AP Bio Chapter 5 Lecture

Chapter 5
The Structure and Function of

Large Biological Molecules
PowerPoint® Lecture Presentations for
Biology
Eighth Edition
Neil Campbell and Jane Reece
Lectures by Chris Romero, updated by Erin Barley with contributions from Joan Sharp
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Question 1- Define the following:
• 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

• 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
Question 2 - Describe the reaction by which polymers are formed and
broken down.
• A condensation reaction, or more specifically

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

Fig. 5-2a
HO 1 2 3 H HO H
Short polymer Unlinked monomer
Dehydration removes a water

molecule, forming a new bond
H2O
HO 1 2 3 4 H
Longer polymer
(a) Dehydration reaction in the synthesis of a polymer
Fig. 5-2b
HO 1 2 3 4 H
Hydrolysis adds a water H2O

molecule, breaking a bond
HO 1 2 3 H HO H
(b) Hydrolysis of a polymer

Question 3 - What is a monosaccharide? Give examples. What is the most
common monosaccharide?
• Carbohydrates include sugars and the polymers of sugars

• The simplest carbohydrates are monosaccharides, or
single sugars
• Monosaccharides have molecular formulas that are
usually multiples of CH2O
• Glucose (C6H12O6) is the most common monosaccharide
• Though often drawn as linear skeletons, in aqueous
solutions many sugars form rings
• Monosaccharides serve as a major fuel for cells and as
raw material for building molecules

Fig. 5-4b
(b) Abbreviated ring structure

• A disaccharide is formed when a dehydration
reaction joins two monosaccharides
• This covalent bond is called a glycosidic
linkage
Animation: Disaccharides

Fig. 5-5
1–4
glycosidic
linkage
Glucose Glucose Maltose

(a) Dehydration reaction in the synthesis of maltose
1–2
glycosidic
linkage
Glucose Fructose Sucrose

(b) Dehydration reaction in the synthesis of sucrose
Polysaccharides
• Polysaccharides, consist of three or more

monosaccharides.
• The structure and function of a polysaccharide
are determined by its sugar monomers and the
positions of glycosidic linkages

Question 6 – What compound do plants use to store glucose? Animals?
• Starch, a storage polysaccharide of plants,

consists entirely of glucose monomers
• Plants store surplus starch as granules within
chloroplasts and other plastids
• Glycogen is a storage polysaccharide in
animals
• Humans and other vertebrates store glycogen
mainly in liver and muscle cells

Fig. 5-6
Chloroplast Starch Mitochondria Glycogen granules
0.5 µm
1 µm
Amylose Glycogen
Amylopectin
(a) Starch: a plant polysaccharide (b) Glycogen: an animal polysaccharide

Question 7 – From a structural standpoint, what is the difference between the
glucose monomers that make up starch and cellulose?
• Cellulose is the most abundant organic

compound on Earth.
• The polysaccharide cellulose is a major
component of the tough wall of plant cells
• Starch and cellulose are both composed of
glucose monomers.
• The difference is based on two ring forms for
glucose: alpha () and beta ()

Fig. 5-7bc
(b) Starch: 1–4 linkage of alpha glucose monomers
(c) Cellulose: 1–4 linkage of beta glucose monomers

Glucose monomers are upside down with respect to their
neighbors.
Fig. 5-8
Cell walls
Cellulose
microfibrils
in a plant
cell wall
Microfibril
10 µm
0.5 µm
Cellulose
molecules
b Glucose
monomer
Question 8 – Why is cellulose important for humans? Cows? Termites?
• Enzymes that digest starch by hydrolyzing 

linkages can’t hydrolyze  linkages in cellulose
• Cellulose in human food passes through the
digestive tract as insoluble fiber
• Some microbes use enzymes to digest
cellulose
• Many herbivores, from cows to termites, have
symbiotic relationships with these microbes

Fig. 5-9
• Chitin, another structural polysaccharide, is found in the
exoskeleton of arthropods
• Chitin also provides structural support for the cell walls of
many fungi
(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.
Question 9 – What is the main trait that all lipids share?
• Lipids are the one class of large biological

molecules that do not form polymers
• The unifying feature of lipids is having little
or no affinity for water
• Lipids are hydrophobic because they consist
mostly of hydrocarbons, which form nonpolar
covalent bonds
• The most biologically important lipids are fats,
phospholipids, and steroids
Question 10 – List the two components from which a fat is constructed.
• Fats are constructed from two types of smaller

molecules: glycerol and fatty acids
• Glycerol is a three-carbon alcohol with a
hydroxyl group attached to each carbon
• A fatty acid consists of a carboxyl group
attached to a long carbon skeleton
• In a fat, three fatty acids are joined to glycerol
by an ester linkage, creating a triacylglycerol,
or triglyceride
Fig. 5-11a
Fatty acid
(palmitic acid)
Glycerol
(a) Dehydration reaction in the synthesis of a fat
Fig. 5-11
Fatty acid
(palmitic acid)
Glycerol
(a) Dehydration reaction in the synthesis of a fat
Ester linkage
(b) Fat molecule (triacylglycerol)

