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LECTURE PRESENTATIONS

For CAMPBELL BIOLOGY, NINTH EDITION


Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson

Chapter 5

The Structure and Function of


Large Biological Molecules

Lectures by
Erin Barley
Kathleen Fitzpatrick
2011 Pearson Education, Inc.

Figure 5.1

Concept 5.1: Macromolecules are


polymers, built from monomers
polymer
monomers
Three of the four classes of lifes organic
molecules are polymers
Carbohydrates
Proteins
Nucleic acids

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The Synthesis and Breakdown of Polymers


dehydration reaction
hydrolysis

Animation: Polymers
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Figure 5.2a

(a) Dehydration reaction: synthesizing a polymer


1

Unlinked monomer

Short polymer
Dehydration removes
a water molecule,
forming a new bond.

Longer polymer

Figure 5.2b

(b) Hydrolysis: breaking down a polymer


1

Hydrolysis adds
a water molecule,
breaking a bond.

Concept 5.2: Carbohydrates serve as fuel


and building material
Carbohydrates
Monosaccharides - or single
sugars
Polysaccharides - polymers
composed of many sugar building
blocks

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Sugars
Monosaccharides 1:2:1 ratio CHO
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 (Aldehyde Sugars)

Ketoses (Ketone Sugars)

Trioses: 3-carbon sugars (C3H6O3)

Glyceraldehyde

Dihydroxyacetone

Pentoses: 5-carbon sugars (C5H10O5)

Ribose

Ribulose

Hexoses: 6-carbon sugars (C6H12O6)

Glucose

Galactose

Fructose

Figure 5.3c

Aldose (Aldehyde Sugar)

Ketose (Ketone Sugar)

Hexoses: 6-carbon sugars (C6H12O6)

Glucose

Galactose

Fructose

Figure 5.4

1
2

3
4

4
5

1
3

(a) Linear and ring forms

6
5
4

1
3

(b) Abbreviated ring structure

1
3

Figure 5.5

14
glycosidic
1 linkage 4

Glucose

Glucose

Maltose

(a) Dehydration reaction in the synthesis of maltose

12
glycosidic
1 linkage 2

Glucose

Fructose

(b) Dehydration reaction in the synthesis of sucrose

Sucrose

Polysaccharides

Polysaccharides
storage
structural roles

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Storage Polysaccharides

Starch - glucose monomers


stores surplus starch as granules
within chloroplasts and other
plastids
simplest form of starch is amylose

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Figure 5.6

Chloroplast

Starch granules
Amylopectin

Amylose
(a) Starch:
1 m
a plant polysaccharide
Mitochondria

Glycogen granules

Glycogen
(b) Glycogen:
0.5 m
an animal polysaccharide

Figure 5.6a

Chloroplast

Starch granules

1 m

Glycogen is a storage polysaccharide in


animals
Humans and other vertebrates store
glycogen mainly in liver and muscle cells

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Figure 5.6b

Mitochondria

Glycogen granules

0.5 m

Structural Polysaccharides
cellulose is a major component of the tough
wall of plant cells
polymer of glucose with different glycosidic
linkages differ
The difference is based on two ring forms for
glucose: alpha () and beta ()

Animation: Polysaccharides
2011 Pearson Education, Inc.

Figure 5.7

(a) and glucose


ring structures
4

Glucose

Glucose

1 4

(b) Starch: 14 linkage of glucose monomers

1 4

(c) Cellulose: 14 linkage of glucose monomers

Figure 5.8

Cellulose
microfibrils in a
plant cell wall

Cell wall

Microfibril

10 m
0.5 m

Cellulose
molecules

Glucose
monomer

Enzymes that digest starch by hydrolyzing


linkages cant hydrolyze linkages in cellulose
Cellulose in human food passes through the
digestive tract as insoluble fiber
Some microbes use enzymes to digest
cellulose
Many herbivores, from cows to termites, have
symbiotic relationships with these microbes

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Figure 5.9

The structure
of the chitin
monomer

Chitin forms the exoskeleton


of arthropods.

Chitin is used to make a strong and flexible


surgical thread that decomposes after the
wound or incision heals.

Concept 5.3: Lipids are a diverse group of


hydrophobic molecules
do not form polymers
hydrophobic becausethey consist mostly of
hydrocarbons, which form nonpolar covalent
bonds
important lipids are fats, phospholipids, and
steroids

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Figure 5.10

Fatty acid
(in this case, palmitic acid)

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

(b) Fat molecule (triacylglycerol)

Figure 5.11

(a) Saturated fat

Structural
formula of a
saturated fat
molecule

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

(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.

Hydrogenation
trans fats
Energy storage
Omega-3
Adipose tissue

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Hydrophobic tails

Hydrophilic head

Figure 5.12

Choline

Phosphate
Glycerol

Fatty acids
Hydrophilic
head
Hydrophobic
tails

(a) Structural formula

(b) Space-filling model

(c) Phospholipid symbol

Hydrophobic tails

Hydrophilic head

Figure 5.12a

(a) Structural formula

Choline
Phosphate
Glycerol

Fatty acids

(b) Space-filling model

Figure 5.13

Hydrophilic
head

Hydrophobic
tail

WATER

WATER

Figure 5.14

Concept 5.4:
Proteins
50% of the dry mass of most cells
functions
a. structural support
b. Storage
c. Transport
d. cellular communications
e. Movement
f. defense against foreign substances

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Figure 5.15a

Enzymatic proteins
Function: Selective acceleration of chemical reactions
Example: Digestive enzymes catalyze the hydrolysis
of bonds in food molecules.

Enzyme

Figure 5.15b

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

Figure 5.15c

Hormonal proteins
Function: Coordination of an organisms activities
Example: Insulin, a hormone secreted by the
pancreas, causes other tissues to take up glucose,
thus regulating blood sugar concentration

High
blood sugar

Insulin
secreted

Normal
blood sugar

Figure 5.15d

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

Muscle tissue

100 m

Myosin

Figure 5.15e

Defensive proteins
Function: Protection against disease
Example: Antibodies inactivate and help destroy
viruses and bacteria.

Antibodies
Virus

Bacterium

Figure 5.15f

Transport proteins
Function: Transport of substances
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.

Transport
protein

Cell membrane

Figure 5.15g

Receptor proteins
Function: Response of cell to chemical stimuli

Example: Receptors built into the membrane of a


nerve cell detect signaling molecules released by
other nerve cells.

Signaling
molecules

Receptor
protein

Figure 5.15h

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.

Collagen

Connective
tissue

60 m

Amino Acid Monomers

carboxyl and amino groups


differ in their properties due to
differing side chains, called R
groups

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Figure 5.UN01

Side chain (R group)


carbon

Amino
group

Carboxyl
group

Figure 5.16
Nonpolar side chains; hydrophobic
Side chain
(R group)

Glycine
(Gly or G)

Alanine
(Ala or A)

Methionine
(Met or M)

Isoleucine
(Ile or I)

Leucine
(Leu or L)

Valine
(Val or V)

Phenylalanine
(Phe or F)

Tryptophan
(Trp or W)

Proline
(Pro or P)

Polar side chains; hydrophilic

Serine
(Ser or S)

Threonine
(Thr or T)

Cysteine
(Cys or C)

Electrically charged side chains; hydrophilic

Tyrosine
(Tyr or Y)

Asparagine
(Asn or N)

Glutamine
(Gln or Q)

Basic (positively charged)

Acidic (negatively charged)

Aspartic acid
(Asp or D)

Glutamic acid
(Glu or E)

Lysine
(Lys or K)

Arginine
(Arg or R)

Histidine
(His or H)

Figure 5.17

Peptide bond

New peptide
bond forming
Side
chains

Backbone

Amino end
(N-terminus)

Peptide
bond

Carboxyl end
(C-terminus)

Figure 5.18

Groove
Groove

(a) A ribbon model

(b) A space-filling model

Figure 5.19

Antibody protein

Protein from flu virus

Four Levels of Protein Structure

primary structure
Secondary structure
Tertiary
Quaternary

Animation: Protein Structure Introduction


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Figure 5.20a

Primary structure
Amino
acids

Amino end

Primary structure of transthyretin

Carboxyl end

Figure 5.20b

Tertiary
structure

Secondary
structure

Quaternary
structure

helix
Hydrogen bond
pleated sheet
strand
Hydrogen
bond

Transthyretin
polypeptide

Transthyretin
protein

Figure 5.20c

Secondary structure

helix

pleated sheet

Hydrogen bond
strand, shown as a flat
arrow pointing toward
the carboxyl end

Hydrogen bond

Figure 5.20d

Tertiary structure is determined by


interactions between R groups
hydrogen bonds
ionic bonds
hydrophobic interactions
van der Waals interactions
disulfide bridges may reinforce the proteins
structure

Animation: Tertiary Protein Structure


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Figure 5.20f

Hydrogen
bond

Hydrophobic
interactions and
van der Waals
interactions

Disulfide
bridge
Ionic bond

Polypeptide
backbone

Figure 5.20g

Quaternary structure

Transthyretin
protein
(four identical
polypeptides)

Figure 5.20h

Collagen

Figure 5.20i

Heme
Iron
subunit

subunit

subunit

subunit

Hemoglobin

Figure 5.20j

Sickle-Cell Disease: A Change in Primary


Structure
A slight change in primary structure can affect
a proteins structure and ability to function
Sickle-cell disease, an inherited blood
disorder, results from a single amino
acid(valine) substitution (for glutamic acid) in
the protein hemoglobin

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Figure 5.21

Sickle-cell hemoglobin

Normal hemoglobin

Primary
Structure
1
2
3
4
5
6
7

Secondary
and Tertiary
Structures

Quaternary
Structure

Function
Molecules do not
associate with one
another; each carries
oxygen.

Normal
hemoglobin

subunit

Red Blood
Cell Shape

10 m

1
2
3
4
5
6
7

Exposed
hydrophobic
region

Sickle-cell
hemoglobin

subunit

Molecules crystallize
into a fiber; capacity
to carry oxygen is
reduced.

10 m

Figure 5.21a

10 m

Figure 5.21b

10 m

What Determines Protein Structure?


This loss of a proteins native structure is
called denaturation
A denatured protein is biologically inactive

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Figure 5.22

aturat ion
n
e
D

Normal protein

Re
na

t ura t i on

Denatured protein

Figure 5.23b

Polypeptide

Correctly
folded
protein

Steps of Chaperonin 2 The cap attaches, causing 3 The cap comes


Action:
off, and the
the cylinder to change
1 An unfolded polyproperly folded
shape in such a way that
peptide enters the
protein is
it creates a hydrophilic
cylinder from
released.
environment for the
one end.
folding of the polypeptide.

Techniques to determine protein structure


X-ray crystallography
nuclear magnetic resonance (NMR)
spectroscopy
Bioinformatics uses computer programs to
predict protein structure from amino acid
sequences

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Figure 5.24

EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
Crystal

Digital detector

X-ray diffraction
pattern

RESULTS
RNA

DNA

RNA
polymerase II

Figure 5.25-1

DNA

1 Synthesis of
mRNA

mRNA

NUCLEUS
CYTOPLASM

Figure 5.25-2

DNA

1 Synthesis of
mRNA

mRNA

NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into
cytoplasm

Figure 5.25-3

DNA

1 Synthesis of
mRNA

mRNA

NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into
cytoplasm

Ribosome

3 Synthesis
of protein

Polypeptide

Amino
acids

Figure 5.26
5 end

Sugar-phosphate backbone

Nitrogenous bases
Pyrimidines

5C
3C
Nucleoside
Nitrogenous
base

Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA)


Purines

5C
1C
5C
3C

Phosphate
group

3C

Sugar
(pentose)
Guanine (G)

Adenine (A)
(b) Nucleotide

3 end

Sugars

(a) Polynucleotide, or nucleic acid

Deoxyribose (in DNA)


(c) Nucleoside components

Ribose (in RNA)

Figure 5.27

Sugar-phosphate
backbones
Hydrogen bonds

Base pair joined


by hydrogen
bonding

(a) DNA

Base pair joined


by hydrogen bonding
(b) Transfer RNA

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

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The Theme of Emergent Properties in the


Chemistry of Life: A Review
Higher levels of organization result in the
emergence of new properties
Organization is the key to the chemistry of life

2011 Pearson Education, Inc.

Figure 5.UN02

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Figure 5.UN02b

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