Biological

Macromolecules
GENERAL BIOLOGY 1
2ND QUARTER
 Biological Macromolecules
• are organic molecules (has atoms of carbon that are
bonded to atoms of hydrogen)

4 Groups of Biomolecules:
 Biological Macromolecules
• are considered to be polymers formed through
polymerization reaction.
“poly” -- many,” “-mer” – unit

• Polymers are large molecules made of many

repeating subunits called monomers.
• Monomers are molecules considered as building
block for larger molecules (polymers).
1. Carbohydrates
 Carbohydrates
§ refers to any of the group of organic compounds
consisting of carbon, hydrogen, and oxygen, usually in
the ratio of 1:2:1

§ general formula: Cn(H2O)n

§ Carbohydrates = hydrates of carbon (ratio of H:O = 2:1)

§ the most abundant among the major classes

of biomolecules.
Classification of Carbohydrates
Monosaccharides
• Glucose, galactose and fructose
have the same chemical formula
(C6H12O6)
• Glucose and fructose are isomers
because they have an identical
molecular formula but different
structures
• Glucose consists of an aldehyde
group while fructose consists of a
ketone functional group.
• Aldehydes contain the carbonyl
group bonded to at least one
hydrogen atom. Ketones contain the
carbonyl group bonded to two
carbon atoms.
 Monosaccharides
• Glucose
• Common name: Blood sugar; also
known as dextrose
• Sources: honey, agave, molasses, dried
fruit, fruits, fruit juices, and sweet corn

• Galactose
• Common Name: Milk sugar
• Sources: milk and dairy foods

• Fructose
• Common name: fruit sugar
• Sources: fruits, fruit juices, some
vegetables and honey
 Disaccharides
• composed of two
monosaccharide units linked
together by a glycosidic bond

• The glycosidic bonds between

residues use an oxygen
molecule to bridge two carbon
rings.
• A Hydroxyl group will be lost
from one monosaccharide, and
a hydrogen will be removed
from the Hydroxyl group of the
other to leave a free oxygen à
dehydration reaction
 Polymerization
● Polymers are made up of a ● Dehydration reaction, or condensation
combination of smaller reaction or dehydration synthesis occurs
molecules called monomers, when two molecules are joined by
through a process called removing water. This allows for the
polymerization. creation of a larger molecule from two
smaller molecules
 Disaccharides
• Sucrose = glucose + fructose
• Common name: table sugar
• Sources: sugar cane, sugar beets,
apples, oranges, carrots, and other fruits
and vegetables

• Maltose = glucose + glucose

• Common Name: Malt sugar
• Sources: beer, bread, breakfast cereal

• Lactose = glucose + galactose

• Common name: milk sugar
• Sources: found naturally in the milk of
mammals—including cows, goats and
humans
 Polysaccharides
• Polysaccharides are long chains
of more than 10
monosaccharide molecules linked
by glycosidic bonds.

• structure can vary widely depending

upon the
• shape and size of the residues that
make it up,
• the locations of the bonds holding
those residues together,
• where and how the polysaccharide
is made,
• where it is stored, and its function
 Polysaccharides
Starch
•Found in granules in plants
•Storage of carbohydrates for plant cells to use as energy
•Made up of glucose molecules in a coil structure
•Makes up about 50% of our dietary carbohydrate intake

Glycogen
•Found in granules in animal cells, especially liver and muscle cells
•Storage of carbohydrates for animal cells to use as energy
•Made up of glucose residues in a branched structure
•About 70% of the glycogen in the human body is stored in the skeletal
muscle

Cellulose
•Fibrous carbohydrate that makes up plants' cell walls
•Provides structure for plant cells, the chains have hydrogen bonds that
link them together to increase their strength
•Linear structure that binds together into fibers
•Cellulose is used to produce over 70% of textiles
 Functions of Carbohydrates
1. Provide energy to organisms
Monosaccharides, in particular, are the main source of
energy for metabolism. When they are not yet needed, they
are converted into energy-storing polysaccharides, such as
starch in plants and glycogen in animals.

2. Important structural components

At the cellular level, polysaccharides (e.g. cellulose) are
constituents of the cell walls of plant cells and many algae.
Cells without cell walls are more prone to structural and
mechanical damage. In plants, the cell wall prevents the cell
from bursting into a hypotonic solution.
 Common Biological Reactions Involving
Carbohydrates
In plants and other photosynthetic
autotrophs, the synthesis of simple
sugars (e.g. glucose) is done through
photosynthesis.

