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CARBOHYDRATES-

is a naturally occurring compound, or a

derivative of such a compound, with the
general chemical formula Cx(H2O)y, made up
of molecules of carbon (C), hydrogen (H),
and oxygen (O).
CARBONYL GROUP(-OH)

is a functional group composed of a carbon atom

double-bonded to an oxygen atom.
HYDROXYL GROUP(-OH)

are a functional group found in sugars and

alcohols. A hydroxyl group consists of one
hydrogen and one oxygen atom and can be
written as either -OH or HO-. Hydroxyl groups
are polar, and the oxygen side is always negative,
while the hydrogen side is always positive.
Fischer projection-
method of representing the three-
dimensional structures of molecules on a
page, devised by Emil Fischer.

Key Features of the Fischer Projection:

Vertical and Horizontal Lines-
Carbon Backbone:
Chirality-
Haworth projection-
is a common way of writing a structural
formula of sugars (monosaccharides and
disaccharides) in a three-dimensional
perspective or cyclical form.
How to Draw a Hayworth Projection?
How to Draw a Hayworth Projection?
How to Draw a Hayworth Projection?
Aldose- carbonyl group is on the C1
carbon, forming an aldehyde group.

The carbonyl group (C=O) is located at

the terminal carbon (carbon 1).

The aldehyde can be oxidized via a

redox reaction in which another
compound is reduced. Thus, aldoses
are reducing sugars.
Glucose (C₆H₁₂O₆) → Gluconic Acid (C₆H₁₂O₇)
KETOSE- ketone is an organic
compound that contains a
carbonyl group (C=O) located
within the carbon chain.
ISOMERS- Chemical
compounds that have identical
chemical formula but differ in
properties and the
arrangement of atoms in the
molecule.

C6H12O6
Polymers – are long chain,
giant organic molecules are
assembled from many smaller
molecules called monomers.
Polymers consist of many
repeating monomer units in
long chains, sometimes with
branching or cross-linking
between the chains
Pyranose – is sugar molecule
that has a six-membered ring
structure, consisting of five
carbon atoms and one oxygen
atom
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During the process hydroxyl
group of one monosaccharide
combines with the hydrogen of
another monosaccharide,
releasing a molecule of water
and forming a covalent bond
called glycosidic bond.
✓ is a type of chemical bond
where two atoms share one
or more pairs of electrons to
achieve stability

✓ are generally strong and

require significant energy to
break.
✓ This a process of adding a hydroxyl group (-OH) to one molecule and
a hydrogen atom (H) to another, breaking the bond.

✓ water is used to break the bond ("hydro" means water, "lysis" means
breaking).
Amylose or Starch - is a polysaccharide made of
α-D-glucose units, bonded to each other
through α(1→4) glycosidic bonds.

The number of repeated glucose subunits

(n) is usually in the range of 300 to 3000,
but can be many thousands.

Is the stored form of glucose in plants (e.g.,

potatoes, rice, wheat).
Glycogen is the stored form of glucose in
animals, found in the liver and muscles.
Cellulose - forms the cell wall surrounding
every plant cell.

It is the most common organic compound in

nature, but humans cannot digest it. Key
component of dietary fiber

The size of cellulose molecules depends on

the degree of polymerization and may vary
from 7000 to 14,000.
Cellulose - forms the cell wall surrounding
every plant cell.

It is the most common organic compound in

nature, but humans cannot digest it. Key
component of dietary fiber

The size of cellulose molecules depends on

the degree of polymerization and may vary
from 7000 to 14,000.
Cellulose - molecules depends on the degree
of polymerization and may vary from 7000
to 14,000.

forms the cell wall surrounding every plant cell.

It is the most common organic compound in

nature, but humans cannot digest it. Key
component of dietary fiber.
Cellulose – Ruminants (cows, horses, goats)
have four-chambered stomachs that break down
cellulose with the help of enzymes and bacteria.
Chitin – second most common polysaccharide in
nature.

Found in the cell walls of fungi and the

exoskeletons of insects, spiders, and crustaceans

It is used in the manufacture of surgical

materials due to its unique properties.
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Molecular structure, which consists mainly of
long chains of carbon-carbon (C-C) and
carbon-hydrogen (C-H) bonds

Both C-C and C-H bonds are nonpolar,

meaning there is no significant difference in
electronegativity between the atoms involved.
As a result, lipids do not dissolve in water and
instead clump together in aqueous solutions,
forming droplets or separating into layers
Polar molecules, like water (H₂O), have
regions where the electrons are unevenly
shared between atoms due to differences in
electronegativity.

