05 lecture presentation pc
TRANSCRIPT
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LECTURE PRESENTATIONS
For CAMPBELL BIOLOGY, NINTH EDITIONJane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
© 2011 Pearson Education, Inc.
Lectures by
Erin 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 classesof large biological molecules: carbohydrates,lipids, proteins, and nucleic acids
• Macromolecules are large molecules
composed of thousands of covalentlyconnected atoms
• Molecular structure and function areinseparable
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Concept 5.1: Macromolecules are polymers,
built from monomers
• A polymer is a long molecule consisting ofmany similar building blocks
•These small building-block molecules arecalled monomers
• Three of the four classes of life’s organicmolecules are polymers
– Carbohydrates – Proteins
– Nucleic acids
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• A dehydration reaction occurs when twomonomers bond together through the loss of awater molecule
• Polymers are disassembled to monomers byhydrolysis, a reaction that is essentially thereverse of the dehydration reaction
The Synthesis and Breakdown of Polymers
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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 differentmacromolecules
• Macromolecules vary among cells of anorganism, vary more within a species, andvary even more between species
• An immense variety of polymers can be builtfrom a small set of monomers
HO
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Concept 5.2: Carbohydrates serve as fuel
and building material
• Carbohydrates include sugars and thepolymers of sugars
•
The simplest carbohydrates aremonosaccharides, or single sugars
• Carbohydrate macromolecules arepolysaccharides, polymers composed of
many sugar building blocks
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Sugars
• Monosaccharides have molecular formulasthat are usually multiples of CH2O
• Glucose (C6H12O6) is the most commonmonosaccharide
• Monosaccharides are classified by
– The location of the carbonyl group (as aldoseor ketose)
– The number of carbons in the carbon skeleton
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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, inaqueous solutions many sugars form rings
• Monosaccharides serve as a major fuel forcells and as raw material for buildingmolecules
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Fi 5 4
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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 dehydrationreaction joins two monosaccharides
• This covalent bond is called a glycosidiclinkage
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Fi 5 5
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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 polysaccharideare determined by its sugar monomers and thepositions 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 withinchloroplasts and other plastids
• The simplest form of starch is amylose
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Figure 5 6
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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 m
0.5 m
Figure 5 6a
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Figure 5.6a
Chloroplast Starch granules
1 m
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• Glycogen is a storage polysaccharide inanimals
• Humans and other vertebrates storeglycogen mainly in liver and muscle cells
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Figure 5 6b
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Figure 5.6b
Mitochondria Glycogen granules
0.5 m
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Structural Polysaccharides
• The polysaccharide cellulose is a majorcomponent 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 forglucose: alpha () and beta ()
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Figure 5 7a
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Figure 5.7a
(a) and glucose ring structures
Glucose Glucose
4 1 4 1
Figure 5.7b
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Figure 5.7b
(b) Starch: 1 –4 linkage of glucose monomers
(c) Cellulose: 1 –4 linkage of glucose monomers
41
41
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• Polymers with glucose are helical• Polymers with glucose are straight
• In straight structures, H atoms on one
strand can bond with OH groups on otherstrands
• Parallel cellulose molecules held togetherthis way are grouped into microfibrils,
which form strong building materials forplants
Figure 5.8
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Cell wall
Microfibril
Cellulosemicrofibrils in aplant cell wall
Cellulosemolecules
Glucose
monomer
10 m
0.5 m
g
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• Enzymes that digest starch by hydrolyzing linkages can’t hydrolyze linkages in cellulose
• Cellulose in human food passes through thedigestive tract as insoluble fiber
• Some microbes use enzymes to digestcellulose
• Many herbivores, from cows to termites, have
symbiotic relationships with these microbes
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• Chitin, another structural polysaccharide, isfound in the exoskeleton of arthropods
• Chitin also provides structural support for thecell walls of many fungi
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Figure 5.9
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Chitin forms the exoskeletonof arthropods.