Question 11 - From a structural standpoint, what is the main difference
between saturated and unsaturated fats?
• Fatty acids vary in length (number of carbons)

and in the number and locations of double
bonds
• Saturated fatty acids have the maximum
number of hydrogen atoms possible and no
double bonds
• Unsaturated fatty acids have one or more
double bonds
Animation: Fats

Fig. 5-12
Structural
formula of a
saturated fat
molecule
Stearic acid, a
saturated fatty
acid
(a) Saturated fat
Structural formula
of an unsaturated
fat molecule
Oleic acid, an
unsaturated
fatty acid
cis double
bond causes
(b) Unsaturated fat bending
Question 11 – Saturated/unsaturated fats, cont.
Saturated fats:
• are solid at room temperature
• are found in animals
• Are associated with cardiovascular disease
• Hydrogenation is the process of converting unsaturated
fats to saturated fats by adding hydrogen
• Hydrogenating vegetable oils also creates unsaturated fats
with trans double bonds
• These trans fats may contribute more than saturated fats to
cardiovascular disease

Question 11 – Saturated/unsaturated fats, cont.
Unsaturated fats:
• Fats made from unsaturated fatty acids are called
unsaturated fats or oils, and are liquid at room temperature
• are liquid at room temperature
• usually come from plants and fish
• are associated with healthy cardiovascular systems

Question 13 – What are some of the useful purposes fat serves for humans?
• The major function of fats

is energy storage
• Humans and other
mammals store their fat in
adipose cells
• Adipose tissue also
cushions vital organs and
insulates the body

Fig. 5-13
In a phospholipid, two
Hydrophilic head
Choline hydrophobic fatty acids

and a hydrophilic
Phosphate
phosphate group are
Glycerol attached to glycerol
Hydrophobic tails
Fatty acids
Hydrophilic
head
Hydrophobic
tails
(a) Structural formula (b) Space-filling model (c) Phospholipid symbol

• When phospholipids are added to water, they
self-assemble into a bilayer, with the
hydrophobic tails pointing toward the interior
• The structure of phospholipids results in a
bilayer arrangement found in cell membranes
• Phospholipids are the major component of all
cell membranes

Fig. 5-14
Hydrophilic WATER
head
Hydrophobic
WATER
tail
Question 15 – Describe the structure of steroids. Why is cholesterol important to
humans?
• Steroids are lipids characterized by a carbon

skeleton consisting of four fused rings

Question 15 – Describe the structure of steroids. Why is cholesterol important to
humans?
• Cholesterol, an important steroid, is a

component in animal cell membranes
– Cholesterol helps cell membranes remain
flexible in cold temps
• Although cholesterol is essential in animals,

high levels in the blood may contribute to
cardiovascular disease

Question 16 – What is the origin of the word “protein.”
• Comes from the Greek word proteios, which

means “first place.”
• Proteins account for more than 50% of the dry
mass of most cells
• Protein functions include structural support,
storage, transport, cellular communications,
movement, enzymatic functions, and defense
against foreign substances

More protein stuff!
• Life would not be possible without enzymes, most

of which are proteins.
• Enzymatic proteins regulate metabolism by acting
as catalysts, chemical agents that speed up
chemical reactions without being consumed by the
reaction.
• #17. Diverse as proteins are, they are all polymers
constructed from the same set of 20 amino acids.
Polymers of amino acids are called polypeptides.
A protein consists of one or more polypeptides.

Table 5-1
Fig. 5-16
Substrate
(sucrose)
Glucose
Enzyme
(sucrase)
OH
H2O
Fructose
HO
Question 18 – Draw the basic structure of an amino acid.
• Amino acids are organic molecules with carboxyl and

amino groups
• Amino acids differ in their properties due to differing side
chains, called R groups
Amino
Carboxyl
Group
Group

Fig. 5-17
Nonpolar
Glycine Alanine Valine Leucine Isoleucine

(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)
Methionine Phenylalanine Trypotphan Proline

(Met or M) (Phe or F) (Trp or W) (Pro or P)
Polar
Serine Threonine Cysteine Tyrosine Asparagine Glutamine

(Ser or S) (Thr or T) (Cys or C) (Tyr or Y) (Asn or N) (Gln or Q)
Electrically
charged
Acidic Basic
Aspartic acid Glutamic acid Lysine Arginine Histidine

(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)
Question 19 – What is the covalent bond called that holds two amino acids
together? What type of Rx is it? Draw an example.
• Amino acids are linked by peptide bonds

• A polypeptide is a polymer of amino acids
• Polypeptides range in length from a few to
more than a thousand monomers
• Each polypeptide has a unique linear sequence
of amino acids
• They are joined through dehydration reactions.

