ST.

JOHN PAUL II COLLEGE OF DAVAO

COLLEGE OF NURSING
Physically Detached Yet Academically Attached

COLLEGE OF NURSING

SIMPLIFIED COURSE PACK (SCP) FOR SELF-

DIRECTRED LEARNING

BIOCHEMISTRY

This Simplified Course Pack (SCP) is a draft version only and may not
be used, published or redistributed without the prior written consent of
the Academic Council of SJPIICD. Contents of this SCP is only intended
for the consumption of the students who are officially enrolled in the
course/subject. Revision and modification process of this SCP are
expected.

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 ST. JOHN PAUL II COLLEGE OF DAVAO

COLLEGE OF NURSING
Physically Detached Yet Academically Attached

COLLEGE OF NURSING

By 2023, a recognized professional institution providing quality,

Vision
economically accessible, and transformative education grounded on
the teachings of St. John Paul II.

Serve the nation by providing competent JPCean graduates through

quality teaching and learning, transparent governance, holistic
Mission
student services, and meaningful community-oriented researches,
guided by the ideals of St. John Paul II.

● Respect
● Hard Work
● Perseverance
Core Values
● Self-Sacrifice
● Compassion
● Family Attachment

● Inquisitive
● Ingenious
Graduate Attributes
● Innovative
● Inspiring
Course Code/Title MC 2 / BIOCHEMISTRY
This course deals with the rational approach in studying biochemistry the correlation of
Course Description the structure of biomolecules and related systems with their functions and biochemical
reactions.
Course Requirement
Time Frame 102 Hours
Grading System “Based 40” Cumulative Averaging Grading System

Contact Details
Instructor Zajada C. Balono, RN, MN (09162620411)
Dean/Program Head Emalyn D. Santiesteban (09161985269)

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 ST. JOHN PAUL II COLLEGE OF DAVAO

COLLEGE OF NURSING
Physically Detached Yet Academically Attached

Course
COLLEGE OFMap
NURSING

MC 2- Simplified Course Pack (SCP)

SCP-Topics: Prelim Period SCP- Topics: Midterm Period SCP- Topics: Final Period

Week 1 The nature of biochemistry Week

Week 7 Digestion Midterm Examination
13

Week 2 Carbohydrates Week

Week 8 Metabolism of Carbohydrate Body fluid : Blood
14

Week 3 Lipids Week

Week 9 Metabolism of Fat Vitamins
15

Week 4 Proteins Week

Week 10 Metabolism of Protein Hormones
16

Week 5 Nucleic Acids Week

Week 11 Body fluids : Urine Immunochemistry
17

Week 6
Enzymes Midterm Examination Week
Week 12 Final Examination
Preliminary Examination (Holy Week) 18

Course Outcomes

1. Develop the appreciation on the structure- functional relationship of the different

biomolecules which allow them some vital functions in the human system.
2. Relate the different biochemical metabolisms to the varied provisions for the
utilization of complex food substances for the biosynthesis of biomolecules and
energy production.
3. Be familiar with the clinical applications of biochemistry having a full grasp in the
different metabolic pathways and regulations.
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COLLEGE OF NURSING
Physically Detached Yet Academically Attached

Welcome Aboard! ThisCOLLEGEcourse OFprovides

NURSINGthe students with the
application of nursing as a science, an art, vocation and a
profession. It deals with the concept of a man as a holistic being
comprised of bio-psychosocial and spiritual dimension. It includes a
discussion on the different roles of a nurse emphasizing health
promotion maintenance of health as well as prevention of illness
utilizing the nursing process. It includes the basic nursing skills
needed in the care of individual client.

SCP-TOPICS: PRELIM PERIOD TOPICS

Week 4 PROTEINS

1. The nitrogen cycle.

Lesson Title 2. Sources and functions.
3. Amino acids and its structure and composition.
4. Classification and properties.

1. Become familiar with the structures and reactions of

amino acids.
2. Indicate the classification of proteins according to
solubility, composition, function and shape.
Learning Outcome(s)
3. Draw the structures of dipeptides.
4. Describe the primary, secondary, and tertiary
structures of protein.
5. Understand the significance of protein denaturation.

Time Frame LEC 54 Hours ( 3 units ); LAB 108 Hours ( 2 units )

At SJPIICD, I Matter!
LEARNING INTENT!
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COLLEGE OF NURSING
Physically Detached Yet Academically Attached

This section provides meaning and

COLLEGE definition of the terms that are
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important to better understand the concepts specified in the course
pack of Biochemistry.
Terms to Ponder

Proteins are a primary constituent of living things and one

of the chief classes of molecules studied in biochemistry.
Proteins provide most of the molecular machinery of cells.

