Chapter 2: Biomolecules
Macromolecules: Carbs, Proteins, Lipids, Nucleic
Acids
-Large molecules formed by joining smaller organic
molecules together
Introduction
1. Matter consist of chemical elements in
pure form and in combinations called
compounds
● Organisms are composed of matter
● Element is a substance that cannot be
broken down to other substances by
chemical reactions
● Compound is a substance consisting of
two or more elements in a fixed ratio
2. Formation and function of molecules
depend on chemical bonding between
atoms
● Incomplete valence shell- results to
another attraction
● Ionic bond
- Metal and nonmetal elements
- Metal gives off the valence electron for
the nonmetal
- Anion and cation
● Covalent bond
- 2 nonmetals
- Metal and metalloid
- Share electrons since they do not have
opposite charges
● When an atom gives off (+)>cation
● When receive an extra electron (-)>anion
➔ Polar covalent bond -One atom is more
electronegative> unequal sharing of
electrons
➔ Nonpolar covalent bond- share the
electron equally
BIOMOLECULES
● Compounds found in living organisms
● Organic and inorganic substances
● Polymers built from monomers
Polymer- long molecule consisting of many similar
building blocks
- Broken down into monomers via
hydrolysis reactions
- Adding water to break bond resulting to a
simpler components
Monomers- repeating units that serves as building
blocks
- Made into polymers via dehydration
reactions
- Removal of water in order to create a
larger molecule
Carbon is the Central Element
- All biomolecules contain carbon
- Carbon has 4 outer shell electrons
- Bonding capacity is great
- It forms covalent bonds
- Once bound to other elements (or other
carbon), it is very stable
CARBOHYDRATES
● contain carbon, hydrogen and oxygen
`atoms in a ratio of approximately
1C:2H:1O (CH2O)n
● Sugars and starches
● Can contain:
- One sugar unit (monosaccharides)
- Two sugar units (disaccharides)
- Many sugar units (polysaccharides)
● Contain three to seven carbon atoms in A
hydroxyl group is bonded to each carbon
except one
● One carbon is double bonded to an oxygen
atom (carbonyl group), forming aldehydes
and ketones
● Glucose, C6H12O6, is the most abundant
monosaccharide and used as the primary
energy source
● Bond: glycosidic linkage
● Building blocks: sugar
KINDS OF CARBOHYDRATES
1. Monosaccharide- simple sugar
2. Disaccharides-two simple sugars combine
3. Oligosaccharide- fall under
polysaccharides
4. Polysaccharide- long chain of repeating
units of monosaccharides
MONOSACCHARIDES
- Simplest form of sugar (CH20)
- CnH2non
- Building blocks of larger carbohydrates
- They are polar>high soluble in water
- Only one 3-C, 5-C, 6-C chain or ring
involved
Example: Glucose (C6H12O6)
DISACCHARIDES
- Double sugars by a dehydration reaction
- Consist of two 6-C chains or ring bonded
together
- Two monosaccharide rings joined by a
glycosidic linkage, consisting of a central
oxygen covalently bonded to two carbons,
one in each ring
➔ Common disaccharides:
● Maltose (malt sugar):
- m2 covalently linked α-glucose units
● Sucrose (table sugar):
- 1 glucose + 1 fructose
● Lactose (milk sugar):
- 1 glucose + 1 galactose
POLYSACCHARIDES
- Complex sugars known for their storage
and structural roles
- Storage (starch and glycogen)a and
Structural (cellulose and chitin)
➔ Common polysaccharides:
● Starches: energy storage in plants
● Glycogen: energy storage in animals.
● Cellulose: structural polysaccharide in
plants.