The process uses carbon

dioxide, water, and light energy (from
sunlight) captured by light-absorbing
pigments, such as chlorophyll and
other accessory pigments to produce
glucose and oxygen molecules.
 Common Biological Reactions Involving Carbohydrates
• Cellular respiration is a series of chemical
reactions that break down glucose to
produce ATP, which may be used as
energy to power many reactions
throughout the body.

3 main steps of cellular respiration:

• Glycolysis - Cytosol
• Kreb’s cycle – Mitochondrial matrix
• Oxidative phosphorylation - Inner
mitochondrial membrane.

• One molecule of glucose can produce a net

of 30-32 ATP.
 Assignment : Carbohydrates

Answer the following questions in 5

sentences:
1.What is the primary function of carbohydrates in the
human body?
2. What is the function of glycogen in the liver? In the
skeletal muscles?
3.What is the role of chlorophyll and sunlight in
photosynthesis?
 Quiz No. 1 : Carbohydrates

Answer the following questions in not less than 5

sentences:
1. Glycogen is the stored form of carbohydrates in humans and
particularly found in liver and skeletal muscles. Give two
importance of glycogen in relation to its function in the liver
and muscle cells.
2. Why are carbohydrates considered energy-giving foods.
Explain your answers in relation to the different biological
processes.
2. Proteins
Proteins
A protein is a biomolecule composed
of amino acids joined together
by peptide bonds.

Glutathione (cysteine, glutamic acid,

and glycine)

An amino acid is a molecule consisting

of the basic amino group (NH2), the
acidic carboxylic group (COOH), a
hydrogen atom, and an organic side
group (R) attached to the carbon
atom.
Amino Acids
Amino Acids and
R groups
Dehydration Synthesis
 Common Sources of Proteins

Eggs | Milk | Yogurt | Fish and seafoods |

Chicken and turkey | Soya | Nuts and seeds |
Pork | Beef | Lentils

A food is considered a complete protein when

it contains all nine essential amino acids:
histidine, isoleucine, leucine, lysine,
methionine, phenylalanine, threonine,
tryptophan, and valine
Nine Major Categories of Proteins

§ Enzymes
§ Structural Proteins
§ Motility Proteins
§ Regulatory Proteins
§ Transport proteins
§ Signaling proteins
§ Receptor proteins
§ Defensive proteins
§ Storage proteins
1. Enzymes - serve as catalysts that greatly increase the
rates of the thousands of chemical reactions on
which life depends

Exa:
Amylase – mouth and pancreas – breaks down complex
carbohydrates
Lipase – pancreas – breaks down fats
Proteases – breaks down proteins
2. Structural Proteins - provide physical support and
shape to cells and organelles, giving them their
characteristic appearances
Exa:
Collagen – connective tissue
Keratin – hair, nails, feathers
Actin (intermediate filaments), Tubulin (microtubules)
3. Motility Proteins - play key roles in the contraction and
movement of cells and intracellular materials

Exa:
Actin – most abundant protein in eukaryotic cells;
functions in muscle contraction and cell
movements
Myosin – muscle contraction and movement on
actin filaments
4. Regulatory Proteins - responsible for control and
coordination of cellular functions, ensuring that cellular
activities are regulated to meet cellular needs

Exa:
Insulin – regulator of glucose metabolism
CDK – cyclin-dependent kinase – controls cell cycle
progression
5. Transport proteins
are involved in the
movement of other
substances into, out
of, and within the cell.
Exa: Channel proteins,
carrier proteins,
sodium-potassium
pump, hemoglobin
6. Signaling proteins mediate
communication between cells in an
organism
Exa:
Thyrotropin releasing hormone
(TRH) triggers the release of thyroid
stimulating hormone (TSH), which, in
turn, triggers the release of thyroxine
from the thyroid gland.