Essential Content
Proteins
 Proteins are the most abundant biological
macromolecules, occurring in all cells.
 It is also the most versatile organic molecule of the
living systems and occur in great variety; thousands of
different kinds, ranging in size from relatively small
peptides to large polymers.
 Proteins are the polymers of amino acids covalently
linked by the peptide bonds.
 The building blocks of proteins are the twenty
naturally occurring amino acids.
 Thus, proteins are the polymers of amino acids.

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Properties of Proteins
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Solubility in Water
 The relationship of proteins with water is complex.
 The secondary structure of proteins depends largely on
the interaction of peptide bonds with water through
hydrogen bonds.
 Hydrogen bonds are also formed between protein
(alpha and beta structures) and water. The protein-
rich static ball is more soluble than the helical
structures.
 At the tertiary structure, water causes the orientation
of the chains and hydrophilic radicals to the outside of
the molecule, while the hydrophobic chains and
radicals tend to react with each other within the
molecule (hydrophobic effect).
Denaturation and Renaturation
 Proteins can be denatured by agents such as heat and
urea that cause unfolding of polypeptide chains
without causing hydrolysis of peptide bonds.
 The denaturing agents destroy secondary and tertiary
structures, without affecting the primary structure.
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 If a denatured protein returns

COLLEGE to its native state after
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the denaturing agent is removed, the process is called

renaturation.

Some of the denaturing agents include :

Physical agents: Heat, radiation, pH
Chemical agents: Urea solution which forms new
hydrogen bonds in the protein, organic solvents,
detergents.

Coagulation
When proteins are denatured by heat, they form insoluble
aggregates known as coagulum. All the proteins are not
heat coagulable, only a few like the albumins, globulins are
heat coagulable.

Isoelectric point
 The isoelectric point (pI) is the pH at which the
number of positive charges equals the number of
negative charges, and the overall charge on the amino
acid is zero.
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 At this point, when subjected

COLLEGE to an electric field the
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proteins do not move either towards anode or cathode,

hence this property is used to isolate proteins.

Molecular Weights of Proteins

 The average molecular weight of an amino acid is
taken to be 110.
 The total number of amino acids in a protein
multiplied by 110 gives the approximate molecular
weight of that protein.
 Different proteins have different amino acid
composition and hence their molecular weights differ.
 The molecular weights of proteins range from 5000 to
109 Daltons.
Posttranslational modifications
 It occurs after the protein has been synthesized on the
ribosome.
 Phosphorylation, glycosylation, ADP ribosylation,
methylation, hydroxylation, and acetylation affect the
charge and the interactions between amino acid

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residues, alteringCOLLEGE
the three-dimensional
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and, thus, the function of the protein.

Chemical Properties
1. Biuret test:
When 2 ml of test solution is added to an equal volume of
10% NaOH and one drop of 10% CuSO4 solution, a violet
colour formation indicates the presence of peptide linkage.
2. Ninhydrin test:
When 1 ml of Ninhydrin solution is added to 1 ml protein
solution and heated, formation of a violet colour indicates
the presence of α-amino acids.

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COLLEGE OF NURSING
Physically Detached Yet Academically Attached

Protein Structure COLLEGE OF NURSING

 The linear sequence of amino acid residues in a

polypeptide chain determines the three-dimensional
configuration of a protein, and the structure of a
protein determines its function.
 All proteins contain the elements carbon, hydrogen,
oxygen, nitrogen and sulfur some of these may also
contain phosphorus, iodine, and traces of metals like
ion, copper, zinc and manganese.
 A protein may contain 20 different kinds of amino
acids. Each amino acid has an amine group at one end
and an acid group at the other and a distinctive side
chain.
 The backbone is the same for all amino acids while the
side chain differs from one amino acid to the next.
The structure of proteins can be divided into four levels of
organization:
1. Primary Structure
 The primary structure of a protein consists of the
amino acid sequence along the polypeptide chain.
 Amino acids are joined by peptide bonds.
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 Because there are no dissociable

COLLEGE protons in peptide
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bonds, the charges on a polypeptide chain are due

only to the N-terminal amino group, the C-terminal
carboxyl group, and the side chains on amino acid
residues.
 The primary structure determines the further levels of
organization of protein molecules.
2. Secondary Structure
 The secondary structure includes various types of local
conformations in which the atoms of the side chains
are not involved.
 Secondary structures are formed by a regular
repeating pattern of hydrogen bond formation between
backbone atoms.
 The secondary structure involves α-helices, β-sheets,
and other types of folding patterns that occur due to a
regular repeating pattern of hydrogen bond formation.
 The secondary structure of protein could be :
1. Alpha-helix
2. Beta-helix
 The α-helix is a right-handed coiled strand.
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 The side-chain substituents of the amino acid groups

COLLEGE OF NURSING

in an α-helix extend to the outside.