● Chitin: Skeletal of shrimps and shell of
crabs
• Starch is a polymer consisting of α-glucose
subunits and occurs in two forms:
1. Amylose (unbranched chain)
2. Amylopectin (branched chain)
Beta and Alpha Linkages
● How our body responds
- Enzymes that digest starch by hydrolysing
a linkages cannot hydrolyze b linkages
- Food items with a linkages are easily
broken down
- Food items with b linkages are not
digested by our digestive system>
insoluble fiber
- Food items with b linkages, you get
minerals, but it does not add up to the
blood sugar level of your body
FUNCTIONS OF CARBOHYDRATES
1. Provide quick energy to body
2. Dietary fiber can help lower blood
cholesterol
3. Spare protein from being burned so it can
be used to build and repair
- Protein wasting > body will use
proteins and tissues to be
converted as energy
4. Stores energy
PASTA LOADING
- Used for athletes
-
-
- Stored energy in order to finish and
sustain them throughout the game or
competition
DIFFERENCE OF CARBOHYDRATES FROM SWEETS
AND VEGETABLES
SWEETS > Alpha Linkages
● Digests easily by our body
● Increases blood sugar
VEGETABLES> Beta Linkages
● Nutrient-based
● Does not add up to your blood sugar
LIPIDS
● Not true polymer
- Because of you will consider the
structure of carbs, lipids are
quite smaller than carbs and
other biomolecules
● Fats, Phospholipids, Steroids
● Building blocks: fatty acids, glycerol
● Waxy or oily substances which are present
in all living organism as a main constituent
of all cell membrane
● fats , oil, cholesterol, lecithin
● Primary function:Used for energy storage,
structural components of cell membranes,
and in key hormones
● Building blocks: fatty acids and glycerol
KINDS OF LIPIDS
SATURATED FAT
- Single bond between carbon to carbon
- Raises low-density lipoproteins
- Increases cholesterol
- Solidify at room temperature
- Ex: animal fat, dairy, butter, coconut oil
UNSATURATED FAT
- Include one or more pairs of carbon
atoms joined by a double bond
- Tend to be liquid at room Temperature
- Poly and mono identifies the number of
the double bond
1. Polyunsaturated fat - more than one
double bond
Ex: sunflower, corn oil
2. Monounsaturated fat - one double bond
Ex; avocado oil, peanut oil
- Presence of a double bond changes the
structure of your fatty acid and creates a
kink/ distortion in the structure
FATTY ACIDS
- Can be considered as fatty acid if a
glycerol has one or two fatty acids
FAT MOLECULE
- 3 fatty acids connected to glycerol via
ester linkage
 4. Generate heat

5. Giving cell membrane structures

CIS FAT
- Unsaturated
- There is a double bond
- Attached molecule to carbons are upward
TRANS FAT
- Attached molecules to carbon are pointing
in diff. directions: upward and downward
SATURATED FAT
PHOSPHOLIPIDS
- All connections between carbon are single
- Phosphate group attached to a glycerol
bond
- Glycerol attached to a fatty acid
- The more the double bond>the more the
distortion
- 2 fatty acids and a phosphate group are
attached to a glycerol
Ex: Cell membrane
- Phospholipid bilayer
- Hydrophilic head>attracted to water
- Pointing upward
- Hydrophobic tail>not attracted to water
- Kept in the middle because they poorly
mix with water
KETO DIET
- 75% fat
- 20% Protein
- 5% Carbs
- Huge amount of fat> huge amount of
energy
- But you must inatake good fat, because
bad fat/ cholesterol may block the
bloodstream
STEROIDS
FAT CONTENT IN PANCAKES AND OLIVE OIL
- Lipids characterized by a carbon skeleton
- Olive oil is better but it is 100% good fat
consisting of four fused rings
- Pancake contains 4-11% Bad fat
Ex: Cholesterol, Cortisol, Progesterone,
Testosterone
PROTEINS
● Basis for the major structural components
of animals and humans
● Building blocks: Amino acids
- Number of amino acids
● Amino acids are organic molecules with
the amino acids and carboxyl group
- AMINO GROUP: Nitrogen,
hydrogen>bonded to central carbon atom
FUNCTIONS OF LIPIDS - CARBOXYL GROUP:double bond oxygen
1. Energy Source - Amino acids differ in their properties
- Provide energy twice as much as carbs, due to differing side chains >R GROUPS:
but it does not add up to your blood sugar small or long molecule attached to alpha
level carbon/central carbon atom )
2. Protecting and structuring organs
3. Helps insulate our body
- Ex: Sea Lions: Blubber, layer of fat that
keeps them insulated and maintains
homeostasis
 Ex: Collagen and elastin proteins, provide a
fibrous framework in animal connective tissues.
