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Biology in Focus Chapter 3
- 1. CAMPBELL BIOLOGY IN FOCUS
© 2014 Pearson Education, Inc.
Urry • Cain • Wasserman • Minorsky • Jackson • Reece
Lecture Presentations by
Kathleen Fitzpatrick and Nicole Tunbridge
3
Carbon and
the Molecular
Diversity of Life
- 2. Overview: Carbon Compounds and Life
Aside from water, living organisms consist mostly
of carbon-based compounds
Carbon is unparalleled in its ability to form large,
complex, and diverse molecules
A compound containing carbon is said to be an
organic compound
© 2014 Pearson Education, Inc.
- 3. Critically important molecules of all living things fall
into four main classes
Carbohydrates
Lipids
Proteins
Nucleic acids
The first three of these can form huge molecules
called macromolecules
© 2014 Pearson Education, Inc.
- 5. Concept 3.1: Carbon atoms can form diverse
molecules by bonding to four other atoms
An atom’s electron configuration determines the
kinds and number of bonds the atom will form with
other atoms
This is the source of carbon’s versatility
© 2014 Pearson Education, Inc.
- 6. The Formation of Bonds with Carbon
With four valence electrons, carbon can form four
covalent bonds with a variety of atoms
This ability makes large, complex molecules
possible
In molecules with multiple carbons, each carbon
bonded to four other atoms has a tetrahedral shape
However, when two carbon atoms are joined by a
double bond, the atoms joined to the carbons are in
the same plane as the carbons
© 2014 Pearson Education, Inc.
- 7. When a carbon atom forms four single covalent
bonds, the bonds angle toward the corners of an
imaginary tetrahedron
When two carbon atoms are joined by a double bond,
the atoms joined to those carbons are in the same
plane as the carbons
© 2014 Pearson Education, Inc.
- 8. © 2014 Pearson Education, Inc.
Figure 3.2
Methane
Structural
Formula
Molecular
Formula
Space-Filling
Model
Ball-and-Stick
Model
Name
Ethane
Ethene
(ethylene)
- 9. The electron configuration of carbon gives it covalent
compatibility with many different elements
The valences of carbon and its most frequent
partners (hydrogen, oxygen, and nitrogen) are the
“building code” that governs the architecture of living
molecules
© 2014 Pearson Education, Inc.
- 10. © 2014 Pearson Education, Inc.
Figure 3.3
Hydrogen
(valence = 1)
Carbon
(valence = 4)
Nitrogen
(valence = 3)
Oxygen
(valence = 2)
- 11. Carbon atoms can partner with atoms other than
hydrogen; for example:
Carbon dioxide: CO2
Urea: CO(NH2)2
© 2014 Pearson Education, Inc.
- 12. © 2014 Pearson Education, Inc.
Figure 3.UN01
Estradiol
Testosterone
- 13. Molecular Diversity Arising from Variation in
Carbon Skeletons
Carbon chains form the skeletons of most organic
molecules
Carbon chains vary in length and shape
© 2014 Pearson Education, Inc.
Animation: Carbon Skeletons
- 14. © 2014 Pearson Education, Inc.
Figure 3.4
(a) Length
(b) Branching
(c) Double bond position
(d) Presence of rings
Ethane Propane
Butane BenzeneCyclohexane
1-Butene 2-Butene
2-Methylpropane
(isobutane)
- 15. © 2014 Pearson Education, Inc.
Figure 3.4a
(a) Length
Ethane Propane
- 16. © 2014 Pearson Education, Inc.
Figure 3.4b
(b) Branching
Butane 2-Methylpropane
(isobutane)
- 17. © 2014 Pearson Education, Inc.
Figure 3.4c
(c) Double bond position
1-Butene 2-Butene
- 18. © 2014 Pearson Education, Inc.
Figure 3.4d
(d) Presence of rings
BenzeneCyclohexane
- 19. Hydrocarbons are organic molecules consisting
of only carbon and hydrogen
Many organic molecules, such as fats, have
hydrocarbon components
Hydrocarbons can undergo reactions that release
a large amount of energy
© 2014 Pearson Education, Inc.
- 20. The Chemical Groups Most Important to Life
Functional groups are the components of organic
molecules that are most commonly involved in
chemical reactions
The number and arrangement of functional groups
give each molecule its unique properties
© 2014 Pearson Education, Inc.
- 21. The seven functional groups that are most important
in the chemistry of life:
Hydroxyl group
Carbonyl group
Carboxyl group
Amino group
Sulfhydryl group
Phosphate group
Methyl group
© 2014 Pearson Education, Inc.
- 22. © 2014 Pearson Education, Inc.
Figure 3.5
Chemical Group
Hydroxyl group ( OH)
Compound Name Examples
Alcohol
Ketone
Aldehyde
Methylated
compound
Organic
phosphate
Thiol
Amine
Carboxylic acid,
or organic acid
Ethanol
Acetone Propanal
Acetic acid
Glycine
Cysteine
Glycerol
phosphate
5-Methyl cytosine
Amino group ( NH2)
Carboxyl group ( COOH)
Sulfhydryl group ( SH)
Phosphate group ( OPO3
2–
)
Methyl group ( CH3)
Carbonyl group ( C O)
- 23. © 2014 Pearson Education, Inc.
Figure 3.5a
Chemical Group
Hydroxyl group ( OH)
Compound Name Examples
Alcohol
Ketone
Aldehyde
Amine
Carboxylic acid,
or organic acid
Ethanol
Acetone Propanal
Acetic acid
Glycine
Amino group ( NH2)
Carboxyl group ( COOH)
Carbonyl group ( C O)
- 24. © 2014 Pearson Education, Inc.
Figure 3.5aa
Hydroxyl group ( OH)
Alcohol
(The specific name
usually ends in -ol.)
Ethanol, the alcohol present
in alcoholic beverages
(may be written HO )
- 25. © 2014 Pearson Education, Inc.
