BIOLOGICAL MOLECULES

Objectives

• Categorize the biological molecules

(lipids, carbohydrates, proteins, and
nucleic acids) according to their
structure and function.

• Explain the role of each biological

molecule in specific metabolic
processes.
Biomolecules

• A living system grows, sustains, and

reproduces itself. The most amazing
thing about a living system is that it is
composed of nonliving atoms and
molecules.

• Living systems are made up of various

complex biomolecules that interact
with each other and constitute the
molecular logic of life processes.
• Biomolecules are very large
molecules of many atoms,
which are covalently bound
together.
• It consists mainly of carbon
and hydrogen with nitrogen,
oxygen, sulfur, and
phosphorous.
• There are four major classes of
biomolecules: carbohydrates,
lipids, proteins, and nucleic
acids.
 Carbohydrates
These are organic compounds consisting of
Carbon, Hydrogen, and Oxygen. They are a
source of energy and provide
structural support.
Roles of
Carbohydrates (CHO)
• Chief energy source of living
organisms and the most abundant
organic compound around us.
• Backbone of other molecules (DNA
and RNA)
• Primarily for storage of chemical
energy (starch for plants, glycogen for
animals)
• Form a structural component of living
cells (chitin, cellulose, glycoproteins,
proteoglycans)
Classification of Carbohydrates
Classification of Carbohydrates

1. Monosaccharides (C6H12O6)
• Simple sugar with only
one sugar unit.
• Building blocks for more
complex form of sugars.
Examples of Monosaccharides
Glucose (blood sugar) Galactose (milk sugar) Fructose (fruit sugar)
• Component of the blood • Isomer of glucose • Isomer of glucose
• Fuel for the brain, liver, • Found in milk as part of • Found in fruits and
pancreas, pituitary, and the sugar lactose crops
adrenal glands.
• Instant source of energy • Found in dairy products • Is the sweetest naturally
because it easily dissolves occurring carbohydrate
in water.
• Small enough to pass
through the cell membrane
and into the cell.
Classification of Carbohydrates

2. Disaccharides (C12H22O11)
• Consists of two monosaccharides
joined by a glycosidic linkage, a
covalent bond formed between two
monosaccharides by a dehydration
reaction.
• Dehydration synthesis – type of
chemical reaction in which two smaller
molecules are joined together to form a
larger molecule by removing water.
Classification of Carbohydrates

2. Disaccharides (C12H22O11)
• Disaccharides must be broken down into
monosaccharides to be used for energy by organisms.
• Hydrolysis – breaking down of a disaccharide molecule
by introduction of water.
Examples of Disaccharides
Sucrose (table sugar) Lactose (milk sugar) Maltose (malt sugar)
• Formed by combining • Formed by combining • Formed by combining
glucose and fructose. glucose and galactose. two units of glucose.
• Used to sweeten our • Used to sweeten our • Used in making beer
food and drink. food and drink. and other alcoholic
• Found in dairy products. beverages.
Classification of Carbohydrates

3. Oligosaccharides
• Complex form of carbohydrates that
consist of three to twenty sugar units.
• Glycosidic bonds hold each sugar unit
that is bonded together.
Classification of Carbohydrates