● 20 amino acids Also maintains elasticity of our skin
● Biologically functional molecule that
consists of one or more polypeptides FOUR LEVELS OF PROTEIN STRUCTURE
(unbranched polymers) built from these 1. Primary structure
amino acids - Unique sequence of amino acids
● Peptide bonds - covalent bond that link 2. Secondary Structure
amino acids together in order to form - Consist of coils and folds in the
polypeptides polypeptide chain
- Range in length from few to more - Specific sequence of amino acids coils/
than 1000 monomers folds so that you’ll have Alpha Helix and
AMINO ACID CONTAINS beta pleated sheet
- Central Carbon (Alpha) 3. Tertiary Structure
- Amine Group - Interactions among various side chains (R
- Carboxyl Group group)
- R group - One side of the side meets and come in
FUNCTIONS OF PROTEINS contact with the other side
4. Quaternary Structure
1. Enzymatic protein
- Results when a protein consist of multiple
- Fasten chemical reaction inside our body
polypeptide chains
Ex: Digestive enzymes catalyze the hydrolysis of
bonds in food molecules
2. Defensive proteins
- Protection against diseases
Ex: Antibodies that fights and destroys viruses and
bacteria
3. Storage Proteins
- Storage of amino acids
Ex: Casein, the protein of milk that is a major
source of amino acids for baby mammals. Plants
IMPORTANCE OF STUDYING PROTEIN STRUCTURE
have storage proteins in their seeds.
Sickle Cell Disease: A change in primary structure
- Can affect the protein structure and
Ex: Ovalbumin is the protein of egg white, used as
ability to function
an amino acid source for the developing embryo
- Inherited blood disorder, results from a
single amino acid substitution in the
4. Transport proteins
protein hemoglobin
- Transport of substances
➔ The capacity of a sickle cell to carry
Ex: Hemoglobin, the iron-containing protein of
oxygen throughout our body is reduced
vertebrate blood, transports oxygen from the lungs
- Abnormal hemoglobin molecules cause the
to other parts of the body. Other proteins transport
red blood cells to aggregate into chains
molecules across membranes
and to deform into a sickle cell shape
5. Hormonal Proteins
➔ DENATURATION
- Coordination of an organism’s activities
- Loss of protein’s native structure
Ex: Insulin, a hormone secreted by the pancreas
(biologically inactive)
that causes other tissues to take up glucose, thus
- Breaks the peptide bond of the
regulating blood sugar concentration
protein and makes the structure
6. Receptor Proteins
come apart
- Response of cell to chemical stimuli
Ex: Receptors built into the membrane of a nerve
cell detect signaling molecules released by other
nerve cells
7. Structural Proteins
- Support
Ex:Keratin, protein of hair, horns, feathers, and
other skin appendages. Insects and spiders use silk
fibers to make their cocoons and webs.
WHY DO PEOPLE USE WHEY PROTEIN ?
- Because these are easily absorbed by our
body
- It does not passes the digestive tract in
order to break down to simpler forms
- It takes effect instantly in order to build
muscles
- 3’5
- OH attachment
Types of Nitrogenous bases
Pyrimidines- composed of carbons in rings
Purines- composed of two fused rings

NUCLEIC ACIDS
● Long thread like water soluble
macromolecules present in high
concentration in the nuclei of all living
cells
● Made from monomers called nucleotides
● Responsible for transmission of
hereditary characters from parents to
their offsprings and for the biosynthesis
of protein
TWO KINDS OF NUCLEIC ACIDS
1. DNA
2. RNA
- Both are composed of Pentose sugar and
nitrogenous bases
FUNCTION OF NUCLEIC ACIDS
1. Transmission of inherent characters from parent
to offspring
2. Synthesis of protein in our body, directs its own
replication, through DNA replication (gene
expression)
3.DNA fingerprinting is a method used by forensic
experts to determine paternity or maternity.
4.identification of criminals, you can see body
fluids, and secretions in the crime scene. Experts
will extract DNA from fluid charges
5.Played a major role in studies regarding
biological evolution and genetics
STRUCTURE OF NUCLEIC ACIDS
- DNA and RNA both contain nitrogenous ● A slight change in the amino sequence of a
bases (Nucleoside) particular specie would result to a
- Adenine, Guanine, Cytosine, Thymine, different organism
1. DNA (Deoxyribonucleic Acid) ● Any alteration would resolve to another
● Found in the nucleus organism
● Double helix
● Nitrogenous bases (A,G,C,T) WHY BIOMOLECULES ARE IMPORTANT?
● Pairing (A:T, C:G)
● Serve different metabolic processes in our
● Sugar: Deoxyribose
body
- Controls the transmission hereditary
● They provide us energy (carbs)
factors/ traits from your parents
● Structural components for tissues
- 5’3
(proteins)
- Attachment if hydrogen only
● Stored energy for a long period of time
2. RNA (Ribonucleic Acid)
(lipids)
● Found in the cytoplasm
● Important in the gene expression and the
● Single Strand
traits that we inherit from our parents,
● Nitrogenous bases (A,G, C, T)
and being expressed internally and
● Pairing (A:U, C:G)
externally in our body
● Sugar: Ribose
- Controls the synthesis of protein