The Structure and

Function of
Macromolecules
 Overview: The Molecules of Life
• All living things are made up of four classes
of large biological molecules: carbohydrates,
lipids, proteins, and nucleic acids
• Macromolecules are large molecules
composed of thousands of covalently
connected atoms
• Molecular structure and function are
inseparable

© 2011 Pearson Education, Inc.

 Concept 1: Macromolecules are
polymers, built from monomers
• A polymer is a long molecule consisting of
many similar building blocks
• These small building-block molecules are
called monomers
• Three of the four classes of life’s organic
molecules are polymers
– Carbohydrates
– Proteins
– Nucleic acids

© 2011 Pearson Education, Inc.

 The Synthesis and Breakdown of
Polymers
• A dehydration reaction occurs when two
monomers bond together through the loss of a
water molecule
• Polymers are disassembled to monomers by
hydrolysis, a reaction that is essentially the
reverse of the dehydration reaction

© 2011 Pearson Education, Inc.

 Figure 5.2a

(a) Dehydration reaction: synthesizing a polymer

1 2 3

Short polymer Unlinked monomer

Dehydration removes
a water molecule,
forming a new bond.

1 2 3 4

Longer polymer
 Figure 5.2b

(b) Hydrolysis: breaking down a polymer

1 2 3 4

Hydrolysis adds
a water molecule,
breaking a bond.

1 2 3
 I. Polymers
• What is a polymer?
• Poly = many; mer = part. A polymer is
a large molecule consisting of many
smaller sub-units bonded together.
• What is a monomer?
• A monomer is a sub-unit of a polymer.
 A. Making and Breaking
Polymers
• How are covalent linkages between
monomers formed in the creation of
organic polymers?
• Condensation or dehydration synthesis
reactions.
• Monomers are covalently linked to one
another through the removal of water.
Condensation Synthesis
 Hydrolysis
• What is a hydrolysis reaction?
• Polymers are broken down into
monomers.
• Hydro = water; lysis = loosening/
• Water is added and the lysis of the
polymer occurs.
Hydrolysis
 II. Classes of Organic
Molecules:
• What are the four classes of organic
molecules?
• Carbohydrates
• Lipids
• Proteins
• Nucleic Acids
 A. Carbohydrates
• Sugars
• Carbo = carbon, hydrate = water;
carbohydrates have the molecular
formula (CH2O)n
• Functions:
• Store energy in chemical bonds
• Glucose is the most common
monosaccharide
• Glucose is produced by photosynthetic
autotrophs
 1. Structure of
Monosaccharides
• An OH group is attached to each carbon
except one, which is double bonded to
an oxygen (carbonyl).
 • Classified according to the size of their
carbon chains, varies from 3 to 7
carbons.
Triose = 3 carbons Pentose = 5 carbons Hexose = 6 carbons
• In aqueous solutions many
monosaccharides form rings:
2. Structure of Disaccharides
• Double sugar that consists of 2
monosaccharides, joined by a glycosidic
linkage.
• What reaction forms the glycosidic
linkage?
• Condensation synthesis
 Examples of Disaccharides:
Lactose = glucose + galactose Sucrose = glucose + fructose
 3. Polysaccharides
• Structure: Polymers of a few hundred or a few
thousand monosaccharides.
• Functions: energy storage molecules or for structural
support:
• Starch is a plant storage from of energy,
easily hydrolyzed to glucose units
• Cellulose is a fiber-like structureal
material - tough and insoluble - used in
plant cell walls
• Glycogen is a highly branched chain
used by animals to store energy in
muscles and the liver.
• Chitin is a polysaccharide used as a
structural material in arthropod
exoskeleton and fungal cell walls.
Fig. 5-8
Cell walls
Cellulose
microfibrils
in a plant
cell wall
Microfibril

10 µm

0.5 µm

Cellulose
molecules

b Glucose
monomer
Fig. 5-10

(a) The structure (b) Chitin forms the (c) Chitin is used to make
of the chitin exoskeleton of a strong and flexible
monomer. arthropods. surgical thread.
Lactose

glucose + galactose

Maltose

glucose + glucose
Sucrose

glucose + fructose
glycogen
 Starch vs. Cellulose

Corn starch

Potato starch
 Starch vs. Cellulose

We can digest starch (amylose) but not cellulose.

