Chapter 5

Biological
Macromolecules
and Lipids

Lecture Presentations by
Nicole Tunbridge and
© 2018 Pearson Education Ltd.
Kathleen Fitzpatrick
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 and are
complex
 Large biological molecules have unique properties
that arise from the orderly arrangement of their
atoms

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Figure 5.1

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Figure 5.1a

The scientist in the foreground is using

3-D glasses to help her visualize the
structure of the protein displayed on her
screen.

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Concept 5.1: Macromolecules are polymers,
built from monomers
 A polymer is a long molecule consisting of many
similar building blocks
 The repeating units that serve as building blocks are
called monomers
 Carbohydrates, proteins, and nucleic acids are
polymers

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The Synthesis and Breakdown of Polymers

 Enzymes are specialized macromolecules that

speed up chemical reactions such as those that
make or break down 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

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Figure 5.2
(a) Dehydration reaction: synthesizing a polymer

1 2 3
Short polymer Unlinked
monomer
Dehydration removes a water
molecule, forming a new bond. H2O

1 2 3 4

Longer polymer

(b) Hydrolysis: breaking down a polymer

1 2 3 4

Hydrolysis adds a water H2O

molecule, breaking a bond.

1 2 3 H
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The Diversity of Polymers

 A cell has thousands of different macromolecules

 Macromolecules vary among cells of an organism,
vary more within a species, and vary even more
between species
 A huge variety of polymers can be built from a small
set of monomers

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Concept 5.2: Carbohydrates serve as fuel and
building material
 Carbohydrates include sugars and the polymers of
sugars
 The simplest carbohydrates are monosaccharides,
or simple sugars
 Carbohydrate macromolecules are polysaccharides,
polymers composed of many sugar building blocks

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Sugars

 Monosaccharides have molecular formulas

that are usually multiples of CH2O
 Glucose (C6H12O6) is the most common
monosaccharide
 Monosaccharides are classified by
 The location of the carbonyl group (as aldose
or ketose)
 The number of carbons in the carbon skeleton

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Figure 5.3
Aldoses Ketoses
(Aldehyde Sugars) (Ketone Sugars)
Trioses: three-carbon sugars (C3H6O3)

Glyceraldehyde Dihydroxyacetone
Pentoses: five-carbon sugars (C5H10O5)

Ribose Ribulose
Hexoses: six-carbon sugars (C6H12O6)

Glucose Galactose Fructose

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Figure 5.3a

Aldose Ketose
(Aldehyde Sugar) (Ketone Sugar)

Trioses: three-carbon sugars (C3H6O3)

Glyceraldehyde Dihydroxyacetone

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Figure 5.3b

Aldose Ketose
(Aldehyde Sugar) (Ketone Sugar)

Pentoses: five-carbon sugars (C5H10O5)

Ribose Ribulose

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Figure 5.3c

Aldose Ketose
(Aldehyde Sugar) (Ketone Sugar)

Hexoses: six-carbon sugars (C6H12O6)

Glucose Galactose Fructose

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 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

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Figure 5.4

(a) Linear and ring forms

(b) Abbreviated ring structure

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 A disaccharide is formed when a dehydration
reaction joins two monosaccharides
 This covalent bond is called a glycosidic linkage

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Figure 5.5

(a) Dehydration reaction in the synthesis of maltose

1–4
glycosidic
linkage

H2O
Glucose Glucose Maltose

(b) Dehydration reaction in the synthesis of sucrose

1–2
glycosidic
linkage

H2O
Glucose Fructose Sucrose

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Polysaccharides

 Polysaccharides, the polymers of sugars, have

storage and structural roles
 The architecture and function of a polysaccharide
are determined by its sugar monomers and the
positions of its glycosidic linkages

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Storage Polysaccharides

 Starch, a storage polysaccharide of plants, consists

of glucose monomers
 Plants store surplus starch as granules within
chloroplasts and other plastids
 The simplest form of starch is amylose

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Figure 5.6

Storage structures (plastids)

containing starch granules Amylose (unbranched)
in a potato tuber cell

Glucose
Amylopectin monomer
(somewhat branched)
50 µm
(a) Starch
Muscle
tissue
Glycogen granules Glycogen (extensively
stored in muscle branched)
tissue

Cell
1 µm
wall
(b) Glycogen
Plant cell,
surrounded Cellulose microfibrils Cellulose molecule
by cell wall in a plant cell wall (unbranched)
10 µm
Hydrogen bonds
Microfibril

0.5 µm

(c) Cellulose

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Figure 5.6a

Storage structures (plastids) Amylose Glucose

containing starch granules (unbranched) monomer
in a potato tuber cell

Amylopectin
(somewhat branched)
50 µm
(a) Starch

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Figure 5.6b

Glycogen granules Glycogen

stored in muscle (extensively branched)
tissue

1 µm

(b) Glycogen

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Figure 5.6c

Cellulose microfibrils
in a plant cell wall Cellulose molecule (unbranched)

Hydrogen bonds
Microfibril

0.5 µm

(c) Cellulose

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Figure 5.6d

Cell
wall

Plant cell,
surrounded 10 µm
by cell wall

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 Glycogen is a storage polysaccharide in animals
 Glycogen is stored mainly in liver and muscle cells
 Hydrolysis of glycogen in these cells releases
glucose when the demand for sugar increases

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Structural Polysaccharides

 The polysaccharide cellulose is a major component

of the tough wall of plant cells
 Like starch, cellulose is a polymer of glucose, but the
glycosidic linkages differ
 The difference is based on two ring forms for
glucose: alpha (α) and beta (β)

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Figure 5.7

α Glucose β Glucose

(a) α and β glucose ring structures

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

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

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Figure 5.7a

α Glucose β Glucose

(a) α and β glucose ring structures

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Figure 5.7b

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

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

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 Starch (α configuration) is largely helical
 Cellulose molecules (β configuration) are straight
and unbranched
 Some hydroxyl groups on the monomers of cellulose
can hydrogen-bond with hydroxyls of parallel
cellulose molecules

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 Enzymes that digest starch by hydrolyzing α linkages
can’t hydrolyze β linkages in cellulose
 The 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

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 Chitin, another structural polysaccharide, is found in
the exoskeleton of arthropods
 Chitin also provides structural support for the cell
walls of many fungi

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Figure 5.8

The structure
of the chitin
monomer

Chitin, embedded in proteins,

forms the exoskeleton of
arthropods.

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Concept 5.3: Lipids are a diverse group of
hydrophobic molecules
 Lipids are the one class of large biological
molecules that does not include true polymers
 The unifying feature of lipids is that they mix poorly,
if at all, with water
 Lipids consist mostly of hydrocarbon regions
 The most biologically important lipids are fats,
phospholipids, and steroids

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Fats

 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

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Figure 5.9a

H2O Fatty acid

(in this case, palmitic acid)

Glycerol

(a) One of three dehydration reactions in the synthesis of a fat

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Figure 5.9b

Ester linkage

(b) Fat molecule (triacylglycerol)

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 Fats separate from water because water molecules
hydrogen-bond to each other and exclude the fats
 In a fat, three fatty acids are joined to glycerol
by an ester linkage, creating a triacylglycerol,
or triglyceride
 The fatty acids in a fat can be all the same or of
two or three different kinds

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 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

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Figure 5.10

(a) Saturated fat (b) Unsaturated fat

Structural formula
of a saturated fat
molecule

Structural formula
of an unsaturated
Space-filling model fat molecule
of stearic acid, a
saturated fatty acid
Space-filling model
of oleic acid, an
unsaturated fatty
acid
Cis double bond
causes bending.

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Figure 5.10b
(b) Unsaturated fat

Structural formula
of an unsaturated
fat molecule

Space-filling model of
oleic acid, an
unsaturated fatty acid

Cis double bond

causes bending.
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 Fats made from saturated fatty acids are called
saturated fats and are solid at room temperature
 Most animal fats are saturated
 Fats made from unsaturated fatty acids are called
unsaturated fats or oils and are liquid at room
temperature
 Plant fats and fish fats are usually unsaturated

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 A diet rich in saturated fats may contribute to
cardiovascular disease through plaque deposits
 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

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 The major function of fats is energy storage
 Humans and other mammals store their long-term
food reserves in adipose cells
 Adipose tissue also cushions vital organs and
insulates the body

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Phospholipids

 In a phospholipid, two fatty acids and a phosphate

group are attached to glycerol
 The two fatty acid tails are hydrophobic, but the
phosphate group and its attachments form a
hydrophilic head

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Figure 5.11

Choline Hydrophilic
Hydrophilic head

head

Phosphate Hydrophobic
tails
Glycerol
(c) Phospholipid symbol

Fatty acids
Hydrophobic tails

Kink due to cis

double bond

(a) Structural formula (b) Space-filling model (d) Phospholipid bilayer

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 When phospholipids are added to water, they
self-assemble into double-layered sheets
called bilayers
 At the surface of a cell, phospholipids are also
arranged in a bilayer, with the hydrophobic tails
pointing toward the interior
 The phospholipid bilayer forms a boundary between
the cell and its external environment

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Steroids

 Steroids are lipids characterized by a carbon

skeleton consisting of four fused rings
 Cholesterol, a type of steroid, is a component in
animal cell membranes and a precursor from which
other steroids are synthesized
 A high level of cholesterol in the blood may
contribute to cardiovascular disease

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Figure 5.12

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Concept 5.4: Proteins include a diversity
of structures, resulting in a wide range
of functions
 Proteins account for more than 50% of the dry mass
of most cells
 Some proteins speed up chemical reactions
 Other protein functions include defense, storage,
transport, cellular communication, movement, and
structural support

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Figure 5.13a

Enzymatic proteins Defensive proteins

Function: Selective acceleration of Function: Protection against disease
chemical reactions Example: Antibodies inactivate and help
Example: Digestive enzymes catalyze the destroy viruses and bacteria.
hydrolysis of bonds in food molecules.
Antibodies

Enzyme Virus Bacterium

Storage proteins Transport proteins

Function: Storage of amino acids Function: Transport of substances
Examples: Casein, the protein of milk, is Examples: Hemoglobin, the iron-containing
the major source of amino acids for baby protein of vertebrate blood, transports
mammals. Plants have storage proteins in oxygen from the lungs to other parts of the
their seeds. Ovalbumin is the protein of body. Other proteins transport molecules
egg white, used as an amino acid source across membranes, as shown here.
for the developing embryo.
Transport
protein

Ovalbumin Amino acids

for embryo Cell membrane

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Figure 5.13b

Hormonal proteins Receptor proteins

Function: Coordination of an organism’s Function: Response of cell to chemical
activities stimuli
Example: Insulin, a hormone secreted by Example: Receptors built into the
the pancreas, causes other tissues to take membrane of a nerve cell detect signaling
up glucose, thus regulating blood sugar molecules released by other nerve cells.
concentration.
Receptor
protein
High Insulin Normal Signaling
blood sugar secreted blood sugar molecules

Contractile and motor proteins Structural proteins

Function: Movement Function: Support
Examples: Motor proteins are responsible Examples: Keratin is the protein of hair,
for the undulations of cilia and flagella. horns, feathers, and other skin appendages.
Actin and myosin proteins are responsible Insects and spiders use silk fibers to make
for the contraction of muscles. their cocoons and webs, respectively.
Collagen and elastin proteins provide a
fibrous framework in animal connective
Actin Myosin tissues.

Collagen

Muscle
30 µm
tissue Connective
60 µm
tissue
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 Enzymes are proteins that act as catalysts to speed
up chemical reactions
 Enzymes can perform their functions repeatedly,
functioning as workhorses that carry out the
processes of life

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 Proteins are all constructed from the same set of 20
amino acids
 Polypeptides are unbranched polymers built from
these amino acids
 A protein is a biologically functional molecule that
consists of one or more polypeptides

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Amino Acid Monomers

 Amino acids are organic molecules with amino and

carboxyl groups
 Amino acids differ in their properties due to differing
side chains, called R groups

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Figure 5.UN01

Side chain (R group)

α carbon

Amino Carboxyl
group group

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Figure 5.14
Nonpolar side chains; hydrophobic
Side chain (R group)

Glycine Alanine Valine Leucine Isoleucine

(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)

Methionine Phenylalanine Tryptophan Proline

(Met or M) (Phe or F) (Trp or W) (Pro or P)
Polar side chains; hydrophilic

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 side chains; hydrophilic
Basic (positively charged)

Acidic (negatively charged)

Aspartic acid Glutamic acid Lysine Arginine Histidine

(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)
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Polypeptides (Amino Acid Polymers)

 Amino acids are linked by covalent bonds called

peptide bonds
 A polypeptide is a polymer of amino acids
 Polypeptides range in length from a few to more
than 1,000 monomers
 Each polypeptide has a unique linear sequence of
amino acids, with a carboxyl end (C-terminus) and
an amino end (N-terminus)

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Figure 5.15a

Peptide bond
H2O

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Figure 5.15b

Side
chains
(R
groups)

Back-
bone

Peptide
Amino end Carboxyl end
bond
(N-terminus) (C-terminus)

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Protein Structure and Function

 The specific activities of proteins result from their

intricate three-dimensional architecture
 A functional protein consists of one or more
polypeptides precisely twisted, folded, and coiled
into a unique shape

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Figure 5.16
Structural Models Target molecule (on bacterial
cell surface) bound to lysozyme

Space-filling model Ribbon model Wire-frame model (blue)

Simplified Diagrams Insulin-producing cell

in pancreas

Enzyme Insulin

A transparent A solid shape is

shape shows the used when A simple shape is used A protein can be
overall shape of structural details here to represent a represented simply
the molecule are not needed. generic enzyme. as a dot.
and some
internal details.
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 The sequence of amino acids determines a protein’s
three-dimensional structure
 A protein’s structure determines how it works
 The function of a protein usually depends on
its ability to recognize and bind to some other
molecule

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Figure 5.17

Antibody protein Protein from flu virus

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Four Levels of Protein Structure

 The primary structure of a protein is its unique

sequence of amino acids
 Secondary structure, found in most proteins,
consists of coils and folds in the polypeptide chain
 Tertiary structure is determined by interactions
among various side chains (R groups)
 Quaternary structure results when a protein consists
of multiple polypeptide chains

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Figure 5.18a
Primary Structure

Amino
acids

1 5 10

Amino end
30 25 20 15

35 40 45 50

Primary structure of transthyretin

55
70 65 60

75
80 85 90

95
115 110 105 100

120 125
Carboxyl end
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Figure 5.18aa

Primary Structure

Amino
acids

1 5 10

Amino end
30 25 20 15

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Figure 5.18b

Secondary Tertiary Quaternary

Structure Structure Structure

α helix α helix
Single
Hydrogen bond polypeptide
β pleated subunit
β strand sheet
Hydrogen Transthyretin Transthyretin
bond polypeptide protein

β pleated sheet

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Figure 5.18ba

Secondary Structure

α helix

Hydrogen bond

β strand

Hydrogen
bond

β pleated sheet
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Figure 5.18bb

Tertiary Structure

α helix

β pleated sheet

Transthyretin
polypeptide

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Figure 5.18bc

Quaternary Structure

Single
polypeptide
subunit

Transthyretin
protein

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Figure 5.18d

Hydrogen
bond
Hydrophobic
interactions and
van der Waals
interactions

Disulfide
bridge Ionic bond

Polypeptide
backbone

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Figure 5.18e

Collagen

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Figure 5.18f

Heme
Iron
β subunit

α subunit

α subunit

β subunit
Hemoglobin
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 The primary structure of a protein is its sequence
of amino acids
 Primary structure is like the order of letters in a long
word
 Primary structure is determined by inherited genetic
information

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 The coils and folds of secondary structure result
from hydrogen bonds between repeating
constituents of the polypeptide backbone
 Typical secondary structures are a coil called an
α helix and a folded structure called a β pleated
sheet

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 Tertiary structure, the overall shape of a
polypeptide, results from interactions between
R groups, rather than interactions between
backbone constituents
 These interactions include hydrogen bonds,
ionic bonds, hydrophobic interactions, and
van der Waals interactions
 Strong covalent bonds called disulfide bridges may
reinforce the protein’s structure

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 Quaternary structure results when two or more
polypeptide chains form one macromolecule
 Collagen is a fibrous protein consisting of three
polypeptides coiled like a rope
 Hemoglobin is a globular protein consisting of
four polypeptides: two α and two β subunits

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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
 The abnormal hemoglobin molecules cause the red
blood cells to aggregate into chains and to deform
into a sickle shape

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Figure 5.19

Primary Secondary Quaternary Red Blood Cell

and Tertiary Function
Structure Structure Shape
Structures
Normal β Normal Proteins do not associate
1
subunit hemoglobin with one another; each
2
β carries oxygen.
3
Normal

4 α
5
6
7 5 µm
β α

1 Sickle-cell β Sickle-cell Proteins aggregate into a

subunit hemoglobin fiber; capacity to
2
carry oxygen
3
Sickle-cell

β is reduced.
4
5 α
6
7 5 µm
β α

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Figure 5.19a

Secondary
Primary Quaternary
and Tertiary Function
Structure Structure
Structures
1 Normal β Normal Proteins do not associate
subunit hemoglobin with one another; each
2 carries oxygen.
3 β
Normal

4 α
5
6
7
β α

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Figure 5.19b

Secondary
Primary Quaternary
and Tertiary Function
Structure Structure
Structures
Sickle-cell β Sickle-cell Proteins aggregate into a
1
subunit hemoglobin fiber; capacity to
2 carry oxygen
3 β
Sickle-cell

is reduced.
4
α
5
6
7
β α

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What Determines Protein Structure?

 In addition to primary structure, physical and

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

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Figure 5.20

Normal protein Denatured protein

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Protein Folding in the Cell

 It is hard to predict a protein’s structure from its

primary structure
 Most proteins probably go through several stages on
their way to a stable structure
 Diseases such as Alzheimer’s, Parkinson’s, and mad
cow disease are associated with misfolded proteins

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 Scientists use X-ray crystallography to determine a
protein’s structure
 Another method is nuclear magnetic resonance
(NMR) spectroscopy, which does not require protein
crystallization
 Bioinformatics is another approach to prediction of
protein structure from amino acid sequences

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Figure 5.21
Technique
Diffracted
X-rays
X-ray
source
X-ray
beam

Crystal Digital X-ray diffraction

detector pattern

Results

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Concept 5.5: Nucleic acids store, transmit, and
help express hereditary information
 The amino acid sequence of a polypeptide is
programmed by a unit of inheritance called a gene
 Genes consist of DNA, a nucleic acid made of
monomers called nucleotides

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The Roles 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
 This process is called gene expression

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Figure 5.22_1

DNA

1 Synthesis of
mRNA
mRNA

NUCLEUS
CYTOPLASM

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Figure 5.22_2

DNA

1 Synthesis of
mRNA
mRNA

NUCLEUS
CYTOPLASM

mRNA
2 Movement of
mRNA into
cytoplasm

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Figure 5.22_3

DNA

1 Synthesis of
mRNA
mRNA

NUCLEUS
CYTOPLASM

mRNA
2 Movement of
mRNA into
cytoplasm Ribosome

3 Synthesis of
protein

Amino
Polypeptide acids
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 Each gene along a DNA molecule directs synthesis
of a messenger RNA (mRNA)
 The mRNA molecule interacts with the cell’s protein-
synthesizing machinery to direct production of a
polypeptide
 The flow of genetic information can be summarized
as DNA → RNA → protein

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The Components 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 one or more phosphate groups
 The portion of a nucleotide without the phosphate
group is called a nucleoside

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 Nucleoside = nitrogenous base + sugar
 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
 In DNA, the sugar is deoxyribose; in RNA, the
sugar is ribose
 Nucleotide = nucleoside + phosphate group

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Figure 5.23

NITROGENOUS BASES
Pyrimidines

Sugar-phosphate backbone
5′ end (on blue background) Cytosine (C) Thymine Uracil
5′C
(T, in DNA) (U, in RNA)

Purines
3′C

Nucleoside
Nitrogenous
base
Adenine (A) Guanine (G)
5′C

SUGARS
1′C
Phosphate 3′C
5′C group Sugar
(pentose)
3′C
(b) Nucleotide monomer
in a polynucleotide Deoxyribose Ribose
3′ end (in DNA) (in RNA)

(a) Polynucleotide, or nucleic acid (c) Nucleoside components

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Figure 5.23a
Sugar-phosphate backbone
5′ end (on blue background)

5′C

3′C
Nucleoside

Nitrogenous
base

5′C

1′C
Phosphate 3′C
5′C group Sugar
(pentose)
3′C
(b) Nucleotide monomer
3′ end in a polynucleotide

(a) Polynucleotide, or nucleic acid

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Figure 5.23b
NITROGENOUS BASES

Pyrimidines

Cytosine (C) Thymine Uracil

(T, in DNA) (U, in RNA)

Purines

Adenine (A) Guanine (G)

(c) Nucleoside components

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Figure 5.23c

SUGARS

Deoxyribose Ribose
(in DNA) (in RNA)

(c) Nucleoside components

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Nucleotide Polymers

 Nucleotides are linked together by a phosphodiester

linkage to build a polynucleotide
 A phosphodiester linkage consists of a phosphate
group that links the sugars of two nucleotides
 These links create a backbone of sugar-phosphate
units with nitrogenous bases as appendages
 The sequence of bases along a DNA or mRNA
polymer is unique for each gene

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The Structures of DNA and RNA Molecules

 DNA molecules have two polynucleotides spiraling

around an imaginary axis, forming a double helix
 The backbones run in opposite 5′ → 3′ directions
from each other, an arrangement referred to as
antiparallel
 One DNA molecule includes many genes

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 Only certain bases in DNA pair up and form
hydrogen bonds: adenine (A) always with thymine
(T), and guanine (G) always with cytosine (C)
 This is called complementary base pairing
 This feature of DNA structure makes it possible
to generate two identical copies of each DNA
molecule in a cell preparing to divide

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 RNA, in contrast to DNA, is single-stranded
 Complementary pairing can also occur between
two RNA molecules or between parts of the
same molecule
 In RNA, thymine is replaced by uracil (U), so A
and U pair
 While DNA always exists as a double helix, RNA
molecules are more variable in form

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Figure 5.24

5′ 3′ Sugar-phosphate
backbones
Hydrogen bonds

T A
Base pair joined
G
by hydrogen bonding
C
C G
A T
C G G
G C
U C
A
T A

3′ 5′ Base pair joined

by hydrogen bonding
(a) DNA (b) Transfer RNA

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Concept 5.6: Genomics and proteomics have
transformed biological inquiry and applications

 Once the structure of DNA and its relationship to

amino acid sequence was understood, biologists
sought to “decode” genes by learning their base
sequences
 The first chemical techniques for DNA sequencing
were developed in the 1970s and refined over the
next 20 years

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 It is enlightening to sequence the full complement of
DNA in an organism’s genome
 The rapid development of faster and less expensive
methods of sequencing was a side effect of the
Human Genome Project
 Many genomes have been sequenced, generating
large sets of data

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Figure 5.25

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 Bioinformatics uses computer software and other
computational tools to deal with the data resulting
from sequencing many genomes
 Analyzing large sets of genes or even comparing
whole genomes of different species is called
genomics
 A similar analysis of large sets of proteins including
their sequences is called proteomics

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DNA and Proteins as Tape Measures of
Evolution
 Sequences of genes and their protein products
document the hereditary background of an organism
 Linear sequences of DNA molecules are passed
from parents to offspring
 We can extend the concept of “molecular genealogy”
to relationships between species
 Molecular biology has added a new measure to the
toolkit of evolutionary biology

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