Figure 3.5ab
Carbonyl group ( C O)
Ketone if the carbonyl
group is within a carbon
skeleton
Acetone, the simplest ketone
Aldehyde if the carbonyl
group is at the end of a
carbon skeleton
Propanal, an aldehyde
- 26. © 2014 Pearson Education, Inc.
Figure 3.5ac
Carboxyl group ( COOH)
Acetic acid, which gives
vinegar its sour taste
Carboxylic acid, or
organic acid
Ionized form of COOH
(carboxylate ion),
found in cells
- 27. © 2014 Pearson Education, Inc.
Figure 3.5ad
Amino group ( NH2)
Glycine, an amino acid
(note its carboxyl group)
Amine
Ionized form of NH2
found in cells
- 28. © 2014 Pearson Education, Inc.
Figure 3.5b
Methylated
compound
Organic
phosphate
Thiol Cysteine
Glycerol
phosphate
5-Methyl cytosine
Sulfhydryl group ( SH)
Phosphate group ( OPO3
2–
)
Methyl group ( CH3)
Chemical Group Compound Name Examples
- 29. © 2014 Pearson Education, Inc.
Figure 3.5ba
Sulfhydryl group ( SH)
Cysteine, a sulfur-
containing amino acid
Thiol
(may be written HS )
- 30. © 2014 Pearson Education, Inc.
Figure 3.5bb
Phosphate group ( OPO3
2–
)
Organic phosphate
Glycerol phosphate, which
takes part in many important
chemical reactions in cells
- 31. © 2014 Pearson Education, Inc.
Figure 3.5bc
Methyl group ( CH3)
Methylated compound
5-Methyl cytosine, a
component of DNA that has
been modified by addition of
a methyl group
- 32. ATP: An Important Source of Energy for Cellular
Processes
One organic phosphate molecule, adenosine
triphosphate (ATP), is the primary energy-
transferring molecule in the cell
ATP consists of an organic molecule called
adenosine attached to a string of three phosphate
groups
© 2014 Pearson Education, Inc.
- 34. © 2014 Pearson Education, Inc.
Figure 3.UN03
Adenosine Adenosine
ATP Inorganic
phosphate
Energy
Reacts
with H2O
ADP
- 35. Concept 3.2: 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
Some molecules that serve as monomers also have
other functions of their own
© 2014 Pearson Education, Inc.
- 36. Cells make and break down polymers by the same
process
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
These processes are facilitated by enzymes, which
speed up chemical reactions
The Synthesis and Breakdown of Polymers
© 2014 Pearson Education, Inc.
Animation: Polymers
- 37. © 2014 Pearson Education, Inc.
Figure 3.6
Unlinked monomerShort polymer
Longer polymer
(a) Dehydration reaction: synthesizing a polymer
(b) Hydrolysis: breaking down a polymer
- 38. © 2014 Pearson Education, Inc.
Figure 3.6a
Unlinked monomerShort polymer
Longer polymer
(a) Dehydration reaction: synthesizing a polymer
Dehydration removes
a water molecule,
forming a new bond.
- 39. © 2014 Pearson Education, Inc.
Figure 3.6b
(b) Hydrolysis: breaking down a polymer
Hydrolysis adds
a water molecule,
breaking a bond.
- 40. The Diversity of Polymers
Each cell has thousands of different macromolecules
Macromolecules vary among cells of an organism,
vary more within a species, and vary even more
between species
An immense variety of polymers can be built from a
small set of monomers
HO
© 2014 Pearson Education, Inc.
- 41. Concept 3.3: 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
© 2014 Pearson Education, Inc.
- 42. Sugars
© 2014 Pearson Education, Inc.
Monosaccharides have molecular formulas that
are usually multiples of CH2O
Glucose (C6H12O6) is the most common
monosaccharide
Monosaccharides are classified by the number of
carbons in the carbon skeleton and the placement
of the carbonyl group
- 43. © 2014 Pearson Education, Inc.
Figure 3.7
Glyceraldehyde
An initial breakdown
product of glucose in cells
Ribose
A component of RNA
Triose: 3-carbon sugar (C3H6O3) Pentose: 5-carbon sugar (C5H10O5)
Hexoses: 6-carbon sugars (C6H12O6)
Energy sources for organisms
Glucose Fructose
- 44. © 2014 Pearson Education, Inc.
Figure 3.7a
Glyceraldehyde
An initial breakdown
product of glucose in cells
Triose: 3-carbon sugar (C3H6O3)
- 45. © 2014 Pearson Education, Inc.
Figure 3.7b
Ribose
A component of RNA
Pentose: 5-carbon sugar (C5H10O5)
- 46. © 2014 Pearson Education, Inc.
Figure 3.7c
Hexoses: 6-carbon sugars (C6H12O6)
Energy sources for organisms
Glucose Fructose
- 47. 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
© 2014 Pearson Education, Inc.
- 48. © 2014 Pearson Education, Inc.
Figure 3.8
(a) Linear and ring forms
(b) Abbreviated ring structure
- 49. A disaccharide is formed when a dehydration
reaction joins two monosaccharides
This covalent bond is called a glycosidic linkage
© 2014 Pearson Education, Inc.
Animation: Disaccharides
- 51. © 2014 Pearson Education, Inc.
Figure 3.9-2
1–2
glycosidic
linkage
Glucose
Sucrose
Fructose
- 52. Polysaccharides
Polysaccharides, the polymers of sugars, have
storage and structural roles
The structure and function of a polysaccharide are
determined by its sugar monomers and the positions
of glycosidic linkages
© 2014 Pearson Education, Inc.
- 53. Storage Polysaccharides
Starch, a storage polysaccharide of plants, consists
entirely of glucose monomers
Plants store surplus starch as granules
The simplest form of starch is amylose
© 2014 Pearson Education, Inc.
- 54. Glycogen is a storage polysaccharide in animals
Humans and other vertebrates store glycogen
mainly in liver and muscle cells
© 2014 Pearson Education, Inc.
Animation: Polysaccharides
- 55. © 2014 Pearson Education, Inc.
