BIOCHEMISTRY

BIOCHEMISTRY
LESSON: PROTEIN
WHAT IS PROTEIN? -​ Nutritional Value

●​ The word protein is derived 1.)Size and Shape

from the Greek word, ●​ Fibrous proteins
"proteios" which means -​ are proteins that are insoluble
primary. and have long, thread-like, or
●​ Proteins are large, complex rod-shaped structures.
molecules made up of -​ They are usually arranged in
smaller units called amino parallel chains and are tightly
acids that are linked together packed together, which
by peptide bonds. makes them very strong and
resistant to stretching.
CHARACTERISTIC OF -​ Examples:
Collagen – The most
PROTEIN abundant in all protein in
●​ Proteins are organic humans ( 30% of total body
compounds made up mainly protein). It is found in
of carbon (C), hydrogen (H), connective tissues such as
oxygen (O), and nitrogen (N). skin and cartilage. Collagen is
●​ Nitrogen is characteristic of what makes skin firm and
proteins. what gives strength to
●​ A protein is a long chain tendons.
made of 40 or more of the 20 Keratin – found in hair,
standard a-amino acids. nails, feathers, horns, and the
●​ Proteins are easily affected by outer layer of skin. Keratin
changes in temperature, pH, protects cells and tissues
or chemicals. This is called from damage.
denaturation. Elastin – found in
ligaments and tissues that
CLASSIFICATION OF need elasticity. It provides
PROTEIN flexibility.
●​ Classification of Protein:
Note: For a protein to be
-​ Size & shape
considered fibrous, it must be
-​ Solubility and composition
-​ Function
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insoluble in all kinds of
solvents.
●​ Conjugated Proteins
-​ Combination of proteins with
●​ Globular proteins
a non-protein part that can
-​ are proteins whose be an organic and inorganic,
polypeptide chains are folded called prosthetic group.
into a compact, rounded, and -​ Examples
spherical shape.
-​ They are usually soluble in
water.
-​ Globular proteins are
functional proteins. They are
actively involved in
metabolism and chemical
processes in the body.
-​ Examples:
Enzymes – such as
amylase or pepsin, which
speed up chemical reactions ●​ Derived Proteins
in digestion and metabolism. -​ Derived proteins are proteins
Hemoglobin, the protein that have been altered
in red blood cells that carries (changed) by heat, acids,
oxygen from the lungs to the alkalis, or enzymes.
tissues. -​ They include two types of
derivatives.
2.) Based on solubility and 1.​ Primary derived proteins:
composition -​ Proteins that have been
●​ Simple Proteins slightly altered from their
-​ made of only amino acids original form by physical or
-​ Examples: chemical agents, such as
water, dilute acids, alkalis,
enzymes, etc. They can
appear in three forms:
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Protein 3.) Classification of Proteins based
↓ on Function
Protean: formed by water, dilute acids, or enzymes;
insoluble in neutral solvents.
Catalytic Proteins – Enzymes
(Acids, alkalis) -​ Speed up chemical reactions
↓ in the body.
-​ They ensure that important
Metaprotein: formed when acids or alkalis act on
proteins; insoluble in neutral solvents. processes like digestion,
(Heat, alcohol)
energy production, and DNA
replication occur quickly and
↓
enough to sustain life.
Coagulated protein: formed by heat or alcohol. -​ Examples: Amylase, lipase,
and DNA polymerase.
2.​ Secondary-derived protein
-​ are the products formed
Regulatory Proteins
when proteins undergo
progressive hydrolysis. -​ (Hormones). These are
-​ Unlike primary-derived polypeptides and small
proteins that are only slightly proteins found in relatively
modified, secondary- derived lower concentrations in the
proteins are already degraded animal kingdom, but play an
into soluble forms. important regulatory role in
Protein maintaining order in
(progressive hydrolysis) metabolic reactions.
↓
Proteoses: Are hydrolytic products of proteins,
-​ Examples: growth hormone
which are soluble in water and are not coagulated and insulin.
by heat.
↓ Protective Proteins
Peptones: Peptones are hydrolytic products, which
have simpler structure than proteoses. They are -​ (Antibodies)
soluble in water and are not coagulated by heat. -​ Some proteins have a
↓
Peptides: Peptides are composed of relatively few protective defense function.
amino acids. They are water-soluble and not These proteins combine with
coagulated by heat.
↓
foreign substances and fight
Amino acids against diseases.
-​ Examples: Immunoglobulins
(antibodies) and fibrin in
blood.
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Storage Proteins glycoproteins present in their
bodies.
-​ These proteins function as
-​
reserves of amino acids and
nutrients for growing tissues. 4.) Classification of Proteins Based
-​ Examples: Albumin of egg, on Nutritional Value
casein of milk, globulins in
●​ Nutritionally Rich Proteins
pulses, and glutelins in
-​ They are also called complete
cereals.
proteins or first-class
Transport Proteins proteins. They contain all the
essential amino acids in the
-​ These proteins are capable of
required proportion. By
binding and transporting
supplying these proteins in
molecules through the blood.
the diet, children will grow
-​ Examples: hemoglobin
satisfactorily.
(transports oxygen),
-​ Example: meat, fish, and
myoglobin (stores oxygen in
Casein of milk
muscle).
●​ Incomplete Proteins
Structural Proteins -​ They lack one essential amino
-​ Some proteins serve as acid. They cannot promote
structural materials or as body growth in children, but
components of cellular fluid. may be able to sustain body
-​ Examples: Myosin of muscles, weight in adults.
keratin of skin and hair, and -​ Proteins from pulses are
collagen of connective tissue. deficient in methionine, while
proteins of cereals lack lysine.
Contractile Proteins If both of them are combined
-​ Proteins like actin and myosin in the diet, adequate growth
function as essential elements may be obtained.
in the contractile system of -​ Example: Proteins from
skeletal muscle. beans, cereals, grains.
●​ Poor Proteins
Exotic Proteins -​ They lack many essential
-​ Antarctic fishes live in waters amino acids and a diet based
below freezing temperatures. on these proteins will not
-​ These fishes are prevented even sustain the original body
from freezing by antifreeze weight.
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-​ Example: Zein from corn,
which lacks tryptophan and
lysine.

