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The Molecules of Life

 All living things are made up of four classes of large

biological molecules: carbohydrates, lipids, proteins,
Chapter 5 and nucleic acids
 Macromolecules are large molecules and are
Biological complex
Macromolecules  Large biological molecules have unique properties
that arise from the orderly arrangement of their
and Lipids atoms

Lecture Presentations by
Nicole Tunbridge and
© 2018 Pearson Education Ltd.
Kathleen Fitzpatrick © 2018 Pearson Education Ltd.

Figure 5.1 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, The Synthesis and Breakdown of Polymers
built from monomers
 A polymer is a long molecule consisting of many  Enzymes are specialized macromolecules that
similar building blocks speed up chemical reactions such as those that
 The repeating units that serve as building blocks are make or break down polymers
called monomers  A dehydration reaction occurs when two
 Carbohydrates, proteins, and nucleic acids are monomers bond together through the loss of a
polymers 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 Animation: Polymers
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 Concept 5.2: Carbohydrates serve as fuel and

building material
 A cell has thousands of different macromolecules  Carbohydrates include sugars and the polymers of
 Macromolecules vary among cells of an organism, sugars
vary more within a species, and vary even more  The simplest carbohydrates are monosaccharides,
between species or simple sugars
 A huge variety of polymers can be built from a small  Carbohydrate macromolecules are polysaccharides,
set of monomers polymers composed of many sugar building blocks

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

 Monosaccharides have molecular formulas

that are usually multiples of CH2O
Glyceraldehyde Dihydroxyacetone
 Glucose (C6H12O6) is the most common Pentoses: five-carbon sugars (C5H10O5)

monosaccharide
 Monosaccharides are classified by
 The location of the carbonyl group (as aldose
Ribose Ribulose
or ketose) Hexoses: six-carbon sugars (C6H12O6)

 The number of carbons in the carbon skeleton

Glucose Galactose Fructose

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Figure 5.3a Figure 5.3b

Aldose Ketose
(Aldehyde Sugar) (Ketone Sugar)
Aldose Ketose
(Aldehyde Sugar) (Ketone Sugar)
Pentoses: five-carbon sugars (C5H10O5)
Trioses: three-carbon sugars (C3H6O3)

Glyceraldehyde Dihydroxyacetone
Ribose Ribulose

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Figure 5.3c

Aldose Ketose
(Aldehyde Sugar) (Ketone Sugar)  Though often drawn as linear skeletons, in aqueous
Hexoses: six-carbon sugars (C6H12O6)
solutions many sugars form rings
 Monosaccharides serve as a major fuel for cells and
as raw material for building molecules

Glucose Galactose Fructose

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Figure 5.4

 A disaccharide is formed when a dehydration

reaction joins two monosaccharides
 This covalent bond is called a glycosidic linkage

(a) Linear and ring forms

(b) Abbreviated ring structure

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Figure 5.5
Animation: Disaccharides
(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 Storage Polysaccharides

 Polysaccharides, the polymers of sugars, have  Starch, a storage polysaccharide of plants, consists
storage and structural roles of glucose monomers
 The architecture and function of a polysaccharide  Plants store surplus starch as granules within
are determined by its sugar monomers and the chloroplasts and other plastids
positions of its glycosidic linkages  The simplest form of starch is amylose

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Figure 5.6 Figure 5.6a

Storage structures (plastids)

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

Glucose
Amylopectin monomer
(somewhat branched)
Storage structures (plastids) Amylose Glucose
50 µm
containing starch granules (unbranched) monomer
(a) Starch
Muscle
tissue in a potato tuber cell
Glycogen granules Glycogen (extensively
stored in muscle branched)
tissue

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

0.5 µm

(c) Cellulose

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Figure 5.6aa Figure 5.6b

Glycogen granules Glycogen

Storage structures (plastids)
stored in muscle (extensively branched)
containing starch granules
tissue
in a potato tuber cell

1 µm

50 µm (b) Glycogen

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Figure 5.6ba Figure 5.6c

Glycogen granules Cellulose microfibrils

stored in muscle in a plant cell wall Cellulose molecule (unbranched)
tissue
Hydrogen bonds
Microfibril

0.5 µm

1 µm (c) Cellulose

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Figure 5.6ca Figure 5.6d

Cellulose microfibrils Cell

in a plant cell wall wall

Plant cell,
0.5 µm surrounded 10 µm
by cell wall

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Animation: Polysaccharides

 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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Figure 5.7
Structural Polysaccharides

 The polysaccharide cellulose is a major component

of the tough wall of plant cells α Glucose β Glucose

 Like starch, cellulose is a polymer of glucose, but the

glycosidic linkages differ (a) α and β glucose ring structures

 The difference is based on two ring forms for

glucose: alpha (α) and beta (β)
(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 Figure 5.7b

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

α Glucose β Glucose

(a) α and β glucose ring structures

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

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 Starch (α configuration) is largely helical  Enzymes that digest starch by hydrolyzing α linkages
 Cellulose molecules (β configuration) are straight can’t hydrolyze β linkages in cellulose
and unbranched  The cellulose in human food passes through the
 Some hydroxyl groups on the monomers of cellulose digestive tract as “insoluble fiber”
can hydrogen-bond with hydroxyls of parallel  Some microbes use enzymes to digest cellulose
cellulose molecules  Many herbivores, from cows to termites, have
symbiotic relationships with these microbes

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Figure 5.8

 Chitin, another structural polysaccharide, is found in The structure

of the chitin
the exoskeleton of arthropods monomer

 Chitin also provides structural support for the cell

walls of many fungi

Chitin, embedded in proteins,

forms the exoskeleton of
arthropods.

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Figure 5.8a
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
Chitin, embedded in proteins,
forms the exoskeleton of
arthropods.

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Figure 5.9
Fats

H2O Fatty acid

 Fats are constructed from two types of smaller (in this case, palmitic acid)

molecules: glycerol and fatty acids

Glycerol
 Glycerol is a three-carbon alcohol with a hydroxyl (a) One of three dehydration reactions in the synthesis of a fat

group attached to each carbon Ester linkage

 A fatty acid consists of a carboxyl group attached to

a long carbon skeleton

(b) Fat molecule (triacylglycerol)

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Figure 5.9a Figure 5.9b

Ester linkage

H2O Fatty acid

(in this case, palmitic acid)

Glycerol

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

(b) Fat molecule (triacylglycerol)

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Animation: Fats

 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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Figure 5.10

(a) Saturated fat (b) Unsaturated fat

 Fatty acids vary in length (number of carbons) and in
the number and locations of double bonds
Structural formula
 Saturated fatty acids have the maximum number of of a saturated fat
molecule
hydrogen atoms possible and no double bonds
 Unsaturated fatty acids have one or more double Structural formula
of an unsaturated
bonds Space-filling model
of stearic acid, a
fat molecule

saturated fatty acid

Space-filling model
of oleic acid, an
unsaturated fatty
acid
Cis double bond
causes bending.

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Figure 5.10a Figure 5.10aa

(a) Saturated fat

Structural formula
of a saturated fat
molecule

Space-filling model of
stearic acid, a
saturated fatty acid

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Figure 5.10b Figure 5.10ba

(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  A diet rich in saturated fats may contribute to
saturated fats and are solid at room temperature cardiovascular disease through plaque deposits
 Most animal fats are saturated  Hydrogenation is the process of converting
 Fats made from unsaturated fatty acids are called unsaturated fats to saturated fats by adding
unsaturated fats or oils and are liquid at room hydrogen
temperature  Hydrogenating vegetable oils also creates
 Plant fats and fish fats are usually unsaturated unsaturated fats with trans double bonds
 These trans fats may contribute more than
saturated fats to cardiovascular disease

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Phospholipids

 The major function of fats is energy storage  In a phospholipid, two fatty acids and a phosphate
 Humans and other mammals store their long-term group are attached to glycerol
food reserves in adipose cells  The two fatty acid tails are hydrophobic, but the
 Adipose tissue also cushions vital organs and phosphate group and its attachments form a
insulates the body hydrophilic head

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Figure 5.11 Figure 5.11a

Choline
Hydrophilic head

Choline Hydrophilic
Hydrophilic head

head
Phosphate
Phosphate Hydrophobic
tails
Glycerol
Glycerol
(c) Phospholipid symbol

Fatty acids Fatty acids

Hydrophobic tails
Hydrophobic tails

Kink due to cis

double bond Kink due to cis
double bond

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

(a) Structural formula (b) Space-filling model

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Figure 5.11b

 When phospholipids are added to water, they

self-assemble into double-layered sheets
called bilayers
Hydrophilic
head
 At the surface of a cell, phospholipids are also
arranged in a bilayer, with the hydrophobic tails
pointing toward the interior
Hydrophobic
tails  The phospholipid bilayer forms a boundary between
the cell and its external environment
(c) Phospholipid symbol (d) Phospholipid bilayer

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Figure 5.12
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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Video: Space-filling Model of Cholesterol Video: Stick Model of Cholesterol

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Figure 5.13a
Concept 5.4: Proteins include a diversity
of structures, resulting in a wide range Enzymatic proteins Defensive proteins
of functions Function: Selective acceleration of
chemical reactions
Function: Protection against disease
Example: Antibodies inactivate and help
Example: Digestive enzymes catalyze the destroy viruses and bacteria.
 Proteins account for more than 50% of the dry mass hydrolysis of bonds in food molecules.
Antibodies
of most cells
Enzyme Virus Bacterium

 Some proteins speed up chemical reactions

Storage proteins Transport proteins
 Other protein functions include defense, storage, Function: Storage of amino acids Function: Transport of substances
Examples: Casein, the protein of milk, is Examples: Hemoglobin, the iron-containing
transport, cellular communication, movement, and 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
structural support 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 5.13aa Figure 5.13ab

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

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Figure 5.13ac Figure 5.13aca

Storage proteins
Function: Storage of amino acids
Examples: Casein, the protein of milk, is
the major source of amino acids for baby
mammals. Plants have storage proteins in
their seeds. Ovalbumin is the protein of
egg white, used as an amino acid source
for the developing embryo.

Ovalbumin Amino acids

for embryo

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Figure 5.13ad 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.
Transport proteins concentration.
Function: Transport of substances Receptor
protein
Examples: Hemoglobin, the iron-containing High Insulin Normal Signaling
protein of vertebrate blood, transports blood sugar secreted blood sugar molecules
oxygen from the lungs to other parts of the
body. Other proteins transport molecules Contractile and motor proteins Structural proteins
across membranes, as shown here. Function: Movement Function: Support
Examples: Motor proteins are responsible Examples: Keratin is the protein of hair,
Transport for the undulations of cilia and flagella. horns, feathers, and other skin appendages.
protein 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
Cell membrane
fibrous framework in animal connective
Actin Myosin tissues.

Collagen

Muscle
30 µm
tissue Connective
60 µm
tissue
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Figure 5.13ba Figure 5.13bb

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
Insulin Signaling
High Normal
secreted molecules
blood sugar blood sugar

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Figure 5.13bc Figure 5.13bca

Contractile and motor proteins

Function: Movement
Examples: Motor proteins are responsible
for the undulations of cilia and flagella.
Actin and myosin proteins are responsible
for the contraction of muscles.

Actin Myosin
Muscle
tissue 30 µm

Muscle
tissue 30 µm

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Figure 5.13bd Figure 5.13bda

Structural proteins
Function: Support
Examples: Keratin is the protein of hair,
horns, feathers, and other skin appendages.
Insects and spiders use silk fibers to make
their cocoons and webs, respectively.
Collagen and elastin proteins provide a
fibrous framework in animal connective
tissues.
Connective
tissue 60 µm
Collagen

Connective
tissue 60 µm

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Animation: Contractile Proteins Animation: Defensive Proteins

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Animation: Enzymes Animation: Gene Regulatory Proteins

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Animation: Hormonal Proteins Animation: Receptor Proteins

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Animation: Sensory Proteins Animation: Storage Proteins

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Animation: Structural Proteins Animation: Transport Proteins

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 Enzymes are proteins that act as catalysts to speed  Proteins are all constructed from the same set of 20
up chemical reactions amino acids
 Enzymes can perform their functions repeatedly,  Polypeptides are unbranched polymers built from
functioning as workhorses that carry out the these amino acids
processes of life  A protein is a biologically functional molecule that
consists of one or more polypeptides

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Figure 5.UN01
Amino Acid Monomers

 Amino acids are organic molecules with amino and Side chain (R group)
carboxyl groups
 Amino acids differ in their properties due to differing α carbon
side chains, called R groups

Amino Carboxyl
group group

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Figure 5.14 Figure 5.14a

Nonpolar side chains; hydrophobic
Side chain (R group)

Glycine Alanine Valine Leucine Isoleucine

Nonpolar side chains; hydrophobic
(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)
Side chain (R group)

Methionine Phenylalanine Tryptophan Proline

(Met or M) (Phe or F) (Trp or W) (Pro or P)
Polar side chains; hydrophilic
Glycine Alanine Valine Leucine Isoleucine
(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)

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)

Methionine Phenylalanine Tryptophan Proline

(Met or M) (Phe or F) (Trp or W) (Pro or P)

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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Figure 5.14b Figure 5.14c

Polar side chains; hydrophilic

Electrically charged side chains; hydrophilic

Basic (positively charged)

Acidic (negatively charged)

Serine Threonine Cysteine
(Ser or S) (Thr or T) (Cys or C)

Aspartic acid Glutamic acid Lysine Arginine Histidine

(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)

Tyrosine Asparagine Glutamine

(Tyr or Y) (Asn or N) (Gln or Q)

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Figure 5.15
Polypeptides (Amino Acid Polymers)

 Amino acids are linked by covalent bonds called

peptide bonds
 A polypeptide is a polymer of amino acids
Peptide bond
H2O
 Polypeptides range in length from a few to more
New peptide
than 1,000 monomers bond forming
Side
 Each polypeptide has a unique linear sequence of chains
(R
amino acids, with a carboxyl end (C-terminus) and groups)
an amino end (N-terminus)
Back-
bone

Peptide
Amino end bond Carboxyl end
(N-terminus) (C-terminus)
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Figure 5.15a Figure 5.15b

Side
chains
(R
groups)

Back-
bone

Peptide bond Peptide

Amino end Carboxyl end
H2O bond
(N-terminus) (C-terminus)

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Figure 5.16
Protein Structure and Function Structural Models Target molecule (on bacterial
cell surface) bound to lysozyme

 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 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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Figure 5.16a Figure 5.16b

Simplified Diagrams

Structural Models Target molecule (on bacterial

cell surface) bound to lysozyme
A transparent A solid shape is
shape shows the used when
overall shape of structural details
the molecule and are not needed.
some internal
details.

Insulin-producing cell
in pancreas

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

A simple shape is used A protein can be

here to represent a generic represented simply
enzyme. as a dot.
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Animation: Protein Structure Introduction

 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
Four Levels of Protein Structure

Antibody protein Protein from flu virus

 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 Figure 5.18aa

Primary Structure

Amino
acids

1 5 10 Primary Structure
Amino end
30 25 20 15
Amino
acids
35 40 45 50
1 5 10
Primary structure of transthyretin
55
70 65 60
Amino end
75 30 20 15
80 85 90
25

95
115 110 105 100

120 125
Carboxyl end
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Figure 5.18b Figure 5.18ba

Secondary Structure

Secondary Tertiary Quaternary α helix

Structure Structure Structure

α helix α helix Hydrogen bond

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

β pleated sheet
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Figure 5.18bb Figure 5.18bc

Tertiary Structure Quaternary Structure

α helix
Single
polypeptide
subunit
β pleated sheet

Transthyretin Transthyretin
polypeptide protein

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Figure 5.18c 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 Figure 5.18f

Heme
Iron
β subunit
Collagen

α subunit

α subunit

β subunit
Hemoglobin
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Animation: Primary Protein Structure

 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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Animation: Secondary Protein Structure

 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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Video: An Idealized α Helix Video: An Idealized α Helix: No Sidechains

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Video: An Idealized β Pleated Sheet Video: An Idealized β Pleated Sheet Cartoon

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Animation: Tertiary Protein Structure

 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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Animation: Quaternary Protein Structure

 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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Figure 5.19
Sickle-Cell Disease: A Change in Primary
Structure
Primary Secondary Quaternary Red Blood Cell
and Tertiary Function
Structure Structure Shape
 A slight change in primary structure can affect a Structures
Normal β
1 Normal Proteins do not associate
protein’s structure and ability to function 2
subunit hemoglobin with one another; each
carries oxygen.
3 β
 Sickle-cell disease, an inherited blood disorder,

Normal
4 α
5
results from a single amino acid substitution in the 6
7
protein hemoglobin β α 5 µm

 The abnormal hemoglobin molecules cause the red 1

2
Sickle-cell β
subunit
Sickle-cell
hemoglobin
Proteins aggregate into a
fiber; capacity to
carry oxygen
blood cells to aggregate into chains and to deform 3

Sickle-cell
β is reduced.
4
into a sickle shape 5 α
6
7 5 µm
β α

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Figure 5.19a Figure 5.19aa

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 5 µm
β α

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Figure 5.19b Figure 5.19ba

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 is reduced.
Sickle-cell

4
α
5
6
7 5 µm
β α

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Figure 5.20
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 Normal protein Denatured protein

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Protein Folding in the Cell

 It is hard to predict a protein’s structure from its  Scientists use X-ray crystallography to determine a
primary structure protein’s structure
 Most proteins probably go through several stages on  Another method is nuclear magnetic resonance
their way to a stable structure (NMR) spectroscopy, which does not require protein
 Diseases such as Alzheimer’s, Parkinson’s, and mad crystallization
cow disease are associated with misfolded proteins  Bioinformatics is another approach to prediction of
protein structure from amino acid sequences

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Figure 5.21 MA1

Technique Concept 5.5: Nucleic acids store, transmit, and
Diffracted
X-rays
help express hereditary information
X-ray
source  The amino acid sequence of a polypeptide is
X-ray
beam programmed by a unit of inheritance called a gene
Crystal Digital X-ray diffraction  Genes consist of DNA, a nucleic acid made of
detector pattern
monomers called nucleotides
Results

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Slide 144

MA1 Monday 6Jul2020

Mamoon Al-Rshaidat, 7/6/2020
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Figure 5.22_1
The Roles of Nucleic Acids DNA

 There are two types of nucleic acids 1 Synthesis of

mRNA
mRNA
 Deoxyribonucleic acid (DNA)
 Ribonucleic acid (RNA)
NUCLEUS
 DNA provides directions for its own replication CYTOPLASM

 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_2 Figure 5.22_3

DNA DNA

1 Synthesis of 1 Synthesis of
mRNA mRNA
mRNA mRNA

NUCLEUS NUCLEUS
CYTOPLASM CYTOPLASM

mRNA mRNA
2 Movement of 2 Movement of
mRNA into mRNA into
cytoplasm cytoplasm Ribosome

3 Synthesis of
protein

Amino
Polypeptide acids
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The Components of Nucleic Acids

 Each gene along a DNA molecule directs synthesis  Nucleic acids are polymers called polynucleotides
of a messenger RNA (mRNA)  Each polynucleotide is made of monomers called
 The mRNA molecule interacts with the cell’s protein- nucleotides
synthesizing machinery to direct production of a  Each nucleotide consists of a nitrogenous base, a
polypeptide pentose sugar, and one or more phosphate groups
 The flow of genetic information can be summarized  The portion of a nucleotide without the phosphate
as DNA → RNA → protein group is called a nucleoside

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Figure 5.23

NITROGENOUS BASES
Pyrimidines

 Nucleoside = nitrogenous base + sugar

Sugar-phosphate backbone
5′ end
 There are two families of nitrogenous bases (on blue background) Cytosine (C) Thymine
(T, in DNA)
Uracil
(U, in RNA)
5′C

 Pyrimidines (cytosine, thymine, and uracil) 3′C

Purines

have a single six-membered ring Nucleoside

Nitrogenous
 Purines (adenine and guanine) have a six-membered base
Adenine (A) Guanine (G)
ring fused to a five-membered ring 5′C

SUGARS
 In DNA, the sugar is deoxyribose; in RNA, the Phosphate 3′C
1′C

Sugar
sugar is ribose 5′C group
(pentose)
3′C
(b) Nucleotide monomer
 Nucleotide = nucleoside + phosphate group 3′ end
in a polynucleotide Deoxyribose Ribose
(in DNA) (in RNA)

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

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Figure 5.23a Figure 5.23b

Sugar-phosphate backbone NITROGENOUS BASES
5′ end (on blue background)
Pyrimidines
5′C

3′C
Nucleoside

Nitrogenous
base
Cytosine (C) Thymine Uracil
5′C (T, in DNA) (U, in RNA)

1′C Purines
Phosphate 3′C
5′C group Sugar
(pentose)
3′C
(b) Nucleotide monomer
3′ end in a polynucleotide
Adenine (A) Guanine (G)

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

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Figure 5.23c
Animation: DNA and RNA Structure

SUGARS

Deoxyribose Ribose
(in DNA) (in RNA)

(c) Nucleoside components

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Nucleotide Polymers The Structures of DNA and RNA Molecules

 Nucleotides are linked together by a phosphodiester  DNA molecules have two polynucleotides spiraling
linkage to build a polynucleotide around an imaginary axis, forming a double helix
 A phosphodiester linkage consists of a phosphate  The backbones run in opposite 5′ → 3′ directions
group that links the sugars of two nucleotides from each other, an arrangement referred to as
 These links create a backbone of sugar-phosphate antiparallel
units with nitrogenous bases as appendages  One DNA molecule includes many genes
 The sequence of bases along a DNA or mRNA
polymer is unique for each gene

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 Only certain bases in DNA pair up and form  RNA, in contrast to DNA, is single-stranded
hydrogen bonds:  Complementary pairing can also occur between
 adenine (A) always with thymine (T) two RNA molecules or between parts of the
 guanine (G) always with cytosine (C) same molecule

 This is called complementary base pairing  In RNA, thymine is replaced by uracil (U), so A
and U pair
 This feature of DNA structure makes it possible
to generate two identical copies of each DNA  While DNA always exists as a double helix, RNA
molecule in a cell preparing to divide molecules are more variable in form

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Figure 5.24
Animation: DNA Double Helix
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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Video: Stick Model of DNA (Deoxyribonucleic Video: Surface Model of DNA (Deoxyribonucleic
Acid) Acid)

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Figure 5.UN04

Chapter Summary
 Functional groups from Chapter 4
(PDF file found in E-Learning) Components Examples Functions

Monosaccharides: glucose, Fuel; carbon sources that can be

fructose converted to other molecules or
combined into polymers

 Macromolecular of Life Disaccharides: lactose, sucrose

Polysaccharides:

 Carbohydrates Monosaccharide
Cellulose (plants)
Starch (plants)
Strengthens plant cell walls
Stores glucose for energy
monomer
Glycogen (animals) Stores glucose for energy
 Lipids Chitin (animals and fungi) Strengthens exoskeletons and
fungal cell walls

 Proteins
 Nucleic Acids
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Figure 5.UN05 Figure 5.UN06

Components Examples Functions

Glycerol Triacylglycerols (fats or oils): Important energy source

glycerol + three fatty acids
Components Examples Functions
3 fatty
acids
Enzymes Catalyze chemical reactions
Defensive proteins Protect against disease
Storage proteins Store amino acids
Head Phospholipids: glycerol + Lipid bilayers of membranes
phosphate group + two fatty Hydrophobic Transport proteins Transport substances
with P
acids tails Hormones Coordinate organismal responses
2 fatty Receptor proteins Receive signals from outside cell
acids Hydrophilic
heads Amino acid monomer Motor proteins Function in cell movement
(20 types) Structural proteins Provide structural support
Steroids: four fused rings with Component of cell membranes
attached chemical groups (cholesterol)
Signaling molecules that travel
through the body (hormones)
Steroid backbone

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Figure 5.UN07

Components Examples Functions

Nitrogenous base
DNA: Stores hereditary information
Phosphate Sugar = deoxyribose
group
Nitrogenous bases = C, G, A, T
P Usually double-stranded
Sugar
RNA: Various functions in gene
Sugar = ribose expression, including carrying
Nucleotide (monomer instructions from DNA to
of a polynucleotide) Nitrogenous bases = C, G, A, U ribosomes
Usually single-stranded

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