The structureof the chitinmonomer
Chitin is used to make a strong and flexiblesurgical 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 biologicalmolecules that do not form polymers
•
The unifying feature of lipids is having little orno affinity for water
• Lipids are hydrophobic becausethey consistmostly 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 smallermolecules: glycerol and fatty acids
• Glycerol is a three-carbon alcohol with ahydroxyl group attached to each carbon
• A fatty acid consists of a carboxyl groupattached to a long carbon skeleton
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Figure 5.10
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(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
Figure 5.10a
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(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 watermolecules form hydrogen bonds with eachother and exclude the fats
• In a fat, three fatty acids are joined toglycerol by an ester linkage, creating atriacylglycerol, or triglyceride
Figure 5.10b
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(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 doublebonds
• Saturated fatty acids have the maximumnumber of hydrogen atoms possible and nodouble bonds
• Unsaturated fatty acids have one or more
double bonds
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Animation: FatsRight-click slide / select ―Play‖
( ) S t t d f tFigure 5.11a
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(a) Saturated fat
Structural
formula of asaturated fatmolecule
Space-fillingmodel of stearicacid, a saturated
fatty acid
Figure 5.11b(b) Unsaturated fat
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(b) Unsaturated fat
Structuralformula of anunsaturated fatmolecule
Space-filling modelof oleic acid, anunsaturated fattyacid
Cis double bondcauses bending.
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• Fats made from saturated fatty acids arecalled saturated fats, and are solid at roomtemperature
• Most animal fats are saturated
• Fats made from unsaturated fatty acids arecalled unsaturated fats or oils, and are liquidat room temperature
• Plant fats and fish fats are usually unsaturated
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• A diet rich in saturated fats may contribute tocardiovascular disease through plaque deposits
• Hydrogenation is the process of convertingunsaturated fats to saturated fats by addinghydrogen
• Hydrogenating vegetable oils also createsunsaturated fats with trans double bonds
• These trans fats may contribute more thansaturated fats to cardiovascular disease
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• Certain unsaturated fatty acids are notsynthesized in the human body
• These must be supplied in the diet
•
These essential fatty acids include the omega-3fatty acids, required for normal growth, andthought to provide protection againstcardiovascular disease
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•The major function of fats is energy storage
• Humans and other mammals store their fat inadipose cells
• Adipose tissue also cushions vital organs andinsulates the body
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Phospholipids
•In a phospholipid, two fatty acids and aphosphate group are attached to glycerol
• The two fatty acid tails are hydrophobic, butthe phosphate group and its attachments
form a hydrophilic head
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Figure 5.12
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Choline
Phosphate
Glycerol
Fatty acids
Hydrophilichead
Hydrophobictails
(c) Phospholipid symbol(b) Space-filling model(a) Structural formula
H y d r o p h i l i c h e a d
H y d r o p h o b i c t a i l s
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•When phospholipids are added to water, theyself-assemble into a bilayer, with thehydrophobic tails pointing toward the interior
• The structure of phospholipids results in a
bilayer arrangement found in cell membranes
• Phospholipids are the major component of allcell membranes
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Figure 5.13
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Hydrophilichead
Hydrophobictail
WATER
WATER
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Steroids
•Steroids are lipids characterized by a carbonskeleton consisting of four fused rings
• Cholesterol, an important steroid, is acomponent in animal cell membranes
• Although cholesterol is essential in animals,high levels in the blood may contribute tocardiovascular 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
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Enzymatic proteins Defensive proteins
Storage proteins Transport proteins
Enzyme Virus
Antibodies
Bacterium
Ovalbumin Amino acidsfor embryo
Transportprotein
Cell membrane
Function: Selective acceleration of chemical reactions
Example: 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.