What difference do you see that might be the reason
behind this?
 Digest Cellulose

cecum

Trichonympha, protist
found in termites guts
 B. Lipids
• Structure: Greasy or oily nonpolar
compounds
• Functions:
• Energy storage
• membrane structure
• Protecting against desiccation (drying out).
• Insulating against cold.
• Absorbing shocks.
• Regulating cell activities by hormone
actions.
 1. Structure of Fatty Acids
• Long chains of mostly carbon and hydrogen
atoms with a -COOH group at one end.
• When they are part of lipids, the fatty acids
resemble long flexible tails.
 Saturated and Unsaturated
Fats
• Unsaturated fats :
– liquid at room temp
– one or more double bonds between carbons in the
fatty acids allows for “kinks” in the tails
– most plant fats
• Saturated fats:
– have only single C-C bonds in fatty acid tails
– solid at room temp
– most animal fats
Saturated fatty
acid
Saturated fatty
acid

Unsaturated
fatty acid
 2. Structure of Triglycerides
• Glycerol + 3 fatty acids
• 3 ester linkages are formed between a
hydroxyl group of the glycerol and a
carboxyl group of the fatty acid.
 3. Phospholipids
• Structure: Glycerol + 2 fatty acids + phosphate group.
• Function: Main structural component of membranes, where
they arrange in bilayers.
Phospholipids in Water
 4. Waxes

• Function:
• Lipids that serve as coatings for plant
parts and as animal coverings.
 5. Steroids
• Structure: Four carbon rings with no fatty acid tails
• Functions:
• Component of animal cell membranes
• Modified to form sex hormones
 C. Proteins
• Structure:
• Polypeptide chains
• Consist of peptide bonds between 20
possible amino acid monomers
• Have a 3 dimensional globular shape
 1. Functions of Proteins
• Enzymes which accelerate specific
chemical reactions up to 10 billion times
faster than they would spontaneously
occur.
• Structural materials, including keratin
(the protein found in hair and nails) and
collagen (the protein found in
connective tissue).
• Specific binding, such as antibodies that
bind specifically to foreign substances
to identify them to the body's immune
system.
• Specific carriers, including membrane
transport proteins that move substances
across cell membranes, and blood
proteins, such as hemoglobin, that carry
oxygen, iron, and other substances
through the body.
• Contraction, such as actin and myosin
fibers that interact in muscle tissue.
• Signaling, including hormones such as
insulin that regulate sugar levels in
blood.
 2. Structure of Amino Acid Monomers
• Consist of an asymmetric carbon covalently
bonded to:
• Hydrogen
• Amino group
• Carboxyl (acid) group
• Variable R group specific to each amino acid
 Properties of Amino Acids
• Grouped by polarity
• Variable R groups (side chains) confer different
properties to each amino acid:
• polar, water soluble.
• non-polar, water insoluble
• positively charged
• negatively charged.
4 levels of protein structure:
• primary
• secondary
• tertiary
•quaternary
 3. Primary Structure
• Unique sequence of amino acids in a protein
• Slight change in primary structure can alter function
• Determined by genes
• Condensation synthesis reactions form the peptide
bonds between amino acids
 4. Secondary Structure
• Repeated folding of protein’s polypeptide
backbone
• stabilized by H bonds between peptide
linkages in the protein’s backbone
• 2 types, alpha helix, beta pleated sheets
 5. Tertiary Structure
• Irregular contortions of a protein due to
bonding between R groups
• Weak bonds:
– H bonding between polar side chains
– ionic bonding between charged side chains
– hydrophobic and van der Waals interactions
• Strong bonds:
– disulfide bridges form strong covalent linkages
 5. Quaternary Structure
• Results from interactions among 2 or more
polypeptides
 Factors That Determine Protein Conformation
• Occurs during protein synthesis within cell
• Depends on physical conditions of environment
– pH, temperature, salinity, etc.
• Change in environment may lead to denaturation of
protein
• Denatured protein is biologically inactive
• Can renature if primary structure is not lost
 D. Nucleic Acids
• Two kinds:
– DNA:
double stranded
can self replicate
makes up genes which code for proteins
is passed from one generation to another
– RNA:
single stranded
functions in actual synthesis of proteins coded for by
DNA
is made from the DNA template molecule
 1. Nucleotide Monomer
Structure
• Both DNA and RNA are composed of
nucleotide monomers.
• Nucleotide = 5 carbon sugar,
phosphate, and nitrogenous base

Deoxyribose in DNA Ribose in RNA

 2. Building the Polymer
• Phosphate group of one nucleotide forms
strong covalent bond with the #3 carbon of the
sugar of the other nucleotide.
 3. Functions of Nucleotides
• Monomers for Nucleic Acids
• Transfer chemical energy from one
molecule to another (e.g. ATP)
DNA:
• Double helix
• 2 polynucleotide chains
wound into the double helix
• Base pairing between
chains with H bonds
•A-T
•C-G
Summary of the Organic
Molecules:
Polymers made up of individual nucleotides
Nucleotides contain
• Phosphate group
• Five carbon sugar
• Ring shaped nitrogen base
DNA contains information for almost all cell activities
ATP
 Role of ATP in Energy
Metabolism
ATP  ADP + Pi + Energy
Role of ATP in Energy
Metabolism
 INQUIRY
1. Describe the difference
between saturated and
unsaturated fats.
2. Where are phospholipids
found?
3. Cholesterol is the base
molecule for what type
of lipids?
4. Name a polysaccharide
used to store energy.
5. Name the currency
molecule for all the cells
activities.