In water, the oxygen atom pulls electrons

more strongly than the hydrogen atoms, giving
the oxygen a partial negative charge (δ⁻) and
the hydrogen atoms a partial positive charge
(δ⁺).
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Fats are energy-storing lipids. They are also
known as triacylglycerols or triglycerides and
have two main components:

Glycerol- three-carbon molecule that forms

the backbone of the fat.

Three fatty acids- Long chains of hydrocarbons

(carbon and hydrogen atoms) that attach to
the glycerol.
ESTER BOND- Chemical bond formed when a
carboxyl group (-COOH) of an acid reacts with
a hydroxyl group (-OH) of an alcohol, releasing
water in a process called condensation. This
bond is commonly found in fats (like
triglycerides) and polymers.
✓ Do not have double bond on hydro cardon
chain.
✓ They are easily saturated with hydrogen
molecules leading to a maximum number
of hydrogen atoms
✓ Are straight and are tightly packed against
each other.
✓ Typically, solid.
✓ may increase the risk of cardiovascular
diseases
✓ have one or more double bonds between
carbon atoms leading to a fewer hydrogen
atoms.
✓ Low melting point.
✓ Examples of unsaturated fatty acids are
oleic(-) and linoleic acid(=)
✓ Dietary Fat- cooking oils like olive oil, canola
oil, and peanut oil, omega-6 fatty acid,
✓ moisturizers, creams, and soaps
Monounsaturated- with only one double bond
in a fatty acid. Ex. r oleic acid

Polyunsaturated- there are multiple double

bonds.
✓ Trans fat is created through partial
hydrogenation of unsaturated fats in
vegetable oils.
✓ During the partial hydrogenation changes
some of the cis double bonds (where
hydrogens are on the same side) to trans
double bonds
✓ This process makes the fat chemically
resemble saturated fat.
Margarine-
✓ structure is similar to a triglyceride, typically
consist of fatty acid chains attached to a
glycerol backbone. However, instead of
having three fatty acid tails, phospholipids
generally have only two, and a modified
phosphate group occupies the third carbon
of the glycerol backbone
✓ Are the main components of cell
membranes. These cell membranes are
dynamic, fluid membranes with embedded
or attached proteins and carbohydrates.
are very different from fats and
phospholipids in that they are composed
of four fused rings. These are the
building block of the Steroids.

cyclopentanoperhydrophenanthrene

Despite the difference in structure, they

are classified as lipids because they are
nonpolar and hydrophobic.
Cholesterol is a common steroid found in
animal-based foods such as meat, fish,
and eggs.