Figure 5.15-b
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Hormonal proteins
Function: Coordination of an organism’s activities
Example: Insulin, a hormone secreted by the
pancreas, causes other tissues to take up glucose,thus regulating blood sugar concentration
Highblood sugar
Normalblood sugar
Insulinsecreted
Signalingmolecules
Receptorprotein
Muscle tissue
Actin Myosin
100 m 60 m
Collagen
Connectivetissue
Receptor proteins
Function: Response of cell to chemical stimuli
Example: Receptors built into the membrane of a
nerve cell detect signaling molecules released byother nerve cells.
Contractile and motor proteinsFunction: Movement
Examples: Motor proteins are responsible for theundulations of cilia and flagella. Actin and myosinproteins are responsible for the contraction ofmuscles.
Structural proteinsFunction: 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.
Figure 5.15a
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Enzymatic proteins
Enzyme
Example: Digestive enzymes catalyze the hydrolysisof bonds in food molecules.
Function: Selective acceleration of chemical reactions
Figure 5.15b
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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 the
protein of egg white, used as an amino acid sourcefor the developing embryo.
Figure 5.15c
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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
High
blood sugar
Normal
blood sugar
Insulinsecreted
Figure 5.15d
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Muscle tissue
Actin Myosin
100 m
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.
Figure 5.15e
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Defensive proteins
Virus
Antibodies
Bacterium
Function: Protection against disease
Example: Antibodies inactivate and help destroyviruses and bacteria.
Figure 5.15f
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Transport proteins
Transportprotein
Cell membrane
Function: Transport of substances
Examples: Hemoglobin, the iron-containing protein ofvertebrate blood, transports oxygen from the lungs toother parts of the body. Other proteins transport
molecules across cell membranes.
Figure 5.15g
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Signalingmolecules
Receptorprotein
Receptor proteins
Function: Response of cell to chemical stimuli
Example: Receptors built into the membrane of anerve cell detect signaling molecules released by
other nerve cells.
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•
Enzymes are a type of protein that acts as acatalyst to speed up chemical reactions
• Enzymes can perform their functionsrepeatedly, functioning as workhorses that
carry out the processes of life
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Polypeptides
•
Polypeptides are unbranched polymers builtfrom the same set of 20 amino acids
• A protein is a biologically functional moleculethat consists of one or more polypeptides
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Amino Acid Monomers
•
Amino acids are organic molecules withcarboxyl and amino groups
• Amino acids differ in their properties due todiffering side chains, called R groups
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Figure 5.UN01
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Side chain (R group)
Aminogroup
Carboxylgroup
carbon
Figure 5.16a
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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)
Figure 5.16bPolar side chains; hydrophilic
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Serine(Ser or S)
Threonine(Thr or T)
Cysteine(Cys or C)
Tyrosine(Tyr or Y)
Asparagine(Asn or N)
Glutamine(Gln or Q)
Figure 5.16c
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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)
A i A id P l
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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 tomore than a thousand monomers
• Each polypeptide has a unique linearsequence of amino acids, with a carboxyl end(C-terminus) and an amino end (N-terminus)
© 2011 Pearson Education, Inc.