Insulin is released by the pancreatic

beta cells in response to a rise in blood
sugar after a meal.
7. Receptor proteins enable cells to respond to chemical stimuli from
their environment
Exa: B cell, T cell, Stem cell receptor protein

8. Defensive proteins provide protection against disease

Exa: antibodies (Immunoglobulin A), lectins (plants – defense
proteins and are harmful to insects or pathogens), and antiviral
proteins

9. Storage proteins serve as reservoirs of amino acids.

Exa: Casein, found in mammalian milk, and ovalbumin, found in egg
white, both provide a developing organism with a ready source
of amino acids and organic nitrogen
Ferritin stores iron in hemoglobin
 Key Points: Proteins

• Each amino acid contains a central C atom, an amino

group (NH2), a carboxyl group (COOH), and a specific
R group.
• The R group determines the characteristics (size,
polarity, and pH) for each type of amino acid.
• Peptide bonds form between the carboxyl group of one
amino acid and the amino group of another through
dehydration synthesis.
• A chain of amino acids is a polypeptide.
Levels of Protein
Structure
Which of the following best explains why proteins differ
in their structure and function?
[A] Different proteins contain the same composition of amino acids that
form the same polypeptide chain, but this chain folds in different ways.

[B] Different proteins have different numbers and arrangements of amino

acids in their polypeptide chains, which interact in different ways.

[C] Each protein consists of only one type of amino acid joined into
polypeptide chains, but this amino acid differs between proteins.

[D] All proteins have very similar structures and functions.

Primary Level of Structure
● is the amino acid sequence in its
polypeptide chain.
● Covalent, peptide bonds which connect
the amino acids together maintain the
primary structure of a protein.
● genetic disorders, such as cystic fibrosis,
sickle cell anemia, albinism, etc., are
caused by mutations resulting in
alterations in the primary protein
structures à lead to alterations in the
secondary , tertiary and quaternary
structure.
Primary Level of Structure: Insulin
 Primary Level of Structure

● Dipeptides:
• Compound formed when two amino acids linked by 1 peptide
bond.
• Examples:

• Carnosine ( β-alanyl-L-histidine)

• Anserine (β-alanyl-N-methylhistidine)

• Aspartame (Asparagine-phenylalanine)
 Primary Level of Structure
● Tripeptides
• formed when three amino acids linked by 2 peptide bond.
• Examples:

• Glutathione (cysteine, glutamic acid, and glycine)

• Opthalmic acid (l-γ-glutamyl-l-2-aminobutyryl-glycine)

 Primary Level of Structure
● Oligopeptides
• formed when more than 2 and less than 20 amino acids are linked by
peptide bonds.
• Exa:
• Tetrapeptide
• à Tulfsin ( thrionine-lysine-proline-Arginine)

• à Endomorphin-1 ( Tyrosine-proline-tryptophan-phenylalanine)
• Decapeptide
• à Amanitin (found in a number of poisonous mushrooms)

• Netropsin à antibiotic and antiviral

 Primary Level of Structure
● Polypeptides

Compound formed when more than 20 amino acids are

•
linked by peptide bond.
• Examples:
Growth hormone (191 amino acids)
 Secondary Level of Structure

• Secondary structure refers to the local folded

structure of protein
• The secondary structure is held together by
hydrogen bonds
• The most common types of secondary structures
are α – helix and β – pleated sheet
Secondary Level of Structure
Tertiary Level of Structure
• refers to the three-dimensional
arrangement of a polypeptide chain
that has assumed its secondary
structure.
• It gives rise to two major molecular
shapes called fibrous and globular.
• The main forces which stabilize the
secondary and tertiary structures of
proteins are hydrogen bonds,
disulphide linkages, van der Waals and
electrostatic forces of attraction.
• Examples: Collagen, myoglobin
Quaternary Level of Structure

• made from two or more polypeptide

chains
• Examples of proteins with quaternary
structure include hemoglobin, DNA
polymerase, ribosomes, antibodies,
and ion channels.
Hemoglobin
 Quiz No. 2: Proteins

● Proteins are considered the most important

biomolecule in living organisms because of the
diverse functions they perform in living organisms.
List 5 types of proteins based on their function,
explain their function and importance in the body
and give examples. (20 pts)
3. Lipids
● Lipids are groups of hydrophobic biomolecules that
play important roles in living organisms

● Functions:
○ Long-term energy storage
○ Protection

○ Insulation

○ Lubrication

○ Precursor for different hormones:

estradiol, testosterone, aldosterone, cortisol

○ Key component of cell membranes
 4 Basic Groups of Lipids

● Triglycerides (triacylglycerols)
● Phospholipids
● Steroids
● Waxes

They have different characteristics but all are

insoluble in water
 Triglycerides
Fats
• Lards and butter
• Solid at room temperature
• Used by animals for insulation, protection and
long-term energy storage

