysteine

This document is the property of PHINMA EDUCATION P a g e | 32

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

C. LESSON WRAP-UP
Activity 6: Thinking about Learning (5 mins)

A. Work Tracker
You are done with this session! Let’s track your progress. Shade the session number you just
completed.

P1 P2
1 2 3 4 5 6 7 8 9 10

B. Think about your Learning:

Tell me about your thoughts! Today’s topic is all about the PROTEINS. What interests you about
the lesson today? What else you want to learn?

__________________________________________________________________
__________________________________________________________________
__________________________________________________________________
___________________________________

This document is the property of PHINMA EDUCATION P a g e | 33

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

FAQs

1. Are There Risks Associated with Eating Too Much Protein?

Ans. Protein is an essential part of a healthy diet. It helps to build and repair muscle, organs, and bones.
High-protein diets have also been shown to be helpful with reducing fat, losing weight, increasing satiety,
or a feeling of fullness, and retaining muscle.

However, consuming high amounts of any nutrient for a long period of time typically comes with risks, as
can be the case with protein. Overconsumption may lead to an increased risk of certain health
complications, according to research, such as weight gain, bad breath, constipation, diarrhea,
dehydration, kidney damaged, increase risk of cancer, heart disease and calcium loss.

2. Which of the following foods has the greatest amount of protein: A cup of milk or 3 oz of meat?

Ans: To compare protein sources, a 3-ounce piece of meat has about 21 grams of protein. In contrast, 1
cup of milk has 8 grams of protein, 1 cup of dry beans has about 16 grams of protein, and an 8-ounce
container of yogurt has about 11 grams of protein. Together, these food sources provide 56 grams of
protein, which is enough for an adult male. It is best to choose the overall diet based on a balanced
approach to include other nutrients.

KEY TO CORRECTIONS

A. FILL IN THE TABLE BELOW: Using the clues, fill in the table below with the needed three (3) letter
abbreviation, symbol, polarity, classification as essential or nonessential, and function (1) of the amino
acids being asked.

3 letter Symbol Polarity Essential or Function (1 only)

nonessential
Necessary for the synthesis of neurotransmitter serotonin (5-
hydroxytryptamine). A natural relaxant, helps alleviate insomnia
by inducing normal sleep; reduces anxiety and depression.
Trp W Nonpolar Essential -Can be metabolized to niacin Vit. B3 if needed
-Used to synthesized melatonin (5-methoxy-N-
acetyltryptamine)

Promotes healthy brain function. It is also

Polar
Gln N Nonessential necessary for the synthesis of RNA and DNA
Neutral molecules.

Lys K Polar basic Essential Increases calcium absorption

Essential for baby Blood vessel relaxation, maintain erection in

Arg R Polar basic but not for adult men, removal of excess ammonia

This document is the property of PHINMA EDUCATION P a g e | 34

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

B. PEPTIDE FORMATION and NOMENCLATURE:

1. Name the peptides based on the IUPAC rules. 2. Identify the amino acids in the peptide
and name it using the IUPAC rules.

Ans. Arginylhistidylthreonylglutamylserine Ans:Tryptophylglycylglycylphenylalanylmethionine

C. MATCHING TYPE: Write only the letter of the correct answer

C.1 LEVEL OF STRUCTURAL ORGANIZATION: Using the phrases, statement and examples, fill in the table
that corresponds to the structural characteristics of proteins. Answers may be repeated.

PRIMARY SECONDARY TERTIARY QUATERNARY

B,D,E,F,O A,F,G,H,P A,F,G,I,J,M

C,K,L.N

C.2 BONDS OF PEPTIDE

1. A 2.B 3.D 4.B 5.A 6.D 7.D 8.C 9.B 10.A

C.3 Based on chemical composition

1. A 2.B 3.B 4.A 5.A 6.A 7.C 8.C 9.C 10.B

C.4 Based on type of conjugated protein C.5 Based on type of conjugated protein
1. D 2.A 3.C 4.B 5.F 1.A 2.B 3.A 4. B 5.A

C.6 Based on function

Column A Column B

This document is the property of PHINMA EDUCATION P a g e | 35

 Course Code: BIO 073 (Biochemistry/Biomolecules)
Student Activity Sheet Module #3

Name: _____________________________________________________________ Class number: _______

Section: ____________ Schedule:_____________________________________ Date: ________________

1.A 2.D 3.E 4.H 5.F 1.D 2.F 3.C 4.G 5.B

6.C 7.G 8.B 9.B 10.A 6.A 7.E 8.H 9.E 10.C

C.7 Protein related disorder

1.G 2.C 3.A 4.D 5.B 6.E

D. Case Analysis

1. Marasmus
2. Signs and Symptoms are the following: Weight is less than 60% of the normal (expected) body weight
for the age, good appetite despite of the low body weight, Alert and irritable mood, Absence of edema

SUGGESTED VIDEOS:
https://www.youtube.com/watch?v=HSCUAjZQhXI&t=11s
https://www.youtube.com/watch?v=652GrZpLkPs

PROTEINS and PROTEIN RELATED DISORDERS SUGGESTED VIDEOS:

▪ Hierarchy of protein structure: https://www.youtube.com/watch?v=hok2hyED9go
▪ Protein energy malnutrition: https://www.youtube.com/watch?v=u8isLgQfO_M
You may also watch Jessica soho features KWASHIORKOR
▪ Amyloidosis: https://www.youtube.com/watch?v=j962b8ZdU8w
▪ Prion disease: https://www.youtube.com/watch?v=dXcLb4oCYfg
▪ Sickle cell anemia: https://www.youtube.com/watch?v=fIIJmg_1hv0
▪ Beta Thalassemia: https://www.youtube.com/watch?v=oH6SMG3Ykjg
▪ Methemoglobinemia: https://www.youtube.com/watch?v=C5VQEhKmBQg
▪ Osteogenesis imperfecta: https://www.youtube.com/watch?v=JA5ap43iFrQ (you may watch Jessica soho
featured case in the Philippines)
▪ Ehlers Danlos: https://www.youtube.com/watch?v=cPpl2cxjBuA
▪ Alpha1-antitrypsin deficiency: https://www.youtube.com/watch?v=pXR0RpMMrfk

This document is the property of PHINMA EDUCATION P a g e | 36