Figure 5.17
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Peptide bond
New peptidebond forming
Sidechains
Back-bone
Amino end(N-terminus)
Peptidebond
Carboxyl end(C-terminus)
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Figure 5.18
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(a) A ribbon model (b) A space-filling model
Groove
Groove
Figure 5.18a
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(a) A ribbon model
Groove
Figure 5.18b
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(b) A space-filling model
Groove
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•
The sequence of amino acids determines aprotein’s three-dimensional structure
• A protein’s structure determines its function
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Figure 5.19
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Antibody protein Protein from flu virus
Four Levels of Protein Structure
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Four Levels of Protein Structure
•
The primary structure of a protein is its uniquesequence of amino acids
• Secondary structure, found in most proteins,consists of coils and folds in the polypeptide
chain
• Tertiary structure is determined by interactionsamong various side chains (R groups)
• Quaternary structure results when a proteinconsists of multiple polypeptide chains
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Figure 5.20a Primary structure
Amino
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Aminoacids
Amino end
Carboxyl end
Primary structure of transthyretin
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•
Primary structure, the sequence of aminoacids in a protein, is like the order of lettersin a long word
• Primary structure is determined by inherited
genetic information
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Figure 5.20b
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Secondarystructure
Tertiarystructure
Quaternarystructure
Hydrogen bond
helix
pleated sheet
strand
Hydrogen
bond
Transthyretin
polypeptide
Transthyretinprotein
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•
The coils and folds of secondary structureresult from hydrogen bonds between repeatingconstituents of the polypeptide backbone
• Typical secondary structures are a coil called
an helix and a folded structure called a pleated sheet
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Secondary structureFigure 5.20c
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Hydrogen bond
helix
pleated sheet
strand, shown as a flatarrow pointing towardthe carboxyl end
Hydrogen bond
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•
Tertiary structure is determined byinteractions between R groups, rather thaninteractions between backbone constituents
• These interactions between R groups include
hydrogen bonds, ionic bonds, hydrophobicinteractions, and van der Waals interactions
• Strong covalent bonds called disulfidebridges may reinforce the protein’s structure
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Figure 5.20e
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Tertiary structure
Transthyretinpolypeptide
Figure 5.20f
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Hydrogenbond
Disulfidebridge
Polypeptidebackbone
Ionic bond
Hydrophobicinteractions andvan der Waalsinteractions
Figure 5.20g
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Quaternary structure
Transthyretinprotein(four identicalpolypeptides)
Figure 5.20h
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Collagen
Heme
Iron
Figure 5.20i
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Hemoglobin
subunit
subunit
subunit
subunit
Figure 5.20j
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•
Quaternary structure results when two ormore polypeptide chains form onemacromolecule
• 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 betachains
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Sickle-Cell Disease: A Change in Primary
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Sickle Cell Disease: A Change in Primary
Structure
• A slight change in primary structure can affecta protein’s structure and ability to function
• Sickle-cell disease, an inherited blood
disorder, results from a single amino acidsubstitution in the protein hemoglobin
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Figure 5.21
PrimaryStructure
Secondaryand TertiaryStructures
QuaternaryStructure
FunctionRed BloodCell Shape
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Structuresp
subunit
subunit
Exposedhydrophobicregion
Molecules do notassociate with oneanother; each carriesoxygen.
Molecules crystallizeinto a fiber; capacityto carry oxygen isreduced.
Sickle-cellhemoglobin
Normalhemoglobin
10 m
10 m
S i c k l e - c e l l h e m o g l o b i n
N
o r m a l h e m o g l o b
i n
1
2
3
4
5
6
7
1
2
3
4
5
6
7
What Determines Protein Structure?
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What Determines Protein Structure?
•
In addition to primary structure, physical andchemical 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
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Normal protein Denatured protein
tu
Protein Folding in the Cell
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Protein Folding in the Cell
•
It is hard to predict a protein’s structure fromits primary structure
• Most proteins probably go through severalstages on their way to a stable structure
• Chaperonins are protein molecules thatassist the proper folding of other proteins
• Diseases such as Alzheimer’s, Parkinson’s,
and mad cow disease are associated withmisfolded proteins
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Figure 5.23
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The cap attaches, causingthe cylinder to changeshape in such a way thatit creates a hydrophilic
environment for thefolding of the polypeptide.
Cap
Polypeptide
Correctly
foldedprotein
Chaperonin(fully assembled)
Steps of ChaperoninAction:
An unfolded poly-peptide enters the
cylinder fromone end.
Hollow
cylinder
The cap comesoff, and theproperly foldedprotein is
released.
1
2 3
Figure 5.23a
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Cap
Chaperonin(fully assembled)
Hollow
cylinder
Figure 5.23b
Correctly
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The cap attaches, causingthe cylinder to change
shape in such a way thatit creates a hydrophilicenvironment for thefolding of the polypeptide.