 Hydrogen bonds form between the oxygen of the C=O
of each peptide bond in the strand and the hydrogen of
the N-H group of the peptide bond four amino acids
below it in the helix.
 The side-chain substituents of the amino acids fit in
beside the N-H groups.
 The hydrogen bonding in a ß-sheet is between strands
(inter-strand) rather than within strands (intra-
strand).
 The sheet conformation consists of pairs of strands
lying side-by-side.
 The carbonyl oxygens in one strand hydrogen bond
with the amino hydrogens of the adjacent strand.
 The two strands can be either parallel or anti-parallel
depending on whether the strand directions (N-
terminus to C-terminus) are the same or opposite.
 The anti-parallel ß-sheet is more stable due to the
more well-aligned hydrogen bonds.
3. Tertiary Structure
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 Tertiary structureCOLLEGE
of a protein refers to its overall
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three-dimensional conformation.
 The types of interactions between amino acid residues
that produce the three-dimensional shape of a protein
include hydrophobic interactions, electrostatic
interactions, and hydrogen bonds, all of which are
non-covalent.
 Covalent disulfide bonds also occur.
 It is produced by interactions between amino acid
residues that may be located at a considerable
distance from each other in the primary sequence of
the polypeptide chain.
 Hydrophobic amino acid residues tend to collect in the
interior of globular proteins, where they exclude water,
whereas hydrophilic residues are usually found on the
surface, where they interact with water.
4. Quaternary Structure
 Quaternary structure refers to the interaction of one or
more subunits to form a functional protein, using the
same forces that stabilize the tertiary structure.

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 It is the spatial arrangement of subunits in a protein

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that consists of more than one polypeptide chain.

Classification of Proteins
Based on the chemical nature, structure, shape and
solubility, proteins are classified as:
1. Simple proteins: They are composed of only amino
acid residue. On hydrolysis these proteins yield only
constituent amino acids. It is further divided into:
 Fibrous protein: Keratin, Elastin, Collagen
 Globular protein: Albumin, Globulin, Glutelin,
Histones
2. Conjugated proteins: They are combined with non-
protein moiety. Eg. Nucleoprotein, Phosphoprotein,
Lipoprotein, Metalloprotein etc.
3. Derived proteins: They are derivatives or degraded
products of simple and conjugated proteins. They may
be :
 Primary derived protein: Proteans, Metaproteins,
Coagulated proteins
 Secondary derived proteins: Proteosesn or
albunoses, peptones, peptides.
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COLLEGE OF NURSING
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Functions of Proteins
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Proteins are vital for the growth and repair, and their
functions are endless. They also have enormous diversity of
biological function and are the most important final
products of the information pathways.
 Proteins, which are composed of amino acids, serve in
many roles in the body (e.g., as enzymes, structural
components, hormones, and antibodies).
 They act as structural components such as keratin of
hair and nail, collagen of bone etc.
 Proteins are the molecular instruments through which
genetic information is expressed.
 They execute their activities in the transport of oxygen
and carbon dioxide by hemoglobin and special
enzymes in the red cells.
 They function in the homostatic control of the volume
of the circulating blood and that of the interstitial
fluids through the plasma proteins.
 They are involved in blood clotting through thrombin,
fibrinogen and other protein factors.

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 They act as the defense

COLLEGEagainst infections by means of
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protein antibodies.
 They perform hereditary transmission by
nucleoproteins of the cell nucleus.
 Ovalbumine, glutelin etc. are storage proteins.
 Actin, myosin act as contractile protein important for
muscle contraction.

SELF-SUPPORT: You can click the URL Search Indicator below to help you further understand the lessons.

Search Indicator
https://en.wikibooks.org/wiki/Biochemistry/Proteins

https://microbenotes.com/proteins-properties-structure-classification-
and-functions/

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