4. Polysaccharides
• Complex form of carbohydrates that
consist of more than twenty sugar
units.
• Glycosidic bonds hold each sugar unit
that is bonded together.
• Form long chains or branches.
Examples of Polysaccharides
Starch Glycogen
• Major source of energy • Major source of energy
stored as a carbohydrate in stored as carbohydrate in
plants. animals.
• It is composed of two • Has more sugar units than
substances: amylose and starch. It is found in the
amylopectin liver and muscles.
• Easily digested by animals • It’s a source of reserve
because an enzyme that energy and is ready to be
can break the bond holding converted into glucose
the glucose molecules is units when needed.
present. (amylase)
Examples of Polysaccharides
Cellulose Chitin
• Insoluble carbohydrate • Found in the outer
abundant in tough outer wall of coverings of insects and
plant cells which is used for
support and protection.
crustaceans which
functions for support and
• Microorganisms found in the protection.
gut of ruminants, termites, and
other insects can break down • Rigid, hard, and inflexible
the linkage of sugar units in a than cellulose because of
cellulose molecule because of the presence of more
its ability to produce an
enzyme called cellulase. complex glucose subunits.
• Appear in fibers and paper is
made out of it.
 Lipids
It is a diverse group of nonpolar biological molecules whose
common properties are their ability to dissolve in organic
solvents such as chloroform or benzene, and their inability to
dissolve in water (hydrophobic).
Lipids are varied in form and function, but we will focus on
its types that are most important biologically: fats,
phospholipids, and steroids.
Classification of Lipids
Classes of Lipids

1. Fatty acids
• Transport form of metabolic fuel.
• Non-essential fatty acids – fatty acids
that can be synthesized or produced
by the body.
• Essential fatty acids – fatty acids that
cannot be synthesized or produced by
the body and have to be consumed
through food or dietary supplements.
Fatty acids may be:

a. Saturated fats
• Contains single bonds and solid at
ordinary conditions.
• Examples are margarine, butter, lard,
and animal fat.
• A diet rich in saturated fats is one of
the several factors that may contribute
to an increased risk for heart disease
and stroke.
Fatty acids may be:

b. Unsaturated fats
• contains double bonds and liquid at
ordinary conditions. Examples are
vegetable oil, olive oil, peanut oil, corn
oil, and fish oil.
Did you know?
Trans fats create inflammation,
which is linked to heart disease,
stroke, diabetes, and other chronic
conditions. They contribute to insulin
resistance, which increases the risk
of developing type 2 diabetes. Some
countries, such as Denmark and
Switzerland, have already banned
artificially produced trans fats in
foods.
Fatty acids may be:

c. Trans fat
• came from partially hydrogenated oils,
formed through a manufacturing
process that converts vegetable oil
into a solid fat at room temperature.
• inexpensive and less likely to spoil, so
foods made with it have a longer shelf
life.
Classes of Lipids
2. Triacylglycerol
(TAG)
• are fats (lipids) that function as long-
term energy storage.
• stored in adipose tissue (body fat) and
can be broken down to release energy
when needed.
• provides insulation against low
temperature and protect vital organs.
This subcutaneous layer is especially
thick in whales, seals, and most other
marine mammals, insulating their
bodies in cold ocean water.
Classes of Lipids

3. Waxes
• Chief storage form of energy for
planktons.
• Have water repellant properties and
firm consistency.
• Found in animal skin and fur of
aquatic mammals, feathers of
waterfowls, and leaves of many
plants.
• Examples are lanolin, beeswax, and
carnauba wax.
Classes of Lipids

4. Phospholipids
• Are essentials for cells because it is
the major constituent of the cell
membrane and is responsible for the
bilayer structure of it.
• Has a hydrophilic (polar) head and
two (nonpolar) hydrophobic tails.
• The phospholipid bilayer serves as a
barrier between the cell and its
surroundings, creating several
compartments within eukaryotic
cells.
Classes of Lipids

5. Steroids
• are lipids with the principal function
of modulating the structure of
biological membranes and signaling
chemical biological activities.
Steroids may be:
• Bile acids
• steroidal derivative that act as emulsifying agent in the digestive system.