Polypeptide
yfoldedprotein
Steps of ChaperoninAction:
An unfolded poly-peptide enters thecylinder fromone end.
The cap comesoff, and the
properly foldedprotein isreleased.
32
1
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•
Scientists use X-ray crystallography todetermine a protein’s structure
• Another method is nuclear magneticresonance (NMR) spectroscopy, which does
not require protein crystallization• Bioinformatics uses computer programs to
predict protein structure from amino acidsequences
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Figure 5.24a
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DiffractedX-rays
X-raysource X-raybeam
Crystal Digital detector X-ray diffractionpattern
EXPERIMENT
Figure 5.24b
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RNA DNA
RNApolymerase II
RESULTS
Concept 5.5: Nucleic acids store, transmit,
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p , ,
and help express hereditary information
• The amino acid sequence of a polypeptide isprogrammed by a unit of inheritance called agene
• Genes are made of DNA, a nucleic acidmade of monomers called nucleotides
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The Roles of Nucleic Acids
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•
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
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Figure 5.25-1
DNA
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Synthesis ofmRNA
mRNA
NUCLEUS
CYTOPLASM
1
Figure 5.25-2
DNA
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Synthesis ofmRNA
mRNA
NUCLEUS
CYTOPLASM
mRNA
Movement ofmRNA intocytoplasm
1
2
Figure 5.25-3
DNA
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Synthesis ofmRNA
mRNA
NUCLEUS
CYTOPLASM
mRNA
Ribosome
AminoacidsPolypeptide
Movement ofmRNA intocytoplasm
Synthesisof protein
1
2
3
The Components of Nucleic Acids
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p
• Nucleic acids are polymers calledpolynucleotides
• Each polynucleotide is made of monomerscalled nucleotides
• Each nucleotide consists of a nitrogenousbase, a pentose sugar, and one or morephosphate groups
•
The portion of a nucleotide without thephosphate group is called a nucleoside
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Figure 5.26ab
Sugar-phosphate backbone5 end
5C
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3C
5C
3C
3 end
(a) Polynucleotide, or nucleic acid
(b) Nucleotide
Phosphategroup
Sugar(pentose)
Nucleoside
Nitrogenousbase
5C
3C
1C
Figure 5.26c
Nitrogenous bases
Pyrimidines
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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
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• Nucleotide polymers are linked together to builda polynucleotide
• Adjacent nucleotides are joined by covalentbonds that form between the —OH group on the
3 carbon of one nucleotide and the phosphateon 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 mRNApolymer is unique for each gene
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The Structures of DNA and RNA Molecules
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• RNA molecules usually exist as singlepolypeptide chains
• DNA molecules have two polynucleotidesspiraling around an imaginary axis, forming a
double helix• In the DNA double helix, the two backbones
run in opposite 5→ 3 directions from eachother, an arrangement referred to asantiparallel
• One DNA molecule includes many genes
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• The nitrogenous bases in DNA pair up and formhydrogen bonds: adenine (A) always withthymine (T), and guanine (G) always withcytosine (C)
• Called complementary base pairing• Complementary pairing can also occur between
two RNA molecules or between parts of the samemolecule
• In RNA, thymine is replaced by uracil (U) so Aand U pair
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Figure 5.27
Sugar-phosphate5 3
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g p pbackbones
Hydrogen bonds
Base pair joinedby hydrogen bonding
Base pair joinedby hydrogen
bonding
(b) Transfer RNA(a) DNA
53
DNA and Proteins as Tape Measures of
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Evolution
• The linear sequences of nucleotides in DNAmolecules 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 assessevolutionary kinship
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The Theme of Emergent Properties in the
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Chemistry of Life: A Review
• Higher levels of organization result in theemergence of new properties
• Organization is the key to the chemistry of life
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Figure 5.UN02a
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Figure 5.UN02b
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