Figure 3.10
Starch granules
in a potato tuber cell
Cellulose microfibrils
in a plant cell wall
Glycogen granules
in muscle
tissue
Cellulose
molecules
Hydrogen bonds
between —OH groups
(not shown) attached to
carbons 3 and 6
Starch (amylose)
Glycogen
Cellulose
Glucose
monomer
- 56. © 2014 Pearson Education, Inc.
Figure 3.10a
Starch granules
in a potato tuber cell
Starch (amylose)
Glucose
monomer
- 57. © 2014 Pearson Education, Inc.
Figure 3.10aa
Starch granules
in a potato
tuber cell
- 58. © 2014 Pearson Education, Inc.
Figure 3.10b
Glycogen granules
in muscle
tissue
Glycogen
- 59. © 2014 Pearson Education, Inc.
Figure 3.10ba
Glycogen
granules
in muscle
tissue
- 60. © 2014 Pearson Education, Inc.
Figure 3.10c
Cellulose microfibrils
in a plant cell wall
Cellulose
molecules
Hydrogen bonds
between —OH
groups on
carbons 3 and 6
Cellulose
- 61. © 2014 Pearson Education, Inc.
Figure 3.10ca
Cellulose
microfibrils
in a plant
cell wall
- 62. Structural Polysaccharides
The polysaccharide cellulose is a major component
of the tough wall of plant cells
Like starch and glycogen, cellulose is a polymer of
glucose, but the glycosidic linkages in cellulose differ
The difference is based on two ring forms for
glucose
© 2014 Pearson Education, Inc.
- 63. © 2014 Pearson Education, Inc.
Figure 3.11
(c) Cellulose: 1–4 linkage of β glucose monomers
(b) Starch: 1–4 linkage of α glucose monomers
(a) α and β glucose
ring structures
α Glucose β Glucose
- 64. © 2014 Pearson Education, Inc.
Figure 3.11a
a) α and β glucose
ring structures
α Glucose β Glucose
- 65. In starch, the glucose monomers are arranged in
the alpha (α) conformation
Starch (and glycogen) are largely helical
In cellulose, the monomers are arranged in the beta
(β) conformation
Cellulose molecules are relatively straight
© 2014 Pearson Education, Inc.
- 66. © 2014 Pearson Education, Inc.
Figure 3.11b
(b) Starch: 1–4 linkage of α glucose monomers
- 67. © 2014 Pearson Education, Inc.
Figure 3.11c
(c) Cellulose: 1–4 linkage of β glucose monomers
- 68. In straight structures (cellulose), H atoms on one
strand can form hydrogen bonds with OH groups on
other strands
Parallel cellulose molecules held together this way
are grouped into microfibrils, which form strong
building materials for plants
© 2014 Pearson Education, Inc.
- 69. Enzymes that digest starch by hydrolyzing α linkages
can’t hydrolyze β 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
© 2014 Pearson Education, Inc.
- 70. Chitin, another structural polysaccharide, is found in
the exoskeleton of arthropods
Chitin also provides structural support for the cell
walls of many fungi
© 2014 Pearson Education, Inc.
- 71. Concept 3.4: Lipids are a diverse group of
hydrophobic molecules
Lipids do not form true 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
© 2014 Pearson Education, Inc.
- 72. 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
© 2014 Pearson Education, Inc.
Animation: Fats
- 73. © 2014 Pearson Education, Inc.
Figure 3.12
(b) Fat molecule (triacylglycerol)
Glycerol
(a) One of three dehydration reactions in the synthesis of a fat
Ester linkage
Fatty acid
(in this case, palmitic acid)
- 74. © 2014 Pearson Education, Inc.
Figure 3.12a
Glycerol
(a) One of three dehydration reactions in the synthesis of a fat
Fatty acid
(in this case, palmitic acid)
- 75. 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
© 2014 Pearson Education, Inc.
- 76. © 2014 Pearson Education, Inc.
Figure 3.12b
(b) Fat molecule (triacylglycerol)
Ester linkage
- 77. 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
© 2014 Pearson Education, Inc.
- 78. © 2014 Pearson Education, Inc.
Figure 3.13
(a) Saturated fat (b) Unsaturated fat
Structural
formula of a
saturated fat
molecule
Structural
formula
of an
unsaturated
fat moleculeSpace-filling
model of
stearic acid,
a saturated
fatty acid
Space-filling
model of oleic
acid, an
unsaturated
fatty acid Double bond
causes bending.
- 79. © 2014 Pearson Education, Inc.
Figure 3.13a
(a) Saturated fat
Structural
formula of a
saturated fat
molecule
Space-filling
model of
stearic acid,
a saturated
fatty acid
- 81. © 2014 Pearson Education, Inc.
Figure 3.13b
(b) Unsaturated fat
Structural
formula
of an
unsaturated
fat molecule
Space-filling
model of
oleic acid, an
unsaturated
fatty acid Double bond
causes bending.
- 83. 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, called
unsaturated fats or oils, are liquid at room
temperature
Plant fats and fish fats are usually unsaturated
© 2014 Pearson Education, Inc.
- 84. The major function of fats is energy storage
Fat is a compact way for animals to carry their
energy stores with them
© 2014 Pearson Education, Inc.
- 85. 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
Phospholipids are major constituents of cell
membranes
© 2014 Pearson Education, Inc.
- 86. © 2014 Pearson Education, Inc.
Figure 3.14
(a) Structural formula (b) Space-filling model
Hydrophilic
head
(d) Phospholipid
bilayer
(c) Phospholipid
symbol
Hydrophobic
tails
Choline
Phosphate
Glycerol
Fatty acids
Hydrophilichead
Hydrophobictails
- 87. © 2014 Pearson Education, Inc.
Figure 3.14ab
(a) Structural formula (b) Space-filling model
Choline
Phosphate
Glycerol
Fatty acids
Hydrophilichead
Hydrophobictails
- 88. When phospholipids are added to water, they self-
assemble into a bilayer, with the hydrophobic tails
pointing toward the interior
This feature of phospholipids results in the bilayer
arrangement found in cell membranes
© 2014 Pearson Education, Inc.