PROTEIN STRUCTURE
●​ PRIMARY STRUCTURE
-​ Refers to the specific
sequence of amino acids in a
protein which amino acids are
linked together. -​ 2. Beta pleated sheet (b
-​ Contain all the information pleated sheet) – Looks like a
necessary for the order of folded sheet of paper;
higher structures. Hydrogen bonds form
-​ EXAMPLE: Insulin, first between different segments
protein with a determined of the chain lying
primary structure; composed side-by-side.
of 51 amino acids and 2
chains.
●​ SECONDARY STRUCTURE
-​ form by hydrogen bonds
-​ Arrangement in space
adopted by the backbone
portion of a protein repeating
pattern of folding.
-​ Helps determine the overall
-​
shape and function of the
●​ TERTIARY STRUCTURE
protein.
-​ Three-dimensional(3D) shape
-​ The folding depends on
that results from the
amino acid arrangement
interaction between Amino
-​ It has 2 COMMON TYPES
Acid Chain (R group)
-​ 1. Alpha helix (a-helix) – spiral
-​ Held together by disulphide
staircase shape; hydrogen
bridges and ionic bond
bonds form between every
-​ It has 4 types of stabilizing
4th amino acid.
interactions to the Tertiary
structure of a protein:
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1. Covalent Disulfide bonds 2. Electrostatic interactions
-​ Only interactions that involve -​ Also called salt bridges
Covalent bonds. -​ Involves ionic bond
-​ The strongest of the -​ Always involves an interaction
Tertiary-structure between (R group), acidic
interactions. side chain and basic side
-​ Results from the SH groups of chain.
two cysteine residues -​ The R group carries charges
reacting with each other. with the acidic side chain
being negatively charged and
the basic side chain being
positively charged.
-​ Electrostatic between
Glutamic acid and Lysine:

-​ Formation of Disulfide bond Glutamic acid

Intramolecular Disulfide
bond – Involves two(2)
cysteine units in the same
peptide chain
Intermolecular Disulfide
bond – Involves two(2)
cysteine units in different
chains. Lysine

3. Hydrogen bonds
-​ Occurs between Amino acids
with Polar R groups.
Ex. Human hormone insulin -​ The Polar R group is pointing
outward, toward an aqueous
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solvent in an aqueous solution Protein Tertiary structure of
which is also polar. Myoglobin
-​ Relatively weak and easily
-​ Conjugated protein
disrupted by changes in pH
-​ Oxygen storage in muscle
and temperature.
tissue
-​ Hydrogen bonds interactions
-​ Single peptide chain of 153
between Glutamine and
amino acids with numerous
serine:
helix segments within the
chain
-​ Contains the PROSTHETIC
HEME group, the iron
containing group that bind
molecular oxygen.

4. Hydrophobic Interactions
-​ Weaker than hydrogen bonds
and Electrostatic interactions.
-​ Results when two nonpolar
side chains are close to each ●QUATERNARY STRUCTURE
other. The non-polar R group
is pointing inward, away from -​ Three-dimensional shape of
aqueous solvent(polar) in protein that involves two or
aqueous solution. more multipeptide subunits
-​ Hydrophobic Interactions that are independent to each
between R group of other.
phenylalanine and leucine: -​ Highest level of protein
organization that is only
found in multimeric protein.
-​ Not covalently bonded
-​ Held together by hydrophobic
interactions that are
particularly important as well
as electrostatic interaction
and hydrogen bonds that are
weaker and can easily
disrupt.
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-​ Quaternary Structure of acids or bases, alcohol, heavy
Hemoglobin: metals, or radiation.
-​ During denaturation, the
Oxygen carrying protein in blood
secondary, tertiary, and
-​ Tetramer quaternary structures of the
-​ Two identical a subunits protein are destroyed, but
-​ Two identical b subunits the primary structure —
-​ a heme group which is the sequence of
amino acids — remains
unchanged.

●​ Chemical Properties
-​ Color Reactions of Proteins -
Proteins can be detected
through special color
reactions. When certain
PROPERTIES OF A PROTEIN chemicals are added, proteins
●​ Physical Properties change color because of the
-​ Pure proteins are generally way the chemicals react with
tasteless, though the their amino acids.
predominant taste of protein -​ Biuret Reaction - A
hydrolysates is bitter. compound, which has more
-​ Pure proteins are odorless. than one peptide bond, when
-​ Because of the large size of treated with Biuret reagent,
the molecules, proteins produces a violet color.
exhibit many properties that ●​ Xanthoproteic Reaction -
are colloidal in nature. -​ When concentrated nitric acid
-​ Proteins, like amino acids, are is added to a protein and
amphoteric and contain both heated, it turns yellow, then
acidic and basic groups. orange when made alkaline.
-​ Denaturation, the process in Nitric acid also stains the skin
which a protein loses its yellow by reacting with its
natural three-dimensional proteins.
structure due to external ●​ Hydrolysis-is the process
factors such as heat, strong where proteins are broken
down into smaller units called
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amino acids. This cuts the
peptide bonds that hold
amino acids together. This is
done with the help of water
and enzymes like pepsin,
trypsin, and chymotrypsin.

References
Vij, J. P. (2025). Textbook of biochemistry: For medical students (6th ed.). Jaypee
Brothers Medical Publishers.
Albalaha. (2014). Fundamentals of Biochemistry. Retrieved
[Link]
Rentals-of-biochemistry

MADE BY
Millan, Raiven Darhleen
Badar, Gennielyn
Cando, Gian
Casita, Angelica
Enriquez, Valerie
Pascua, Hilary
Mana Raiza
Miranda, Angelica
Reyes, Keyt Lyanne