• Cholesterol
• It helps regulate the fluidity of the cell membrane and therefore aid in the
transport of molecules.
• It is also the starting point for the synthesis of other steroids, such as
vertebrate sex hormones.
• In vertebrates, cholesterol is synthesized in the liver and is also obtained
from the diet.
• It can be harmful and cause complications if unregulated.
Steroids may be:

• Steroidal hormones
• group of hormones derived from cholesterol that act as chemical
messengers in the body. They regulate many physiologic
processes, including the development and function of the
reproductive system.
• Male – androgen and testosterone
• Female – estrogen and progesterone
 Proteins
Almost all the vital operations within a living organism rely on proteins.
Their significance is emphasized by their name, derived from the Greek
word "proteios" signifying "first" or "primary".
Proteins are the most abundant intracellular macromolecules and they
are known as the building blocks of life. They make up over half of the
solid matter in the majority of cells, playing a crucial role in nearly all
activities carried out by organisms.
Functions of Proteins
Functions of Proteins
1. Enzymatic Proteins Function: Selective
acceleration of chemical reactions.
Example: Digestive enzyme catalyze the
hydrolysis of bonds in food molecules
2. Defensive Proteins Function: Protects
against disease.
Example: Antibodies inactivate and help
destroy viruses and bacteria.
3. Storage Proteins Function: Reservoir of
metal ions and amino acids, which can be
utilized for the maintenance and growth of
organisms.
Examples: Casein (the protein found in
milk), Plants, Ovalbumin (the protein
present in egg whites)
Functions of Proteins
4. Transport Proteins Function: Also known as
carrier proteins or transporter proteins, serve
the essential function of facilitating the
movement of various molecules across
biological membranes, both within and
between cells.
Example: Hemoglobin, the iron-rich protein
found in the blood of vertebrates.
5. Hormonal Proteins Function: Carry
important information to different parts of the
body to help regulate various processes and
coordinate activities.
Example: Insulin, a hormone secreted by
the pancreas.
Functions of Proteins
6. Receptor Proteins Function: Response of cell
to chemical stimuli. Acts as molecular sensors.
Example: Receptors built into the membrane
of a cell binds to a ligand.
7. Contractile and Motor Proteins Function:
Responsible for generating movement in cells
and tissues.
Example: Actin and myosin proteins enable
muscle cells to contract.
8. Structural Proteins Function: Provide stability,
support, and shape to cells, tissues, and
organisms. They form the structural framework,
ensuring the integrity and strength of various
biological structures.
Example: Keratin, Collagen, and Elastin.
 Four Levels of Protein Structure
1. Primary Structure 2. Secondary Structure
• The simplest structure of all • It is a three-dimensional shape
the proteins. This is composed created by several hydrogen bonds. It
only of the linear sequence of is like how a ribbon can twist and fold
amino acids in a peptide chain. to create pattern, this ribbon is a long
chain of amino acids, and these
chains can twist and fold in specific
ways. The two common patterns are
called "alpha helix" and "beta sheet."
 Four Levels of Protein Structure
3. Tertiary Structure 4. Quaternary Structure
• a three-dimensional shaped of • this happens when proteins
peptide, which can either be have more than one
fibrous or globular in structure, polypeptide. (Hemoglobin)
it can be determined by the
interactions of the side chains
of the different amino acids in
the peptide.
Denaturation

• Disorganization of the overall

molecular shape of the protein
causing it to be biologically
inactive.
• Denaturing agents – reagents or
conditions that brought the
unfolding or disorganization of a
protein.
 Amino acids
• Amino acids are organic compounds that
serve as the building blocks of proteins.
• Contains carbon, hydrogen, oxygen, and
nitrogen atoms, along with a variable side
chain that distinguishes one amino acid
from another.
Common Structure of Amino acids
Common structure of amino acids:
• All amino acids share a common structure: they have a carboxyl group
(COOH) and an amino group (NH2) separated by a carbon backbone.

• The side chain, known as the R group, varies for

each amino acid. This R group can range from
being as basic as a hydrogen atom to
a carbon structure with different functional
groups attached.
• The distinctive traits of a specific amino acid,
including its physical and chemical properties,
are determined by its side chain.
• Polypeptide chain – is a linear chain of amino
acids linked together by peptide bonds.
• Peptide bond – bond between amino acids.
Classification of Amino Acids based on their side chains:

Electrically charged
Nonpolar side chains Polar side chains
side chains
• hydrophobic • hydrophilic • hydrophilic
• low solubility in water • highly soluble in water. • highly soluble in water
• contributes in forming • involved in enzymatic
• plays a crucial role in reactions, substrate
the interaction zone
stabilizing protein between the protein and binding, or protein-protein
structures its aqueous environment. interactions, where
electrostatic attractions or
repulsions are significant.
Classification of Amino Acids based on their role in protein
synthesis:

Essential Amino Acids Non-Essential Amino Acids

• These are amino acids that the • These are amino acids that the
human body cannot synthesize body can synthesize
on its own and must be independently, and they are not
obtained from the diet. strictly required in the diet.
• 9 out of 20 amino acids are • The rest of the 11 amino acids;
essential; histidine, isoleucine, alanine, arginine, asparagine,
leucine, lysine, methionine, aspartic acid, cysteine,
phenylalanine, threonine, glutamic acid, glutamine,
tryptophan, and valine. glycine, proline, serine, and
tyrosine.
 Enzymes

Enzymes can be defined as “biological polymers that catalyze biochemical

reactions”.

Most enzymes are proteins that possess essential catalytic abilities required for
various cellular processes. These enzymes play a vital role in conducting
metabolic and other chemical reactions within the cell, which are necessary to
sustain life.
 Functions of Enzymes

• They break down large • Enzymes perform a number of

molecules into smaller biochemical reactions, including
substances that can be easily oxidation, reduction, hydrolysis, etc.
absorbed by the body. to eliminate the non-nutritive
• They help in generating energy substances from the body.
in the body. ATP synthase is the • They function to reorganize the
enzyme involved in the synthesis internal structure of the cell to
of energy. regulate cellular activities.
• Enzymes are responsible for the
movement of ions across the
plasma membrane.
How do enzymes work?
In order for things to change or react, they need a
certain amount of energy. Sometimes, when there
isn't enough energy, something called a catalyst
helps to make the reaction happen by reducing
the energy needed. This happens not just in animals
and plants but everywhere in the universe.
Enzymes help reduce the activation energy of
the complex molecules in the reaction.
Active site Substrate
• part of an • is a specific
enzyme to molecule that
which the enzyme
substrates acts upon or
bind and interacts with
where during a
a chemical chemical
reaction is reaction.
catalyzed.

The enzyme binds to the substrate and helps facilitate or speed up the
conversion of the substrate into one or more products.
 The common analogy used in illustrating an active site
is the lock-and-key relationship. The key can work
Theories on how perfectly when it exactly fits the lock. However, there
enzymes work are times when certain adjustments are also done by
the enzyme to achieve an optimum fit for the
substrates, this is called induced fit theory.
Factors affecting enzyme activity

Substrate Concentration - directly affects enzyme activity.

As substrate concentration increases, the rate of the
reaction also increases, until all enzyme active sites become
saturated.

Enzyme Concentration - increasing the amount of enzyme in

a reaction can speed up the rate of reaction, assuming that
there is an excess of substrate available. More enzymes
mean more active sites available for substrate binding.
Factors affecting enzyme activity
Temperature - with the increase in temperature, the enzyme activity
increases because of the increase in kinetic energy of the molecules.
Enzymes work most efficiently in the normal body temperature.
When the temperature increases beyond a certain limit, it will begin
to disintegrate and the rate of reaction slows down.

pH Level - enzymes also have an optimal pH range at which

they function best. Changes in pH can alter the charge and shape of
the enzyme's active site, affecting substrate binding and enzyme
activity. Optimum pH level for enzyme is ranging between 5 and 7.
Factors affecting enzyme activity