- 89. © 2014 Pearson Education, Inc.
Figure 3.14cd
Hydrophilic
head
(d) Phospholipid
bilayer
(c) Phospholipid
symbol
Hydrophobic
tails
- 90. Steroids
Steroids are lipids characterized by a carbon
skeleton consisting of four fused rings
Cholesterol, an important steroid, is a component in
animal cell membranes
Although cholesterol is essential in animals, high
levels in the blood may contribute to cardiovascular
disease
© 2014 Pearson Education, Inc.
Video: Cholesterol Stick Model
Video: Cholesterol Space Model
- 92. Concept 3.5: 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
Protein functions include defense, storage,
transport, cellular communication, movement, and
structural support
© 2014 Pearson Education, Inc.
Animation: Contractile Proteins
Animation: Defensive Proteins
Animation: Enzymes
- 93. © 2014 Pearson Education, Inc.
Animation: Gene Regulatory Proteins
Animation: Hormonal Proteins
Animation: Receptor Proteins
Animation: Sensory Proteins
Animation: Storage Proteins
Animation: Structural Proteins
Animation: Transport Proteins
- 94. © 2014 Pearson Education, Inc.
Figure 3.16
Enzymatic proteins
Storage proteins
Hormonal proteins
Contractile and motor proteins
Defensive proteins
Transport proteins
Receptor proteins
Structural proteins
Enzyme
Function: Selective acceleration of chemical reactions
Function: Storage of amino acids
Example: Digestive enzymes catalyze the hydrolysis of bonds in food
molecules.
Ovalbumin Amino acids
for embryo
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.
Example: Insulin, a hormone secreted by the pancreas, causes other
tissues to take up glucose, thus regulating blood sugar
concentration.
Function: Coordination of an organism’s activities
Normal
blood sugar
High
blood sugar
Insulin
secreted
Examples: Motor proteins are responsible for the undulations of cilia
and flagella. Actin and myosin proteins are responsible for the
contraction of muscles.
Function: Movement
Muscle tissue
Actin Myosin
30 µm Connective tissue 60 µm
Collagen
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.
Function: Support
Signaling molecules
Receptor
protein
Example: Receptors built into the membrane of a nerve cell detect
signaling molecules released by other nerve cells.
Function: Response of cell to chemical stimuli
Examples: Hemoglobin, the iron-containing protein of vertebrate
blood, transports oxygen from the lungs to other parts of the body.
Other proteins transport molecules across cell membranes.
Function: Transport of substances
Transport
protein
Cell membrane
Antibodies
BacteriumVirus
Function: Protection against disease
Example: Antibodies inactivate and help destroy viruses and bacteria.
- 95. © 2014 Pearson Education, Inc.
Figure 3.16a
Enzymatic proteins
Storage proteins
Defensive proteins
Transport proteins
Enzyme
Function: Selective acceleration of
chemical reactions
Function: Storage of amino acids
Example: Digestive enzymes catalyze the
hydrolysis of bonds in food molecules.
Ovalbumin Amino acids
for embryo
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.
Examples: Hemoglobin, the iron-containing
protein of vertebrate blood, transports
oxygen from the lungs to other parts of the
body. Other proteins transport molecules
across cell membranes.
Function: Transport of substances
Transport
protein
Cell membrane
Antibodies
BacteriumVirus
Function: Protection against disease
Example: Antibodies inactivate and help
destroy viruses and bacteria.
- 96. © 2014 Pearson Education, Inc.
Figure 3.16aa
Enzymatic proteins
Enzyme
Function: Selective acceleration of
chemical reactions
Example: Digestive enzymes catalyze the
hydrolysis of bonds in food molecules.
- 97. © 2014 Pearson Education, Inc.
Figure 3.16ab
Defensive proteins
Antibodies
BacteriumVirus
Function: Protection against disease
Example: Antibodies inactivate and help
destroy viruses and bacteria.
- 98. © 2014 Pearson Education, Inc.
Figure 3.16ac
Storage proteins
Function: Storage of amino acids
Ovalbumin Amino acids
for embryo
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.
- 100. © 2014 Pearson Education, Inc.
Figure 3.16ad
Transport proteins
Examples: Hemoglobin, the iron-containing
protein of vertebrate blood, transports
oxygen from the lungs to other parts of the
body. Other proteins transport molecules
across cell membranes.
Function: Transport of substances
Transport
protein
Cell membrane
- 101. © 2014 Pearson Education, Inc.
Figure 3.16b
Hormonal proteins
Contractile and motor proteins
Receptor proteins
Structural proteins
Example: Insulin, a hormone secreted by
the pancreas, causes other tissues to
take up glucose, thus regulating blood
sugar concentration.
Function: Coordination of an organism’s
activities
Normal
blood sugar
High
blood sugar
Insulin
secreted
Examples: Motor proteins are responsible
for the undulations of cilia and flagella.
Actin and myosin proteins are
responsible for the contraction of
muscles.
Function: Movement
Muscle tissue
Actin Myosin
30 µm Connective tissue 60 µm
Collagen
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.
Function: Support
Signaling molecules
Receptor
protein
Example: Receptors built into the
membrane of a nerve cell detect signaling
molecules released by other nerve cells.
Function: Response of cell to chemical
stimuli
- 102. © 2014 Pearson Education, Inc.
Figure 3.16ba
Hormonal proteins
Example: Insulin, a hormone secreted by
the pancreas, causes other tissues to
take up glucose, thus regulating blood
sugar concentration.
Function: Coordination of an organism’s
activities
Normal
blood sugar
High
blood sugar
Insulin
secreted
- 103. © 2014 Pearson Education, Inc.
Figure 3.16bb
Receptor proteins
Signaling molecules
Receptor
protein
Example: Receptors built into the
membrane of a nerve cell detect signaling
molecules released by other nerve cells.
Function: Response of cell to chemical
stimuli
- 104. © 2014 Pearson Education, Inc.
