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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



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




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




• 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




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



Figure 5.2b

(b) Hydrolysis: breaking down a polymer

Hydrolysis addsa water molecule,breaking a bond.

1 2 3 4

1 2 3



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




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




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




Figure 5.3a

Aldose (Aldehyde Sugar) Ketose (Ketone Sugar)

Glyceraldehyde

Trioses: 3-carbon sugars (C3H6O3)

Dihydroxyacetone



Figure 5.3b

Pentoses: 5-carbon sugars (C5H10O5)

Ribose Ribulose




Figure 5.3c


Hexoses: 6-carbon sugars (C6H12O6)

Glucose Galactose Fructose



• 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


Fi 5 4



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



• A disaccharide is formed when a dehydrationreaction joins two monosaccharides

• This covalent bond is called a glycosidiclinkage


Fi 5 5



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



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




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


Figure 5 6



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



Figure 5.6a

Chloroplast Starch granules

1 m



• Glycogen is a storage polysaccharide inanimals

• Humans and other vertebrates storeglycogen mainly in liver and muscle cells


Figure 5 6b



Figure 5.6b

Mitochondria Glycogen granules

0.5 m



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 ()


Figure 5 7a



Figure 5.7a

(a) and glucose ring structures

Glucose Glucose

4 1 4 1

Figure 5.7b



Figure 5.7b

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

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

41

41




• 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



Cell wall

Microfibril

Cellulosemicrofibrils in aplant cell wall

Cellulosemolecules

Glucose

monomer

10 m

0.5 m

g



• 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




• Chitin, another structural polysaccharide, isfound in the exoskeleton of arthropods

• Chitin also provides structural support for thecell walls of many fungi


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 the

wound or incision heals.



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




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


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

Figure 5.10a



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

Fatty acid(in this case, palmitic acid)

Glycerol




• 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



(b) Fat molecule (triacylglycerol)

Ester linkage



• 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





Animation: FatsRight-click slide / select ―Play‖

( ) S t t d f tFigure 5.11a



(a) Saturated fat

Structural

formula of asaturated fatmolecule

Space-fillingmodel of stearicacid, a saturated

fatty acid

Figure 5.11b(b) Unsaturated fat



(b) Unsaturated fat

Structuralformula of anunsaturated fatmolecule

Space-filling modelof oleic acid, anunsaturated fattyacid

Cis double bondcauses bending.



• 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




• 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




• 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




•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




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


Figure 5.12



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



•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


Figure 5.13



Hydrophilichead

Hydrophobictail

WATER

WATER



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


Figure 5.14



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


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 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



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



Enzymatic proteins

Enzyme

Example: Digestive enzymes catalyze the hydrolysisof bonds in food molecules.

Function: Selective acceleration of chemical reactions

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 the

protein of egg white, used as an amino acid sourcefor the developing embryo.

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

High

blood sugar

Normal

blood sugar

Insulinsecreted

Figure 5.15d



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



Defensive proteins

Virus

Antibodies

Bacterium

Function: Protection against disease

Example: Antibodies inactivate and help destroyviruses and bacteria.

Figure 5.15f



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



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.




Animation: Storage ProteinsRight-click slide / select ―Play‖




Animation: Transport ProteinsRight-click slide / select ―Play‖




Animation: Receptor ProteinsRight-click slide / select ―Play‖




Animation: Contractile ProteinsRight-click slide / select ―Play‖




Animation: Defensive ProteinsRight-click slide / select ―Play‖




Animation: Hormonal ProteinsRight-click slide / select ―Play‖




Animation: Sensory ProteinsRight-click slide / select ―Play‖




Animation: Gene Regulatory ProteinsRight-click slide / select ―Play‖



•

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





Animation: EnzymesRight-click slide / select ―Play‖



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




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


Figure 5.UN01



Side chain (R group)

Aminogroup

Carboxylgroup

carbon

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)

Figure 5.16bPolar 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)