Inhibitors - presence of certain substances

that inhibit the action of a particular
enzyme. This occurs when the inhibiting
substance attaches itself to the active site
of the enzyme thereby preventing the
substrate attachment and slows down the
process.
Types of Inhibitors: Competitive
Competitive Inhibitor Effect on Enzyme Activity
• are molecules that closely • when a competitive inhibitor
resemble the substrate and is present, it reduces the rate of
compete with the substrate for the enzymatic reaction
binding to the enzyme's active because it occupies the active
site. site and prevents the substrate
• "compete" for the same spot from binding.
on the enzyme. • inhibition is reversible, meaning
that if you add more substrate,
it can outcompete the inhibitor
and restore enzyme activity.
Types of Inhibitors: Non-competitive
Non-competitive Inhibitor Effect on Enzyme Activity
• do not directly compete with • the conformational
the substrate for the active site. change induced by non-
Instead, they bind to a competitive inhibitors makes
different site on the enzyme, the enzyme less effective at
catalyzing the reaction.
called an allosteric site, causing
a conformational change in the • even if you add more substrate,
enzyme's shape. it won't fully overcome the
inhibition because the active
site is not directly blocked.
• non-competitive inhibition
is often non-reversible.
Types of Inhibitors: Uncompetitive
Uncompetitive Inhibitor Effect on Enzyme Activity
• are unique in that they only • they reduce the rate of
bind to the enzyme-substrate reaction by preventing the
complex. They cannot bind to enzyme-substrate complex
the free enzyme or the free from releasing products. This
results in the accumulation of
substrate. enzyme substrate-inhibitor
• once the enzyme binds to complexes and a decrease in
the substrate, the the formation of the reaction's
uncompetitive inhibitor can products.
attach to the enzyme-substrate • uncompetitive inhibition is
complex. often non-reversible
 Nucleic Acids
These are macromolecules made out of one unit called
nucleotides.
The two types of nucleic acids; deoxyribonucleic acid
(DNA) and ribonucleic acid (RNA), enable living organisms to
reproduce their complex components from one generation to
the next.
 DNA Structure
• Deoxyribonucleic acid (DNA)
• genetic material inherited by organisms from their
parents.
• each chromosome has one long DNA molecule that
normally contains several hundred genes.
• when a cell divides to reproduce itself, its DNA
molecules are duplicated and passed down from
one generation of cells to the next.
 DNA Structure
• DNA is composed of two families of
nitrogenous bases: pyrimidines and purines.
They contain the sugar 2-deoxyribose and
are joined by phosphodiester bridges.
• Pyrimidines contain two fused carbon-nitrogen
rings. The members of the pyrimidine family are
cytosine (C), thymine (T), and uracil (U).
• Purines – have a single carbon-nitrogen ring. The
members of the purine family are adenine (A)
and guanine (G).
 DNA Structure
• Adenine (A), guanine (G), and cytosine (C) are found
in both DNA and RNA;
• Thymine (T) is found only in DNA
• Uracil (U) only in RNA
• The purine adenine (A) on one strand of DNA is
always paired with the pyrimidine thymine (T) on the
other strand, while the purine guanine (G) is always
paired with the pyrimidine cytosine (C); thus, the two
strands are said to be complementary.
• G-C , A-T
 DNA Structure
• The two strands are not positioned directly
opposite one another; therefore, a major
groove and a smaller minor groove are
formed by the double helix backbone.
• The two polynucleotide chains are
antiparallel. This means that their sugar-
phosphate backbones are oriented in
opposite directions.
 RNA Structure
• Ribonucleic acid (RNA)
• it differs from DNA in that it is composed of
sugar ribose instead of 2-deoxyribose.
• contains the pyrimidine uracil (U) instead of
thymine (T).
• consists of a single strand that can coil back
on itself, rather than two strands coiled
around each other.
 Types of RNA
• Messenger RNA (mRNA) – provides a template for gene
coding during protein synthesis. It contains the coding
instructions for protein’s amino acid sequence.
• Transfer RNA (tRNA) – carries/transfers specific amino
acids in the cytoplasm to the ribosome to build a polypeptide
chain, aiding the translation.
• Ribosomal RNA (rRNA) – it forms the ribosomes and serves
as the structure of translation.
Any questions or clarifications?