Figure 3.16bc
Contractile and motor proteins
Examples: Motor proteins are responsible
for the undulations of cilia and flagella.
Actin and myosin proteins are
responsible for the contraction of
muscles.
Function: Movement
Muscle tissue
Actin Myosin
30 µm
- 105. © 2014 Pearson Education, Inc.
Figure 3.16bca
Muscle tissue 30 µm
- 106. © 2014 Pearson Education, Inc.
Figure 3.16bd
Structural proteins
Connective tissue
60 µm
Collagen
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.
Function: Support
- 107. © 2014 Pearson Education, Inc.
Figure 3.16bda
Connective tissue 60 µm
- 108. Life would not be possible without enzymes
Enzymatic proteins act as catalysts, to speed up
chemical reactions without being consumed by the
reaction
© 2014 Pearson Education, Inc.
- 109. Polypeptides are unbranched polymers built from
the same set of 20 amino acids
A protein is a biologically functional molecule that
consists of one or more polypeptides
© 2014 Pearson Education, Inc.
- 110. Amino Acids
Amino acids are organic molecules with carboxyl
and amino groups
Amino acids differ in their properties due to differing
side chains, called R groups
© 2014 Pearson Education, Inc.
- 111. © 2014 Pearson Education, Inc.
Figure 3.UN04
Side chain (R group)
Carboxyl
group
Amino
group
α carbon
- 112. © 2014 Pearson Education, Inc.
Figure 3.17 Nonpolar side chains; hydrophobic
Side chain
(R group)
Glycine
(Gly or G)
Alanine
(Ala or A)
Methionine
(Met or M)
Phenylalanine
(Phe or F)
Polar side chains; hydrophilic
Leucine
(Leu or L)
Isoleucine
(Ιle or Ι)
Tryptophan
(Trp or W)
Proline
(Pro or P)
Valine
(Val or V)
Serine
(Ser or S)
Threonine
(Thr or T)
Tyrosine
(Tyr or Y)
Asparagine
(Asn or N)
Cysteine
(Cys or C)
Glutamine
(Gln or Q)
Aspartic acid
(Asp or D)
Glutamic acid
(Glu or E)
Arginine
(Arg or R)
Lysine
(Lys or K)
Histidine
(His or H)
Electrically charged side chains; hydrophilic
Acidic (negatively charged)
Basic (positively charged)
- 113. © 2014 Pearson Education, Inc.
Figure 3.17a
Nonpolar side chains; hydrophobic
Side chain
(R group)
Glycine
(Gly or G)
Alanine
(Ala or A)
Methionine
(Met or M)
Phenylalanine
(Phe or F)
Leucine
(Leu or L)
Isoleucine
(Ιle or Ι)
Tryptophan
(Trp or W)
Proline
(Pro or P)
Valine
(Val or V)
- 114. © 2014 Pearson Education, Inc.
Figure 3.17b
Polar side chains; hydrophilic
Serine
(Ser or S)
Threonine
(Thr or T)
Tyrosine
(Tyr or Y)
Asparagine
(Asn or N)
Cysteine
(Cys or C)
Glutamine
(Gln or Q)
- 115. © 2014 Pearson Education, Inc.
Figure 3.17c
Aspartic acid
(Asp or D)
Glutamic acid
(Glu or E)
Arginine
(Arg or R)
Lysine
(Lys or K)
Histidine
(His or H)
Electrically charged side chains; hydrophilic
Acidic (negatively charged)
Basic (positively charged)
- 116. Polypeptides
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, with a carboxyl end (C-terminus) and
an amino end (N-terminus)
© 2014 Pearson Education, Inc.
- 117. © 2014 Pearson Education, Inc.
Figure 3.18
New peptide
bond forming
Peptide bond
Side
chains
Back-
bone
Amino end
(N-terminus)
Carboxyl end
(C-terminus)
Peptide
bond
- 119. © 2014 Pearson Education, Inc.
Figure 3.18b
Side
chains
Back-
bone
Amino end
(N-terminus)
Carboxyl end
(C-terminus)
Peptide
bond
- 120. Protein Structure and Function
A functional protein consists of one or more
polypeptides precisely twisted, folded, and coiled
into a unique shape
© 2014 Pearson Education, Inc.
- 121. © 2014 Pearson Education, Inc.
Figure 3.19
(a) A ribbon model (b) A space-filling model
Groove
Groove
- 122. © 2014 Pearson Education, Inc.
Figure 3.19a
(a) A ribbon model
Groove
- 123. © 2014 Pearson Education, Inc.
Figure 3.19b
(b) A space-filling model
Groove
- 124. The sequence of amino acids, determined
genetically, leads to a protein’s three-dimensional
structure
A protein’s structure determines its function
© 2014 Pearson Education, Inc.
- 125. © 2014 Pearson Education, Inc.
Figure 3.20
Antibody protein Protein from flu virus
- 126. Four Levels of Protein Structure
Proteins are very diverse, but share three
superimposed levels of structure called primary,
secondary, and tertiary structure
A fourth level, quaternary structure, arises when a
protein consists of more than one polypeptide chain
© 2014 Pearson Education, Inc.
- 127. 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 from interactions
between multiple polypeptide chains
© 2014 Pearson Education, Inc.
- 128. © 2014 Pearson Education, Inc.
Video: Alpha Helix with No Side Chain
Video: Alpha Helix with Side Chain
Video: Beta Pleated Sheet
Video: Beta Pleated Stick
Animation: Introduction to Protein Structure
Animation: Primary Structure
Animation: Secondary Structure
Animation: Tertiary Structure
Animation: Quaternary Structure
- 129. © 2014 Pearson Education, Inc.
Figure 3.21a
Primary structure
Amino end
Carboxyl end
Primary structure of transthyretin
125
95
90
100105110
120
115
80
70 60
85
75
65
55
504540
2530
35
20 15
1051
Amino
acids
- 130. © 2014 Pearson Education, Inc.
Figure 3.21aa
Primary structure
Amino end
2530 20 15
1051
Amino
acids
- 131. © 2014 Pearson Education, Inc.
Figure 3.21b
Secondary
structure
Tertiary
structure
Quaternary
structure
Transthyretin
polypeptide
Transthyretin
protein
β pleated sheet
α helix
- 132. © 2014 Pearson Education, Inc.
Figure 3.21ba
Secondary structure
Hydrogen
bond
β pleated sheet
α helix
Hydrogen bond
β strand
- 133. © 2014 Pearson Education, Inc.
Figure 3.21bb
Tertiary structure
Transthyretin
polypeptide
- 134. © 2014 Pearson Education, Inc.
Figure 3.21bc
Quaternary structure
Transthyretin
protein
- 136. © 2014 Pearson Education, Inc.
Figure 3.21d
Hydrogen
bond
Disulfide
bridge
Polypeptide
backbone
Hydrophobic
interactions and
van der Waals
interactions
Ionic bond
- 138. © 2014 Pearson Education, Inc.
Figure 3.21f
Heme
Iron
α subunit
α subunit
β subunit
β subunit
Hemoglobin
- 139. Sickle-Cell Disease: A Change in Primary Structure
Primary structure is the sequence of amino acids
on the polypeptide chain
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
© 2014 Pearson Education, Inc.
- 140. © 2014 Pearson Education, Inc.
Figure 3.22
β subunit
β subunit
Function
Red Blood Cell
Shape
Quaternary
Structure
Secondary
and Tertiary
Structures
Primary
Structure
Normal
hemoglobin
Sickle-cell
hemoglobin
Exposed hydro-
phobic region
Molecules crystallized
into a fiber; capacity to
carry oxygen is reduced.
Molecules do not
associate with one
another; each carries
oxygen.
β
β
β
β
α
α
α
α
1
2
3
4
5
6
7
1
2
3
4
5
6
7
NormalSickle-cell
5 µm
5 µm
- 141. © 2014 Pearson Education, Inc.
Figure 3.22a
β subunit
FunctionQuaternary
Structure
Secondary
and Tertiary
Structures
Primary
Structure
Normal
hemoglobin
Molecules do not
associate with one
another; each carries
oxygen.
β
β
α
α
1
2
3
4
5
6
7
Normal
- 143. © 2014 Pearson Education, Inc.
Figure 3.22b
β subunit
Function
Quaternary
Structure
Secondary
and Tertiary
Structures
Primary
Structure
Sickle-cell
hemoglobin
Exposed hydro-
phobic region
Molecules crystallized
into a fiber; capacity to
carry oxygen is reduced.
β
β
α
α
1
2
3
4
5
6
7
Sickle-cell
- 145. 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
© 2014 Pearson Education, Inc.
- 147. © 2014 Pearson Education, Inc.
Figure 3.23-2
Normal protein Denatured protein
- 148. © 2014 Pearson Education, Inc.
Figure 3.23-3
Denatured proteinNormal protein
- 149. Protein Folding in the Cell
It is hard to predict a protein’s structure from its
primary structure
Most proteins probably go through several
intermediate structures on their way to their final,
stable shape
Scientists use X-ray crystallography to determine
3-D protein structure based on diffractions of an
X-ray beam by atoms of the crystalized molecule
© 2014 Pearson Education, Inc.
- 150. © 2014 Pearson Education, Inc.
Figure 3.24
Digital detectorCrystal
Experiment
Results
X-ray
source X-ray
beam
X-ray diffraction
pattern
Diffracted
X-rays
DNARNA
RNA
polymerase ΙΙ
- 151. © 2014 Pearson Education, Inc.
Figure 3.24a
Digital detectorCrystal
Experiment
X-ray
source X-ray
beam
X-ray diffraction
pattern
Diffracted
X-rays
- 152. © 2014 Pearson Education, Inc.
Figure 3.24b
Results
DNARNA
RNA
polymerase ΙΙ
- 153. Concept 3.6: 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 are made of DNA, a nucleic acid made of
monomers called nucleotides
© 2014 Pearson Education, Inc.
- 154. 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
© 2014 Pearson Education, Inc.
- 155. © 2014 Pearson Education, Inc.
Figure 3.25-1
CYTOPLASM
NUCLEUS
Synthesis
of mRNA
mRNA
DNA
1
- 156. © 2014 Pearson Education, Inc.
Figure 3.25-2
CYTOPLASM
mRNA
Movement of
mRNA into
cytoplasm
NUCLEUS
Synthesis
of mRNA
mRNA
DNA
2
1
- 157. © 2014 Pearson Education, Inc.
Figure 3.25-3
CYTOPLASM
Ribosome
Amino
acids
mRNA
Polypeptide
Synthesis
of protein
Movement of
mRNA into
cytoplasm
NUCLEUS
Synthesis
of mRNA
mRNA
DNA
3
2
1
- 158. 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
© 2014 Pearson Education, Inc.
Animation: DNA and RNA Structure
- 159. © 2014 Pearson Education, Inc.
Figure 3.26
Sugar-phosphate backbone
(on blue background)
(a) Polynucleotide, or nucleic acid
(b) Nucleotide
(c) Nucleoside components
5′ end
3′ end
5′C
5′C
3′C
3′C
Phosphate
group Sugar
(pentose)
Nitrogenous
base
Nucleoside
Nitrogenous bases
Pyrimidines
Cytosine (C) Thymine
(T, in DNA)
Uracil
(U, in RNA)
Purines
Adenine (A) Guanine (G)
Sugars
Deoxyribose (in DNA) Ribose (in RNA)
- 160. © 2014 Pearson Education, Inc.
Figure 3.26a
Sugar-phosphate backbone
(on blue background)
(a) Polynucleotide, or nucleic acid
(b) Nucleotide
5′ end
3′ end
5′C
5′C
3′C
3′C
Phosphate
group Sugar
(pentose)
Nitrogenous
base
Nucleoside
- 161. © 2014 Pearson Education, Inc.