Fig. 5-18
Peptide
bond
(a)
Side chains
Peptide
bond
Backbone
Amino end Carboxyl end

(b) (N-terminus) (C-terminus)
Question 20 – Are the terms polypeptide and protein synonymous? Explain.
• They are not synonymous.

• A polypeptide is the linear sequence of amino
acids
• A protein is one or more polypeptides precisely
twisted, folded, and coiled into a unique shape.
• Think yarn and sweater example.

Question 21
• The sequence of amino acids determines a protein’s three-

dimensional structure
• A protein’s structure determines its function
• Ex:
– Antibody binding to a flu virus
– An enzyme recognizing and binding to its substrate
– Endorphins binding to specific protein receptors in the
brain
– Cystic fibrosis

Question 22 – List and briefly describe the four levels of protein structure.
• The primary structure of a protein is its unique

sequence of amino acids
– determined by inherited genetic information
• Secondary structure, found in most proteins,
consists of coils and folds in the polypeptide
chain
– result from hydrogen bonds between repeating
constituents of the polypeptide backbone
Animation: Protein Structure Introduction

Question 22 – List and briefly describe the four levels of protein structure.
• Tertiary structure is determined by interactions among

various side chains (R groups)
– determined by interactions between R groups,
• Quaternary structure results when a protein consists of
multiple polypeptide chains
– results when two or more polypeptide chains form one
macromolecule
– Collagen (40% of human body) is a fibrous protein
consisting of three polypeptides coiled like a rope
– Hemoglobin is a globular protein consisting of four
polypeptides: two alpha and two beta chains

Fig. 5-21
Primary Secondary Tertiary Quaternary

Structure Structure Structure Structure
pleated sheet
+H N
3
Amino end
Examples of
amino acid
subunits
helix
Sickle-Cell Disease: A Change in
Primary Structure
• A slight change in primary structure can affect

a protein’s structure and ability to function
• Sickle-cell disease, an inherited blood disorder,
results from a single amino acid substitution in
the protein hemoglobin

Fig. 5-22
Normal hemoglobin Sickle-cell hemoglobin
Val His Leu Thr Pro Glu Glu
Primary
Primary Val His Leu Thr Pro Val Glu
structure
structure 1 2 3 4 5 6 7 1 2 3 4 5 6 7
Exposed
Secondary Secondary hydrophobic
and tertiary subunit and tertiary region subunit
structures structures
Quaternary Normal Quaternary Sickle-cell

structure hemoglobin structure hemoglobin
(top view)
Function Molecules do Function Molecules

not associate interact with
with one one another and
another; each crystallize into
carries oxygen. a fiber; capacity
to carry oxygen
is greatly reduced.
10 µm 10 µm
Red blood Normal red blood Red blood Fibers of abnormal

cell shape cells are full of cell shape hemoglobin deform
individual red blood cell into
hemoglobin sickle shape.
moledules, each
carrying oxygen.
Fig. 5-22c
10 µm 10 µm
Normal red blood Fibers of abnormal

cells are full of hemoglobin deform
individual red blood cell into
hemoglobin sickle shape.
molecules, each
carrying oxygen.
Question 23 – What happens when a protein is denatured? What are some
environmental factors that can cause this?
• In addition to primary structure, physical and

chemical conditions can affect structure
• This loss of a protein’s native structure is called
denaturation
• Alterations in pH, salt concentration,
temperature, or other environmental factors
can cause a protein to unravel
• A denatured protein is biologically inactive

Concept 5.5: Nucleic acids store and transmit
hereditary information
• The amino acid sequence of a polypeptide is

programmed by a unit of inheritance called a
gene
• Genes are made of DNA, a nucleic acid

Question 24 – List the two types of nucleic acids.
• There are two types of nucleic acids:

– Deoxyribonucleic acid (DNA)
– Ribonucleic acid (RNA)
• DNA provides directions for its own replication

• DNA directs synthesis of messenger RNA
(mRNA) and, through mRNA, controls protein
synthesis
• Protein synthesis occurs in ribosomes
Fig. 5-26-1
DNA
1 Synthesis of
mRNA in the
nucleus mRNA
NUCLEUS
CYTOPLASM
Fig. 5-26-2
DNA
1 Synthesis of
mRNA in the
nucleus mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm
via nuclear pore
Fig. 5-26-3
DNA
1 Synthesis of
mRNA in the
nucleus mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm Ribosome
via nuclear pore
3 Synthesis
of protein
Amino
Polypeptide acids
The Structure of Nucleic Acids
• Nucleic acids are polymers called

polynucleotides
• Each polynucleotide is made of monomers
called nucleotides
• Each nucleotide consists of a nitrogenous
base, a pentose sugar, and a phosphate group