Animal cells use cholesterol to produce

other lipids, including vitamin D and the
sex hormones testosterone and
estrogen.
Waxes are simple lipids composed of a
long chain of alcohol bonded to a fatty
acid by an ester bond. In plants, cuticles
are made up of waxes. Cuticles are
protective coatings of plants to prevent
water loss. Bees also produce wax to
store honey and eggs. More commonly,
your ears have wax that protects them
from infection.
•Proteins
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• The most diverse among biomolecules
in terms of structure and function,
proteins.
• They do the most work in the cell, from
degradation to homeostasis.
• Proteins are large, complex, nitrogenous
biomolecules that are made up of
smaller units called amino acids.
• Proteins are synthesized in cells through
a process called translation.
• is the building block of a protein.
• It is composed of an alpha
carbon, an amino group (-NH2),
a carboxyl group (-COOH), and a
side chain.
• The side chain can be an atom or
a group of atoms and is also
called the R group.
• When two or more amino acids
are combined, they form a
peptide.
• Amino acids are joined together
by covalent bonds called peptide
bonds
• During peptide bonding, the
carboxyl group of one amino
acid and the amino group of the
other amino acid combine
• Peptide bond is formed between
amino acids through dehydration
process.
• As more amino acids are added,
the growing chain is referred to as
a polypeptide.
• A protein is defined as at least one
polypeptide chain with a unique
molecular structure and function.
Primary Structure
• The primary structure of a
protein is the sequence of
amino acids it has, which is
determined by the DNA
through the processes of
transcription and translation.
Transcription
✓ Converts DNA into messenger
RNA (mRNA).
✓ Occurs in the nucleus
✓ The mRNA serves as a copy of
the genetic instructions encoded
in DNA.
✓ A single-stranded mRNA
molecule, which carries the
genetic code from DNA to the
ribosome for protein synthesis.
Translation
✓ Converts mRNA into a protein
(sequence of amino acids).
✓ Occurs in the ribosome
✓ The mRNA serves as a copy of
the genetic instructions encoded
in DNA.
✓ The ribosome reads the mRNA
codons and matches them with
tRNA molecules that bring the Transcription = DNA → mRNA (copying genetic instructions).
Translation = mRNA → Protein (building the functional product).
corresponding amino acids.
“What happens to a protein when it
folds incorrectly?”
What are the implications of
misfolded proteins in diseases such as
Alzheimer’s?”
 SECONDARY STRUCTURE
✓ formed from the interactions
among adjacent amino acids.
✓ This structure is formed by the
hydrogen bonds between the local
groups of these amino acids.
✓ The usual structures formed are
the α-helix and β-pleated sheet
structures.
TERTIARY STRUCTURE
✓ Refers to its three-dimensional
(3D) conformation. This structure
is formed by interactions among
the side chains of amino acids
when several secondary
structures come together. If a
protein loses its 3D structure, it
will lose its function.
TERTIARY STRUCTURE
✓ Affected by the pattern of polar and
Non-Polar Amino Acids, in the
polypeptide chain which determines
the final chain confirmation.
✓ Hydrophobic such as non polar side
chains amino acids found in the
interior proteins. Polar amino bond
with the external hydrogen or H2O
around the proteins.
QUATERNARY STRUCTURE
Some proteins are composed of subunits
of polypeptide chains. For example, the
protein insulin is composed of two
polypeptide chains. How these subunits
of polypeptide chains are oriented or
arranged together is what the
quaternary structure shows. Only those
proteins with multiple subunits have a
quaternary structure.
Composition: Insulin, a hormone that regulates
blood sugar, is an example of a protein with a
quaternary structure. It is composed of two
polypeptide chains: one A chain and one B
chain.
Subunit Arrangement: The two chains are held
together by disulfide bonds (covalent bonds
between sulfur atoms in cysteine residues) that
link the subunits together. This specific
arrangement allows insulin to be biologically
active and able to interact with its receptor to
regulate glucose uptake.
Types of
Proteins
Hormones

are the chemical messengers in the

body. They regulate many body
processes and functions.
Enzymes
A biological catalyst is any compound that
speeds up a particular reaction rate
without getting used up in the reaction
itself. Examples of these proteins include
digestive enzymes, such as lipase,
protease, and amylase. The names of
enzymes contain some information about
the reactions they are made to catalyze
and usually possess the suffix “ -ase”
Transport Proteins
The structures of some proteins are
arranged in such a way that they can
carry certain molecules or substances.
One example of a transport protein is
hemoglobin, mainly used to carry
oxygen in the blood.
Structural Proteins
✓ Keratin is the main structural protein
of hairs, feathers, and nails.
✓ Collagen is a structural protein that
supports connective tissues. It is
present in the skin, ligaments, and
tendons.
✓ Tubulin is the main structural protein
present in the microtubules of cells.
Structural Proteins
Keratin, collagen, and tubulin are
examples of proteins used in
constructing or supporting
cellular structures.
Defensive Proteins
Some proteins are used to defend
the body against contaminants,
pathogens, and other foreign
materials. An example of these
defensive proteins is the
immunoglobulins, critical
components of the body's immune
system.
Contractile Proteins
These proteins are vital for
movement. Two notable
examples of contractile proteins
are myosin and actin, both of
which are present in muscles.
Storage Proteins
An example of a storage
protein is ferritin, which
stores iron. Another example
of a storage protein is
ovalbumin, which contains
nutrients for the developing
embryo in eggs.
ACTIVITTY:
• Reflect on the importance of proteins in health and
nutrition, emphasizing their role in body functions.
• Share experiences or examples of protein deficiency
and discuss how this knowledge impacts lifestyle
choices.
• Connect the study of proteins to real-world
applications like medical research and disease
treatment.