Figure 3.26b
(b) Nucleotide
Phosphate
group Sugar
(pentose)
Nitrogenous
base
Nucleoside
- 162. © 2014 Pearson Education, Inc.
Figure 3.26c
Nitrogenous bases
Pyrimidines
Cytosine (C) Thymine
(T, in DNA)
Uracil
(U, in RNA)
Purines
Adenine (A) Guanine (G)
- 163. © 2014 Pearson Education, Inc.
Figure 3.26d
Sugars
Deoxyribose (in DNA) Ribose (in RNA)
- 164. Each nitrogenous base has one or two rings that
include nitrogen atoms
The nitrogenous bases in nucleic acids are called
cytosine (C), thymine (T), uracil (U), adenine (A),
and guanine (G)
Thymine is found only in DNA, and uracil only in
RNA; the rest are found in both DNA and RNA
© 2014 Pearson Education, Inc.
- 165. The sugar in DNA is deoxyribose; in RNA it is
ribose
A prime (′) is used to identify the carbon atoms in the
ribose, such as the 2′ carbon or 5′ carbon
A nucleoside with at least one phosphate attached is
a nucleotide
© 2014 Pearson Education, Inc.
- 166. Nucleotide Polymers
Adjacent nucleotides are joined by covalent bonds
that form between the —OH group on the 3′ carbon
of one nucleotide and the phosphate on the 5′
carbon of the next
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
© 2014 Pearson Education, Inc.
- 167. The Structures of DNA and RNA Molecules
RNA molecules usually exist as single polypeptide
chains
DNA molecules have 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
© 2014 Pearson Education, Inc.
- 168. The nitrogenous 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
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
© 2014 Pearson Education, Inc.
- 169. © 2014 Pearson Education, Inc.
Animation: DNA Double Helix
Video: DNA Stick Model
Video: DNA Surface Model
- 170. © 2014 Pearson Education, Inc.
Figure 3.27
(a) DNA
Sugar-phosphate
backbones
5′
5′
3′
3′
(b) Transfer RNA
Base pair joined
by hydrogen bonding
Hydrogen bonds
Base pair joined
by hydrogen
bonding
- 171. © 2014 Pearson Education, Inc.
Figure 3.27a
(a) DNA
Sugar-phosphate
backbones
5′
5′
3′
3′ Base pair joined
by hydrogen bonding
Hydrogen bonds
- 172. © 2014 Pearson Education, Inc.
Figure 3.27b
Sugar-phosphate
backbones
(b) Transfer RNA
Hydrogen bonds
Base pair joined
by hydrogen
bonding
- 173. 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
© 2014 Pearson Education, Inc.
Hinweis der Redaktion
- Figure 3.1 Why do scientists study the structures of macromolecules?
- Figure 3.2 The shapes of three simple organic molecules
- Figure 3.3 Valences of the major elements of organic molecules
- Figure 3.UN01 In-text figure, sex hormones, p.44 (upper left)
- Figure 3.4 Four ways that carbon skeletons can vary
- Figure 3.4a Four ways that carbon skeletons can vary (part 1: length)
- Figure 3.4b Four ways that carbon skeletons can vary (part 2: branching)
- Figure 3.4c Four ways that carbon skeletons can vary (part 3: double bond position)
- Figure 3.4d Four ways that carbon skeletons can vary (part 4: presence of rings)
- Figure 3.5 Some biologically important chemical groups
- Figure 3.5a Some biologically important chemical groups (part 1)
- Figure 3.5aa Some biologically important chemical groups (part 2: hydroxyl)
- Figure 3.5ab Some biologically important chemical groups (part 3: carbonyl)
- Figure 3.5ac Some biologically important chemical groups (part 4: carboxyl)
- Figure 3.5ad Some biologically important chemical groups (part 5: amino)
- Figure 3.5b Some biologically important chemical groups (part 6)
- Figure 3.5ba Some biologically important chemical groups (part 7: sulfhydryl)
- Figure 3.5bb Some biologically important chemical groups (part 8: phosphate)
- Figure 3.5bc Some biologically important chemical groups (part 9: methyl)
- Figure 3.UN02 In-text figure, ATP phosphate chain, p.44 (lower left)
- Figure 3.UN03 In-text figure, ATP to ADP reaction, p.44 (upper right)
- Figure 3.6 The synthesis and breakdown of polymers
- Figure 3.6a The synthesis and breakdown of polymers (part 1: dehydration)
- Figure 3.6b The synthesis and breakdown of polymers (part 2: hydrolysis)
- Figure 3.7 Examples of monosaccharides
- Figure 3.7a Examples of monosaccharides (part 1: a triose)
- Figure 3.7b Examples of monosaccharides (part 2: a pentose)
- Figure 3.7c Examples of monosaccharides (part 3: two hexoses)
- Figure 3.8 Linear and ring forms of glucose
- Figure 3.9-1 Disaccharide synthesis (step 1)
- Figure 3.9-2 Disaccharide synthesis (step 2)
- Figure 3.10 Polysaccharides of plants and animals
- Figure 3.10a Polysaccharides of plants and animals (part 1: starch)
- Figure 3.10aa Polysaccharides of plants and animals (part 2: starch, micrograph)
- Figure 3.10b Polysaccharides of plants and animals (part 3: glycogen)
- Figure 3.10ba Polysaccharides of plants and animals (part 4: glycogen, micrograph)
- Figure 3.10c Polysaccharides of plants and animals (part 5: cellulose)
- Figure 3.10ca Polysaccharides of plants and animals (part 6: cellulose, micrograph)
- Figure 3.11 Monomer structures of starch and cellulose
- Figure 3.11a Monomer structures of starch and cellulose (part 1: ring structures)
- Figure 3.11b Monomer structures of starch and cellulose (part 2: starch linkage)
- Figure 3.11c Monomer structures of starch and cellulose (part 3: cellulose linkage)
- Figure 3.12 The synthesis and structure of a fat, or triacylglycerol
- Figure 3.12a The synthesis and structure of a fat, or triacylglycerol (part 1: dehydration reaction)
- Figure 3.12b The synthesis and structure of a fat, or triacylglycerol (part 2: a triacylglycerol molecule)
- Figure 3.13 Saturated and unsaturated fats and fatty acids
- Figure 3.13a Saturated and unsaturated fats and fatty acids (part 1: saturated fat)
- Figure 3.13aa Saturated and unsaturated fats and fatty acids (part 2: butter)
- Figure 3.13b Saturated and unsaturated fats and fatty acids (part 3: unsaturated fat)
- Figure 3.13ba Saturated and unsaturated fats and fatty acids (part 4: olive oil)
- Figure 3.14 The structure of a phospholipid
- Figure 3.14ab The structure of a phospholipid (part 1: formula and space-filling model)
- Figure 3.14cd The structure of a phospholipid (part 2: the phospholipid bilayer)
- Figure 3.15 Cholesterol, a steroid
- Figure 3.16 An overview of protein functions
- Figure 3.16a An overview of protein functions (part 1)
- Figure 3.16aa An overview of protein functions (part 2: enzymatic)
- Figure 3.16ab An overview of protein functions (part 3: defensive)
- Figure 3.16ac An overview of protein functions (part 4: storage)
- Figure 3.16aca An overview of protein functions (part 5: storage, photo)
- Figure 3.16ad An overview of protein functions (part 6: transport)
- Figure 3.16b An overview of protein functions (part 7)
- Figure 3.16ba An overview of protein functions (part 8: hormonal)
- Figure 3.16bb An overview of protein functions (part 9: receptors)
- Figure 3.16bc An overview of protein functions (part 10: contractile and motor proteins)
- Figure 3.16bca An overview of protein functions (part 11: contractile and motor proteins, micrograph)
- Figure 3.16bd An overview of protein functions (part 12: structural)
- Figure 3.16bda An overview of protein functions (part 13: structural, micrograph)
- Figure 3.UN04 In-text figure, amino acid structure, p.52
- Figure 3.17 The 20 amino acids of proteins
- Figure 3.17a The 20 amino acids of proteins (part 1: nonpolar)
- Figure 3.17b The 20 amino acids of proteins (part 2: polar)
- Figure 3.17c The 20 amino acids of proteins (part 3: charged)
- Figure 3.18 Making a polypeptide chain
- Figure 3.18a Making a polypeptide chain (part 1: dehydration reaction)
- Figure 3.18b Making a polypeptide chain (part 2: new peptide bond)
- Figure 3.19 Structure of a protein, the enzyme lysozyme
- Figure 3.19a Structure of a protein, the enzyme lysozyme (part 1: ribbon model)
- Figure 3.19b Structure of a protein, the enzyme lysozyme (part 2: space-filling model)
- Figure 3.20 An antibody binding to a protein from a flu virus
- Figure 3.21a Exploring levels of protein structure (part 1: primary)
- Figure 3.21aa Exploring levels of protein structure (part 2: primary, detail)
- Figure 3.21b Exploring levels of protein structure (part 3: secondary through quaternary)
- Figure 3.21ba Exploring levels of protein structure (part 4: secondary)
- Figure 3.21bb Exploring levels of protein structure (part 5: tertiary)
- Figure 3.21bc Exploring levels of protein structure (part 6: quaternary)
- Figure 3.21c Exploring levels of protein structure (part 7: spider silk, photo)
- Figure 3.21d Exploring levels of protein structure (part 8: tertiary stabilization)
- Figure 3.21e Exploring levels of protein structure (part 9: collagen)
- Figure 3.21f Exploring levels of protein structure (part 10: hemoglobin)
- Figure 3.22 A single amino acid substitution in a protein causes sickle-cell disease.
- Figure 3.22a A single amino acid substitution in a protein causes sickle-cell disease. (part 1: normal hemoglobin)
- Figure 3.22aa A single amino acid substitution in a protein causes sickle-cell disease. (part 2: normal red blood cell, micrograph)
- Figure 3.22b A single amino acid substitution in a protein causes sickle-cell disease. (part 3: sickle-cell hemoglobin)
- Figure 3.22ba A single amino acid substitution in a protein causes sickle-cell disease. (part 4: sickled red blood cell, micrograph)
- Figure 3.23-1 Denaturation and renaturation of a protein (step 1)
- Figure 3.23-2 Denaturation and renaturation of a protein (step 2)
- Figure 3.23-3 Denaturation and renaturation of a protein (step 3)
- Figure 3.24 Inquiry: What can the 3-D shape of the enzyme RNA polymerase II tell us about its function?
- Figure 3.24a Inquiry: What can the 3-D shape of the enzyme RNA polymerase II tell us about its function? (part 1: experiment)
- Figure 3.24b Inquiry: What can the 3-D shape of the enzyme RNA polymerase II tell us about its function? (part 2: results)
- Figure 3.25-1 DNA RNA protein (step 1)
- Figure 3.25-2 DNA RNA protein (step 2)
- Figure 3.25-3 DNA RNA protein (step 3)
- Figure 3.26 Components of nucleic acids
- Figure 3.26a Components of nucleic acids (part 1: a nucleic acid)
- Figure 3.26b Components of nucleic acids (part 2: a nucleotide)
- Figure 3.26c Components of nucleic acids (part 3: nucleoside bases)
- Figure 3.26d Components of nucleic acids (part 4: nucleoside sugars)
- Figure 3.27 The structures of DNA and tRNA molecules
- Figure 3.27a The structures of DNA and tRNA molecules (part 1: DNA)
- Figure 3.27b The structures of DNA and tRNA molecules (part 2: tRNA)
- Figure 3.UN05 Scientific skills: analyzing polypeptide sequence data
- Figure 3.UN06 Summary of key concepts: large biological molecules
- Figure 3.UN06a Summary of key concepts: large biological molecules (part 1: carbohydrates and lipids)
- Figure 3.UN06b Summary of key concepts: large biological molecules (part 2: proteins and nucleic acids)
- Figure 3.UN07 Test your understanding, question 1