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)

A i A id P l



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)


Figure 5.17



Peptide bond

New peptidebond forming

Sidechains

Back-bone

Amino end(N-terminus)

Peptidebond

Carboxyl end(C-terminus)



Figure 5.18



(a) A ribbon model (b) A space-filling model

Groove

Groove

Figure 5.18a



(a) A ribbon model

Groove

Figure 5.18b



(b) A space-filling model

Groove



•

The sequence of amino acids determines aprotein’s three-dimensional structure

• A protein’s structure determines its function


Figure 5.19



Antibody protein Protein from flu virus

Four Levels of Protein Structure



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





Animation: Protein Structure IntroductionRight-click slide / select ―Play‖

Figure 5.20a Primary structure

Amino



Aminoacids

Amino end

Carboxyl end

Primary structure of transthyretin



•

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





Animation: Primary Protein StructureRight-click slide / select ―Play‖

Figure 5.20b



Secondarystructure

Tertiarystructure

Quaternarystructure

Hydrogen bond

helix

pleated sheet

strand

Hydrogen

bond

Transthyretin

polypeptide

Transthyretinprotein



•

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





Animation: Secondary Protein StructureRight-click slide / select ―Play‖

Secondary structureFigure 5.20c



Hydrogen bond

helix

pleated sheet

strand, shown as a flatarrow pointing towardthe carboxyl end

Hydrogen bond



•

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





Animation: Tertiary Protein StructureRight-click slide / select ―Play‖

Figure 5.20e



Tertiary structure

Transthyretinpolypeptide

Figure 5.20f



Hydrogenbond

Disulfidebridge

Polypeptidebackbone

Ionic bond

Hydrophobicinteractions andvan der Waalsinteractions

Figure 5.20g



Quaternary structure

Transthyretinprotein(four identicalpolypeptides)

Figure 5.20h



Collagen

Heme

Iron

Figure 5.20i



Hemoglobin

subunit

subunit

subunit

subunit

Figure 5.20j



•

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





Animation: Quaternary Protein StructureRight-click slide / select ―Play‖

Sickle-Cell Disease: A Change in Primary



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


Figure 5.21

PrimaryStructure

Secondaryand TertiaryStructures

QuaternaryStructure

FunctionRed BloodCell Shape



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?



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


Figure 5.22



Normal protein Denatured protein

tu

Protein Folding in the Cell



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


Figure 5.23



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



Cap

Chaperonin(fully assembled)

Hollow

cylinder

Figure 5.23b

Correctly



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



•

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


Figure 5.24a



DiffractedX-rays

X-raysource X-raybeam

Crystal Digital detector X-ray diffractionpattern

EXPERIMENT

Figure 5.24b



RNA DNA

RNApolymerase II

RESULTS

Concept 5.5: Nucleic acids store, transmit,



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


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


Figure 5.25-1

DNA



Synthesis ofmRNA

mRNA

NUCLEUS

CYTOPLASM

1

Figure 5.25-2

DNA



Synthesis ofmRNA

mRNA

NUCLEUS

CYTOPLASM

mRNA

Movement ofmRNA intocytoplasm

1

2

Figure 5.25-3

DNA



Synthesis ofmRNA

mRNA

NUCLEUS

CYTOPLASM

mRNA

Ribosome

AminoacidsPolypeptide

Movement ofmRNA intocytoplasm

Synthesisof protein

1

2

3

The Components of Nucleic Acids



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


Figure 5.26ab

Sugar-phosphate backbone5 end

5C



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



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



• 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


Nucleotide Polymers



• 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


The Structures of DNA and RNA Molecules



• 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




• 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


Figure 5.27

Sugar-phosphate5 3



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



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


The Theme of Emergent Properties in the



Chemistry of Life: A Review

• Higher levels of organization result in theemergence of new properties

• Organization is the key to the chemistry of life


Figure 5.UN02a



Figure 5.UN02b

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