Oils
• Corn oil. Olive oil
• Liquid at room temperature
• Used by plants for long-term energy storage
 Triglycerides
Structure
• Contains 2 types of sub-unit molecules; Glycerol
(C3H8O3) and fatty acids

Fatty acids: consist of 3 main parts:

1. Hydrocarbon chain – chain of carbon and hydrogen
atoms
2. Methyl group (CH3)
3. Carboxyl Group (COOH)
 Triglycerides

To become a
triglyceride, 3 fatty
acids bond with a
glycerol molecule
(C3H8O3) through
dehydration
synthesis.
 Fatty Acids
Saturated Fatty Acids
• Has single carbon to carbon bonds
• The carbon chain is “saturated” with all the hydrogen
atoms it can hold
• Animal fats

Unsaturated Fatty Acids

• Have one to several double bonds resulting from kinks
in fatty acid chains which affects the melting point of
the fat
• Vegetable oils
Fatty Acids
 Triglycerides

*insert triglyceride structure and dehydration

synthesis
 Trans Fatty Acids
• Trans fatty acids is an example of unsaturated fatty
acid where the hydrogen atoms are on the opposite
sides of the double bond
 Trans Fatty Acids
• Usually formed during the
production of processed foods
and in partially dehydrogenated
oils
• Excess hydrogen atoms are
introduced to unsaturated fats to
increase the shelf life and melting
points of unsaturated oils
• Consumption of trans fats is
associated with cardiovascular
diseases
Phospholipids
Phospholipids
 Steroids
● Steroids are lipids with a
structure consisting of 4 fused
hydrocarbon rings to which 2
different functional groups are
attached.

● Example: Cholesterol – serves

as precursor for other steroids
such as testosterone, estrogen,
vitamin D, cortisone and present
in cell membrane which
stabilizes the membrane
 Steroids
● Testosterone and estrogen have small differences in their functional
groups but large differences on their effects in an organism
 Waxes

● Waxes are nonpolar and

repel water

● Found in protective
coatings on leaves and on
outer surfaces of animals

● Wax is produced in the

ear to protect the eardrum

● Bees construct
honeycomb from wax
 Key Points: Lipids

● The four categories of lipids are: triglycerides,

phospholipids, steroids, and waxes.
● All lipids are insoluble in water
● While the primary function of lipids are for long-term
energy storage, lipids are used for other purposes such
as protection, insulation, and as a key component of
hormones and cell membrane
Nucleic Acids
Nucleic Acids

Nucleic acids are large

biomolecules composed of
chains of nucleotides and
responsible for the storage of
genetic information and
protein synthesis.

Examples:
DNA (Deoxyribonucleic Acid)
RNA (Ribonucleic Acid)
Nucleotides

Nucleotides are molecules

made up of 3 components:
a 5-carbon sugar, a phosphate
group (PO4) and nitrogenous
base.
5-carbon sugar:
DNA: deoxyribose
RNA: ribose
Nitrogenous Bases:
DNA: A-T; C-G
RNA: A-U; C-G
Dehydration Synthesis of Nucleic Acids
RNA and DNA
 DNA
1. Structure:
 DNA
1. Structure:
a. DNA comprises a sugar-phosphate backbone and
the nucleotide bases (guanine, cytosine, adenine
and thymine).

b. Double helix structure – resembles a twisted ladder

c. 4 Nitrogenous bases pair together in the following

way: A with T, and C with G.

d. The order of the nitrogenous bases determines the

genetic code or the DNA’s instructions.
 DNA
2. Functions:

DNA contains the instructions needed for an organism to develop,

survive and reproduce. To carry out these functions, DNA
sequences must be converted into messages that can be used to
produce proteins, which are the complex molecules that do most of
the work in our bodies.

DNA sequences are transcribed into mRNA and in which the

corresponding mRNA molecules are translated into a polypeptide
chain. Every three nucleotides, termed a codon, in a protein coding
sequence encodes 1 amino acid in the polypeptide chain.
Protein Synthesis
RNA
1. Basic Structure:
• RNA has all the components same to
that of the DNA
• RNA has the same nitrogen bases as
that of the DNA except for the Thymine
which is replaced by the uracil.
• Resembles a hairpin-like structure

2. Functions:
• Facilitate the translation of DNA into
proteins
• Serves as a messenger between the
DNA and the ribosomes.
• They are the carrier of genetic
information in all living cells
End of
2nd Quarter
General Biology 1