Fig. 5-27
5 end
Nitrogenous bases
Pyrimidines
5 C
3 C
Nucleoside
Nitrogenous
base Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA)
Purines
Phosphate
group Sugar
5 C (pentose)
Adenine (A) Guanine (G)
3 C (b) Nucleotide
Sugars
3 end
(a) Polynucleotide, or nucleic acid
Deoxyribose (in DNA) Ribose (in RNA)
(c) Nucleoside components: sugars

Fig. 5-27ab
5' end
5'C
3'C
Nucleoside
Nitrogenous
base
5'C
Phosphate 3'C
group Sugar
5'C (pentose)
3'C (b) Nucleotide
3' end
(a) Polynucleotide, or nucleic acid
Nucleotide Monomers
• There are two families of nitrogenous bases:

– Pyrimidines (cytosine, thymine, and uracil)
have a single six-membered ring
– Purines (adenine and guanine) have a six-
membered ring fused to a five-membered ring

Question 27 – What shape is a DN molecule? What is meant when DNA is
described as being antiparallel?
• A DNA molecule has two polynucleotides spiraling

around an imaginary axis, forming a double helix
• In the DNA double helix, the two backbones run in
opposite 5 → 3 directions from each other, an
arrangement referred to as antiparallel
• One DNA molecule includes many genes
• The nitrogenous bases in DNA pair up and form
hydrogen bonds: adenine (A) always with thymine
(T), and guanine (G) always with cytosine (C)

Fig. 5-28
5' end 3' end
Sugar-phosphate
backbones
Base pair (joined by

hydrogen bonding)
Old strands
Nucleotide
about to be
added to a
new strand
3' end
5' end
New
strands
3' end 5' end
5' end 3' end

DNA and Proteins as Tape Measures of Evolution
• The linear sequences of nucleotides in DNA

molecules are passed from parents to offspring
• Two closely related species are more similar in
DNA than are more distantly related species
• Molecular biology can be used to assess
evolutionary kinship

You should now be able to:
1. List and describe the four major classes of molecules

2. Describe the formation of a glycosidic linkage and
distinguish between monosaccharides, disaccharides,
and polysaccharides
3. Distinguish between saturated and unsaturated fats and
between cis and trans fat molecules
4. Describe the four levels of protein structure
5. Distinguish between the following pairs: pyrimidine and
purine, nucleotide and nucleoside, ribose and
deoxyribose, the 5 end and 3 end of a nucleotide

AP Bio Chapter 5 Lecture

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Chapter 5

The Structure and Function of

PowerPoint® Lecture Presentations for

• All living things are made up of four classes of

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• A condensation reaction, or more specifically

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Short polymer Unlinked monomer

Dehydration removes a water

Hydrolysis adds a water H2O

(b) Hydrolysis of a polymer

• Carbohydrates include sugars and the polymers of sugars

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

(b) Abbreviated ring structure

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Glucose Glucose Maltose

Glucose Fructose Sucrose

• Polysaccharides, consist of three or more

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• Starch, a storage polysaccharide of plants,

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Chloroplast Starch Mitochondria Glycogen granules

(a) Starch: a plant polysaccharide (b) Glycogen: an animal polysaccharide

• Cellulose is the most abundant organic

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

(b) Starch: 1–4 linkage of alpha glucose monomers

(c) Cellulose: 1–4 linkage of beta glucose monomers

• Enzymes that digest starch by hydrolyzing 

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• Lipids are the one class of large biological

• Fats are constructed from two types of smaller

(b) Fat molecule (triacylglycerol)

• Fatty acids vary in length (number of carbons)

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• The major function of fats

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Choline hydrophobic fatty acids

(a) Structural formula (b) Space-filling model (c) Phospholipid symbol

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• Steroids are lipids characterized by a carbon

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• Cholesterol, an important steroid, is a

• Although cholesterol is essential in animals,

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• Comes from the Greek word proteios, which

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• Life would not be possible without enzymes, most

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• Amino acids are organic molecules with carboxyl and

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Glycine Alanine Valine Leucine Isoleucine

Methionine Phenylalanine Trypotphan Proline

Serine Threonine Cysteine Tyrosine Asparagine Glutamine

Aspartic acid Glutamic acid Lysine Arginine Histidine

• Amino acids are linked by peptide bonds

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Amino end Carboxyl end

• They are not synonymous.

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

• The sequence of amino acids determines a protein’s three-

Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings