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LECTURE PRESENTATIONSFor CAMPBELL BIOLOGY, NINTH EDITION
Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
© 2011 Pearson Education, Inc.
Lectures byErin Barley
Kathleen Fitzpatrick
The Structure and Function of Large Biological Molecules
Chapter 5
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Overview: The Molecules of Life
• All living things are made up of four classes of large biological molecules: carbohydrates, lipids, proteins, and nucleic acids
• Macromolecules are large molecules composed of thousands of covalently connected atoms
• Molecular structure and function are inseparable
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Figure 5.1
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Concept 5.1: Macromolecules are polymers, built from monomers
• A polymer is a long molecule consisting of many similar building blocks
• These small building-block molecules are called monomers
• Three of the four classes of life’s organic molecules are polymers
– Carbohydrates– Proteins– Nucleic acids
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• 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
The Synthesis and Breakdown of Polymers
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Animation: Polymers
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Figure 5.2(a) Dehydration reaction: synthesizing a polymer
Short polymer Unlinked monomer
Dehydration removesa water molecule,forming a new bond.
Longer polymer
(b) Hydrolysis: breaking down a polymer
Hydrolysis addsa water molecule,breaking a bond.
1
1
1
2 3
2 3 4
2 3 4
1 2 3
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Figure 5.2a
(a) Dehydration reaction: synthesizing a polymer
Short polymer Unlinked monomer
Dehydration removesa water molecule,forming a new bond.
Longer polymer
1 2 3 4
1 2 3
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Figure 5.2b
(b) Hydrolysis: breaking down a polymer
Hydrolysis addsa water molecule,breaking a bond.
1 2 3 4
1 2 3
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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
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Concept 5.2: Carbohydrates serve as fuel and building material
• Carbohydrates include sugars and the polymers of sugars
• The simplest carbohydrates are monosaccharides, or single sugars
• Carbohydrate macromolecules are polysaccharides, polymers composed of many sugar building blocks
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Sugars
• Monosaccharides have molecular formulas that are usually multiples of CH2O
• Glucose (C6H12O6) is the most common monosaccharide
• Monosaccharides are classified by – The location of the carbonyl group (as aldose
or ketose)
– The number of carbons in the carbon skeleton
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Figure 5.3Aldoses (Aldehyde Sugars) Ketoses (Ketone Sugars)
Glyceraldehyde
Trioses: 3-carbon sugars (C3H6O3)
Dihydroxyacetone
Pentoses: 5-carbon sugars (C5H10O5)
Hexoses: 6-carbon sugars (C6H12O6)
Ribose Ribulose
Glucose Galactose Fructose
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Figure 5.3a
Aldose (Aldehyde Sugar) Ketose (Ketone Sugar)
Glyceraldehyde
Trioses: 3-carbon sugars (C3H6O3)
Dihydroxyacetone
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Figure 5.3b
Pentoses: 5-carbon sugars (C5H10O5)
Ribose Ribulose
Aldose (Aldehyde Sugar) Ketose (Ketone Sugar)
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Figure 5.3c
Aldose (Aldehyde Sugar) Ketose (Ketone Sugar)
Hexoses: 6-carbon sugars (C6H12O6)
Glucose Galactose Fructose
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• Though often drawn as linear skeletons, in aqueous solutions many sugars form rings
• Monosaccharides serve as a major fuel for cells and as raw material for building molecules
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Figure 5.4
(a) Linear and ring forms
(b) Abbreviated ring structure
1
2
3
4
5
6
6
5
4
32
1 1
23
4
5
6
1
23
4
5
6
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• A disaccharide is formed when a dehydration reaction joins two monosaccharides
• This covalent bond is called a glycosidic linkage
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Animation: Disaccharide
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Figure 5.5
(a) Dehydration reaction in the synthesis of maltose
(b) Dehydration reaction in the synthesis of sucrose
Glucose Glucose
Glucose
Maltose
Fructose Sucrose
1–4glycosidic
linkage
1–2glycosidic
linkage
1 4
1 2
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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
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Storage Polysaccharides
• Starch, a storage polysaccharide of plants, consists entirely of glucose monomers
• Plants store surplus starch as granules within chloroplasts and other plastids
• The simplest form of starch is amylose
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Figure 5.6
(a) Starch: a plant polysaccharide
(b) Glycogen: an animal polysaccharide
Chloroplast Starch granules
Mitochondria Glycogen granules
Amylopectin
Amylose
Glycogen
1 µm
0.5 µm
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Figure 5.6a
Chloroplast Starch granules
1 µm
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• 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 µm
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Structural Polysaccharides
• The polysaccharide cellulose is a major component of the tough wall of plant cells
• Like starch, cellulose is a polymer of glucose, but the glycosidic linkages differ
• The difference is based on two ring forms for glucose: alpha (α) and beta (β)
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Animation: Polysaccharides
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Figure 5.7
(a) α and β glucose ring structures
(b) Starch: 1–4 linkage of α glucose monomers (c) Cellulose: 1–4 linkage of β glucose monomers
α Glucose β Glucose
4 1 4 1
4141
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Figure 5.7a
(a) α and β glucose ring structures
α Glucose β Glucose
4 1 4 1
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Figure 5.7b
(b) Starch: 1–4 linkage of α glucose monomers
(c) Cellulose: 1–4 linkage of β glucose monomers
41
41
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• Polymers with α glucose are helical• Polymers with β glucose are straight• In straight structures, H atoms on one
strand can bond with OH groups on other strands
• Parallel cellulose molecules held together this way are grouped into microfibrils, which form strong building materials for plants
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Cell wall
Microfibril
Cellulosemicrofibrils in aplant cell wall
Cellulosemolecules
β Glucosemonomer
10 µm
0.5 µm
Figure 5.8
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Figure 5.8a
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Figure 5.8b
Cell wall
10 µm
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Figure 5.8c
Cellulosemicrofibrils in a plant cell wall
0.5 µm
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• 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
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• Chitin, another structural polysaccharide, is found in the exoskeleton of arthropods
• Chitin also provides structural support for the cell walls of many fungi
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Figure 5.9
Chitin forms the exoskeletonof arthropods.
The structureof the chitinmonomer
Chitin is used to make a strong and flexiblesurgical thread that decomposes after thewound or incision heals.
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Figure 5.9a
Chitin forms the exoskeletonof arthropods.
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Figure 5.9b
Chitin is used to make a strong and flexible surgical thread that decomposes after the wound or incision heals.
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Concept 5.3: Lipids are a diverse group of hydrophobic molecules
• Lipids are the one class of large biological molecules that do not form polymers
• The unifying feature of lipids is having little or no affinity for water
• Lipids are hydrophobic because they consist mostly of hydrocarbons, which form nonpolar covalent bonds
• The most biologically important lipids are fats, phospholipids, and steroids
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Fats
• Fats are constructed from two types of smaller molecules: glycerol and fatty acids
• Glycerol is a three-carbon alcohol with a hydroxyl group attached to each carbon
• A fatty acid consists of a carboxyl group attached to a long carbon skeleton
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Figure 5.10
(a) One of three dehydration reactions in the synthesis of a fat
(b) Fat molecule (triacylglycerol)
Fatty acid(in this case, palmitic acid)
Glycerol
Ester linkage
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Figure 5.10a
(a) One of three dehydration reactions in the synthesis of a fat
Fatty acid(in this case, palmitic acid)
Glycerol
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• Fats separate from water because water molecules form hydrogen bonds with 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
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Figure 5.10b
(b) Fat molecule (triacylglycerol)
Ester linkage
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• Fatty acids vary in length (number of carbons) and in the number and locations of double bonds
• Saturated fatty acids have the maximum number of hydrogen atoms possible and no double bonds
• Unsaturated fatty acids have one or more double bonds
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Animation: Fats
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Figure 5.11
(a) Saturated fat(b) Unsaturated fat
Structuralformula of asaturated fatmolecule
Space-fillingmodel of stearicacid, a saturatedfatty acid
Structuralformula of anunsaturated fatmolecule
Space-filling modelof oleic acid, anunsaturated fattyacid
Cis double bondcauses bending.
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(a) Saturated fat
Structuralformula of asaturated fatmolecule
Space-fillingmodel of stearicacid, a saturatedfatty acid
Figure 5.11a
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Figure 5.11b(b) Unsaturated fat
Structuralformula of anunsaturated fatmolecule
Space-filling modelof oleic acid, anunsaturated fattyacid
Cis double bondcauses bending.
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Figure 5.11c
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Figure 5.11d
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• Fats made from saturated fatty acids are called saturated fats, and are solid at room temperature
• Most animal fats are saturated• Fats made from unsaturated fatty acids are
called unsaturated fats or oils, and are liquid at room temperature
• Plant fats and fish fats are usually unsaturated
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• A diet rich in saturated fats may contribute to cardiovascular disease through plaque deposits
• Hydrogenation is the process of converting unsaturated fats to saturated fats by adding hydrogen
• Hydrogenating vegetable oils also creates unsaturated fats with trans double bonds
• These trans fats may contribute more than saturated fats to cardiovascular disease
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• Certain unsaturated fatty acids are not synthesized in the human body
• These must be supplied in the diet
• These essential fatty acids include the omega-3 fatty acids, required for normal growth, and thought to provide protection against cardiovascular disease
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• The major function of fats is energy storage• Humans and other mammals store their fat in
adipose cells• Adipose tissue also cushions vital organs and
insulates the body
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Phospholipids
• In a phospholipid, two fatty acids and a phosphate group are attached to glycerol
• The two fatty acid tails are hydrophobic, but the phosphate group and its attachments form a hydrophilic head
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Figure 5.12
Choline
Phosphate
Glycerol
Fatty acids
Hydrophilichead
Hydrophobictails
(c) Phospholipid symbol(b) Space-filling model(a) Structural formula
Hyd
rop
hil
ic h
ead
Hyd
rop
ho
bic
tai
ls
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Choline
Phosphate
Glycerol
Fatty acids
(b) Space-filling model(a) Structural formula
Hyd
rop
hil
ic h
ead
Hyd
rop
ho
bic
tai
ls
Figure 5.12a
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• When phospholipids are added to water, they self-assemble into a bilayer, with the hydrophobic tails pointing toward the interior
• The structure of phospholipids results in a bilayer arrangement found in cell membranes
• Phospholipids are the major component of all cell membranes
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Figure 5.13
Hydrophilichead
Hydrophobictail
WATER
WATER
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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
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Figure 5.14
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Concept 5.4: Proteins include a diversity of structures, resulting in a wide range of functions
• Proteins account for more than 50% of the dry mass of most cells
• Protein functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances
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Figure 5.15-a
Enzymatic proteins Defensive proteins
Storage proteins Transport proteins
Enzyme Virus
Antibodies
Bacterium
Ovalbumin Amino acidsfor embryo
Transportprotein
Cell membrane
Function: Selective acceleration of chemical reactionsExample: Digestive enzymes catalyze the hydrolysisof bonds in food molecules.
Function: Protection against disease
Example: Antibodies inactivate and help destroyviruses and bacteria.
Function: Storage of amino acids Function: Transport of substances
Examples: Casein, the protein of milk, is the majorsource of amino acids for baby mammals. Plants havestorage proteins in their seeds. Ovalbumin is theprotein of egg white, used as an amino acid sourcefor the developing embryo.
Examples: Hemoglobin, the iron-containing protein ofvertebrate blood, transports oxygen from the lungs toother parts of the body. Other proteins transportmolecules across cell membranes.
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Figure 5.15-b
Hormonal proteins
Function: Coordination of an organism’s activitiesExample: Insulin, a hormone secreted by thepancreas, causes other tissues to take up glucose,thus regulating blood sugar concentration
Highblood sugar
Normalblood sugar
Insulinsecreted
Signalingmolecules
Receptorprotein
Muscle tissue
Actin Myosin
100 µm 60 µm
Collagen
Connectivetissue
Receptor proteins
Function: Response of cell to chemical stimuliExample: Receptors built into the membrane of anerve cell detect signaling molecules released byother nerve cells.
Contractile and motor proteins
Function: MovementExamples: Motor proteins are responsible for theundulations of cilia and flagella. Actin and myosinproteins are responsible for the contraction ofmuscles.
Structural proteins
Function: SupportExamples: Keratin is the protein of hair, horns,feathers, and other skin appendages. Insects andspiders use silk fibers to make their cocoons and webs,respectively. Collagen and elastin proteins provide afibrous framework in animal connective tissues.
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Figure 5.15a
Enzymatic proteins
Enzyme
Example: Digestive enzymes catalyze the hydrolysisof bonds in food molecules.
Function: Selective acceleration of chemical reactions
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Figure 5.15b
Storage proteins
Ovalbumin Amino acidsfor embryo
Function: Storage of amino acids
Examples: Casein, the protein of milk, is the majorsource of amino acids for baby mammals. Plants havestorage proteins in their seeds. Ovalbumin is theprotein of egg white, used as an amino acid sourcefor the developing embryo.
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Figure 5.15c
Hormonal proteins
Function: Coordination of an organism’s activities
Example: Insulin, a hormone secreted by thepancreas, causes other tissues to take up glucose,thus regulating blood sugar concentration
Highblood sugar
Normalblood sugar
Insulinsecreted
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Figure 5.15d
Muscle tissue
Actin Myosin
100 µm
Contractile and motor proteins
Function: Movement
Examples: Motor proteins are responsible for theundulations of cilia and flagella. Actin and myosinproteins are responsible for the contraction ofmuscles.
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Figure 5.15e
Defensive proteins
Virus
Antibodies
Bacterium
Function: Protection against diseaseExample: Antibodies inactivate and help destroyviruses and bacteria.
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Figure 5.15f
Transport proteins
Transportprotein
Cell membrane
Function: Transport of substancesExamples: Hemoglobin, the iron-containing protein ofvertebrate blood, transports oxygen from the lungs toother parts of the body. Other proteins transportmolecules across cell membranes.
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Figure 5.15g
Signalingmolecules
Receptorprotein
Receptor proteins
Function: Response of cell to chemical stimuli
Example: Receptors built into the membrane of anerve cell detect signaling molecules released byother nerve cells.
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Figure 5.15h
60 µm
Collagen
Connectivetissue
Structural proteins
Function: Support
Examples: Keratin is the protein of hair, horns,feathers, and other skin appendages. Insects andspiders use silk fibers to make their cocoons and webs,respectively. Collagen and elastin proteins provide afibrous framework in animal connective tissues.
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© 2011 Pearson Education, Inc.
Animation: Structural Proteins
Animation: Storage Proteins
Animation: Transport Proteins
Animation: Receptor Proteins
Animation: Contractile Proteins
Animation: Defensive Proteins
Animation: Hormonal Proteins
Animation: Sensory Proteins
Animation: Gene Regulatory Proteins
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• Enzymes are a type of protein that acts as a catalyst to speed up chemical reactions
• Enzymes can perform their functions repeatedly, functioning as workhorses that carry out the processes of life
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Animation: Enzymes
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Polypeptides
• 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
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Amino Acid Monomers
• Amino acids are organic molecules with carboxyl and amino groups
• Amino acids differ in their properties due to differing side chains, called R groups
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Figure 5.UN01
Side chain (R group)
Aminogroup
Carboxylgroup
α carbon
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Figure 5.16Nonpolar side chains; hydrophobic
Side chain(R group)
Glycine(Gly or G)
Alanine(Ala or A)
Valine(Val or V)
Leucine(Leu or L)
Isoleucine (Ile or I)
Methionine(Met or M)
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)
Tyrosine(Tyr or Y)
Asparagine(Asn or N)
Glutamine(Gln or Q)
Electrically charged side chains; hydrophilic
Acidic (negatively charged)
Basic (positively charged)
Aspartic acid(Asp or D)
Glutamic acid(Glu or E)
Lysine(Lys or K)
Arginine(Arg or R)
Histidine(His or H)
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Figure 5.16a
Nonpolar side chains; hydrophobic
Side chain
Glycine(Gly or G)
Alanine(Ala or A)
Valine(Val or V)
Leucine(Leu or L)
Isoleucine(Ile or I)
Methionine(Met or M)
Phenylalanine(Phe or F)
Tryptophan(Trp or W)
Proline(Pro or P)
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Figure 5.16b
Polar side chains; hydrophilic
Serine(Ser or S)
Threonine(Thr or T)
Cysteine(Cys or C)
Tyrosine(Tyr or Y)
Asparagine(Asn or N)
Glutamine(Gln or Q)
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Figure 5.16c
Electrically charged side chains; hydrophilic
Acidic (negatively charged)
Basic (positively charged)
Aspartic acid(Asp or D)
Glutamic acid(Glu or E)
Lysine(Lys or K)
Arginine(Arg or R)
Histidine(His or H)
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Amino Acid Polymers
• 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)
© 2011 Pearson Education, Inc.
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Figure 5.17
Peptide bond
New peptidebond forming
Sidechains
Back-bone
Amino end(N-terminus)
Peptidebond
Carboxyl end(C-terminus)
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Protein Structure and Function
• A functional protein consists of one or more polypeptides precisely twisted, folded, and coiled into a unique shape
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Figure 5.18
(a) A ribbon model (b) A space-filling model
Groove
Groove
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Figure 5.18a
(a) A ribbon model
Groove
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Figure 5.18b
(b) A space-filling model
Groove
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• The sequence of amino acids determines a protein’s three-dimensional structure
• A protein’s structure determines its function
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Figure 5.19
Antibody protein Protein from flu virus
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Four Levels of Protein Structure
• The primary structure of a protein is its unique sequence of amino acids
• Secondary structure, found in most proteins, consists of coils and folds in the polypeptide chain
• Tertiary structure is determined by interactions among various side chains (R groups)
• Quaternary structure results when a protein consists of multiple polypeptide chains
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Animation: Protein Structure Introduction
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Figure 5.20aPrimary structure
Aminoacids
Amino end
Carboxyl end
Primary structure of transthyretin
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• Primary structure, the sequence of amino acids in a protein, is like the order of letters in a long word
• Primary structure is determined by inherited genetic information
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Animation: Primary Protein Structure
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Figure 5.20b
Secondarystructure
Tertiarystructure
Quaternarystructure
Hydrogen bond
α helix
β pleated sheet
β strand
Hydrogenbond
Transthyretinpolypeptide
Transthyretinprotein
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• The coils and folds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone
• Typical secondary structures are a coil called an α helix and a folded structure called a β pleated sheet
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Animation: Secondary Protein Structure
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Secondary structure
Hydrogen bond
α helix
β pleated sheet
β strand, shown as a flatarrow pointing towardthe carboxyl end
Hydrogen bond
Figure 5.20c
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Figure 5.20d
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• Tertiary structure is determined by interactions between R groups, rather than interactions between backbone constituents
• These interactions between R groups 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: Tertiary Protein Structure
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Figure 5.20e
Tertiary structure
Transthyretinpolypeptide
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Figure 5.20f
Hydrogenbond
Disulfidebridge
Polypeptidebackbone
Ionic bond
Hydrophobicinteractions andvan der Waalsinteractions
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Figure 5.20g
Quaternary structure
Transthyretinprotein
(four identicalpolypeptides)
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Figure 5.20h
Collagen
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Hemoglobin
Heme
Iron
α subunit
α subunit
β subunit
β subunit
Figure 5.20i
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Figure 5.20j
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• Quaternary structure results when two or more polypeptide chains form one macromolecule
• Collagen is a fibrous protein consisting of three polypeptides coiled like a rope
• Hemoglobin is a globular protein consisting of four polypeptides: two alpha and two beta chains
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Animation: Quaternary Protein Structure
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Sickle-Cell Disease: A Change in Primary Structure
• A slight change in primary structure can affect a protein’s structure and ability to function
• Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin
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Figure 5.21
PrimaryStructure
Secondaryand TertiaryStructures
QuaternaryStructure Function Red Blood
Cell Shape
β subunit
β subunitβ
β
α
α
Exposedhydrophobicregion
Molecules do notassociate with oneanother; each carriesoxygen.
Molecules crystallizeinto a fiber; capacityto carry oxygen isreduced.
Sickle-cellhemoglobin
Normalhemoglobin
10 µm
10 µm
Sic
kle-
cell
hem
og
lob
inN
orm
al h
emo
glo
bin
1
23
456
7
1
23
456
7
β
βα
α
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Figure 5.21a
10 µm
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Figure 5.21b
10 µm
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What Determines Protein Structure?
• In addition to primary structure, physical and chemical conditions can affect structure
• Alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel
• This loss of a protein’s native structure is called denaturation
• A denatured protein is biologically inactive
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Figure 5.22
Normal protein Denatured protein
Den tur t on
Ren t r t on
a a i
a u a i
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Protein Folding in the Cell
• It is hard to predict a protein’s structure from its primary structure
• Most proteins probably go through several stages on their way to a stable structure
• Chaperonins are protein molecules that assist the proper folding of other proteins
• Diseases such as Alzheimer’s, Parkinson’s, and mad cow disease are associated with misfolded proteins
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Figure 5.23
The cap attaches, causingthe cylinder to changeshape in such a way thatit creates a hydrophilicenvironment for thefolding of the polypeptide.
CapPolypeptide
Correctlyfoldedprotein
Chaperonin(fully assembled)
Steps of ChaperoninAction:
An unfolded poly-peptide enters thecylinder fromone end.
Hollowcylinder
The cap comesoff, and theproperly foldedprotein isreleased.
1
2 3
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Figure 5.23a
Cap
Chaperonin(fully assembled)
Hollowcylinder
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Figure 5.23b
The cap attaches, causingthe cylinder to changeshape in such a way thatit creates a hydrophilicenvironment for thefolding of the polypeptide.
Polypeptide
Correctlyfoldedprotein
Steps of ChaperoninAction:
An unfolded poly-peptide enters thecylinder fromone end.
The cap comesoff, and theproperly foldedprotein isreleased.
32
1
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• Scientists use X-ray crystallography to determine a protein’s structure
• Another method is nuclear magnetic resonance (NMR) spectroscopy, which does not require protein crystallization
• Bioinformatics uses computer programs to predict protein structure from amino acid sequences
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Figure 5.24
DiffractedX-rays
X-raysource X-ray
beam
Crystal Digital detector X-ray diffractionpattern
RNA DNA
RNApolymerase II
EXPERIMENT
RESULTS
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Figure 5.24a
DiffractedX-rays
X-raysource X-ray
beam
Crystal Digital detector X-ray diffractionpattern
EXPERIMENT
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Figure 5.24b
RNA DNA
RNApolymerase II
RESULTS
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Concept 5.5: Nucleic acids store, transmit, and help express hereditary information
• The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene
• Genes are made of DNA, a nucleic acid made of monomers called nucleotides
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The Roles of Nucleic Acids
• There are two types of nucleic acids– Deoxyribonucleic acid (DNA)
– Ribonucleic acid (RNA)
• DNA provides directions for its own replication
• DNA directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis
• Protein synthesis occurs on ribosomes
© 2011 Pearson Education, Inc.
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Figure 5.25-1
Synthesis ofmRNA
mRNA
DNA
NUCLEUSCYTOPLASM
1
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Figure 5.25-2
Synthesis ofmRNA
mRNA
DNA
NUCLEUSCYTOPLASM
mRNAMovement ofmRNA intocytoplasm
1
2
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Figure 5.25-3
Synthesis ofmRNA
mRNA
DNA
NUCLEUSCYTOPLASM
mRNA
Ribosome
AminoacidsPolypeptide
Movement ofmRNA intocytoplasm
Synthesisof protein
1
2
3
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The Components of Nucleic Acids
• Nucleic acids are polymers called polynucleotides
• Each polynucleotide is made of monomers called nucleotides
• Each nucleotide consists of a nitrogenous base, a pentose sugar, and one or more phosphate groups
• The portion of a nucleotide without the phosphate group is called a nucleoside
© 2011 Pearson Education, Inc.
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Figure 5.26
Sugar-phosphate backbone5′ end
5′C
3′C
5′C
3′C
3′ end
(a) Polynucleotide, or nucleic acid
(b) Nucleotide
Phosphategroup Sugar
(pentose)
Nucleoside
Nitrogenousbase
5′C
3′C
1′C
Nitrogenous bases
Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA)
Adenine (A) Guanine (G)
Sugars
Deoxyribose (in DNA) Ribose (in RNA)
(c) Nucleoside components
Pyrimidines
Purines
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Figure 5.26ab
Sugar-phosphate backbone5′ end
5′C
3′C
5′C
3′C
3′ end
(a) Polynucleotide, or nucleic acid
(b) Nucleotide
Phosphategroup Sugar
(pentose)
Nucleoside
Nitrogenousbase
5′C
3′C
1′C
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Figure 5.26c
Nitrogenous bases
Cytosine (C)
Thymine (T, in DNA)
Uracil (U, in RNA)
Adenine (A) Guanine (G)
Sugars
Deoxyribose (in DNA)
Ribose (in RNA)
(c) Nucleoside components
Pyrimidines
Purines
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• Nucleoside = nitrogenous base + sugar
• There are two families of nitrogenous bases
– Pyrimidines (cytosine, thymine, and uracil) have a single six-membered ring
– Purines (adenine and guanine) have a six-membered ring fused to a five-membered ring
• In DNA, the sugar is deoxyribose; in RNA, the sugar is ribose
• Nucleotide = nucleoside + phosphate group
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Nucleotide Polymers
• Nucleotide polymers are linked together to build a polynucleotide
• 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 on 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
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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
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• The nitrogenous bases in DNA pair up and form hydrogen bonds: adenine (A) always with thymine (T), and guanine (G) always with cytosine (C)
• 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
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Figure 5.27
Sugar-phosphatebackbones
Hydrogen bonds
Base pair joinedby hydrogen bonding
Base pair joinedby hydrogen
bonding
(b) Transfer RNA(a) DNA
5′ 3′
5′3′
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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
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Figure 5.UN02
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Figure 5.UN02a
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Figure 5.UN02b
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Figure 5. UN03
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Figure 5. UN04
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Figure 5. UN05
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Figure 5. UN06
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Figure 5. UN07
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Figure 5. UN08
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Figure 5. UN09
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Figure 5. UN10
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Figure 5. UN11
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Figure 5. UN12
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Figure 5. UN13