Modern Chemistry - Chapter 23

Chapter 23
Preview
Lesson Starter
Objectives
Carbohydrates
Lipids
Chapter 23
Section 1 Carbohydrates and Lipids
Lesson Starter
Why does the can of diet soft drink float and the can
of regular soft drink sink?
The aspartame used to sweeten the diet soft drink is
about 200 times as sweet as sucrose.
The regular soft drink is denser than the diet soft
drink, because there is such a large amount of sugar
in the regular soft drink, and only a small amount of
sweetener in the diet soft drink.
Chapter 23
Objectives
Describe the structural characteristics of simple
carbohydrates and complex carbohydrates.
Explain the role of carbohydrates in living systems.
Describe the structural characteristics of lipid
molecules.
Identify the functions of lipids in living cells.
Chapter 23
Biochemistry is the study of the chemicals and

reactions that occur in living things.
Biochemical compounds are often large and complex
organic molecules, but their chemistry is similar to
that of the smaller organic molecules
Chapter 23
Carbohydrates
Carbohydrates are molecules that are composed of
carbon, hydrogen, and oxygen atoms in a 1:2:1 ratio,
and provide nutrients to the cells of living things.
sugars, starches, and cellulose
Carbohydrates are produced by plants through a
process called photosynthesis.
Carbohydrates provide nearly all of the energy that is
available in most plant-derived food.
Chapter 23
Carbohydrates
Click below to watch the Visual Concept.
Visual Concept
Chapter 23
Types of Carbohydrates
Chapter 23
Carbohydrates, continued
Monosaccharides
A monosaccharide is a simple sugar that is the
basic subunit of a carbohydrate.
A single monosaccharide molecule contains three to
seven carbon atoms.
Monosaccharide compounds are
typically sweet-tasting
white solids at room temperature
water soluble
Chapter 23
Monosaccharides, continued
The most common
monosaccharides are
glucose (also called
dextrose) and fructose.
Both have the formula
C6(H2O)6.
Their structural formulas
differ.
Chapter 23
Structures of Carbohydrates
Chapter 23
Monosaccharides
Visual Concept
Chapter 23
Disaccharides
A disaccharide is a sugar that consists of two
monosaccharide units that are joined together.
sucrose, C12H22O11
A molecule of sucrose forms when a glucose molecule
bonds to a fructose molecule.
lactose
Lactose is made up of a sugar called galactose and
glucose.
Chapter 23
Disaccharides
Visual Concept
Chapter 23
Carbohydrate Reactions
Carbohydrates undergo two important kinds of
reactions: condensation reactions and hydrolysis
reactions.
A condensation reaction is a reaction in which two

molecules or parts of the same molecule combine.
Chapter 23
Carbohydrate Reactions, continued
Hydrolysis is a chemical reaction between water
and another substance to form two or more new
substances.
Disaccharides and longer-chain polysaccharides
can be broken down into smaller sugar units by
hydrolysis.
Chapter 23
Cation Hydrolysis
Visual Concept
Chapter 23
Anion Hydrolysis
Visual Concept
Chapter 23
Polysaccharides
When many monosaccharides or disaccharides
combine in a series of condensation reactions, they
form a polysaccharide.
A polysaccharide is a carbohydrate made up of long
chains of simple sugars.
Cellulose, starch, and glycogen are polymers of
glucose.
Sheets of cellulose make up plant cell walls.
Starch is the storage form of glucose in plants.
Chapter 23
Polysaccharides, continued
Glycogen, cellulose, and starch differ in their
arrangement of glucose monomers.
Chapter 23
Lipids
A lipid is a type of biochemical that does not dissolve
in water, has a high percentage of C and H atoms,
and is soluble in nonpolar solvents.
As a class, lipids are not nearly as similar to each
other as carbohydrates are.
Long-chain fatty acids, phospholipids, steroids, and
cholesterol are lipids.
Chapter 23
Types of Lipids
Visual Concept
Chapter 23
Lipids, continued
Fatty Acids and Triglycerides
Fatty acids consist of a long, nonpolar hydrocarbon
tail and a polar carboxylic acid functional group at
the head.
They have hydrophilic polar heads, but their

hydrocarbon chains make them insoluble in
water.
H
H
H
H
H
H
H
H
H
H
H
H
H
H
C
HO
hydrophilic region
hydrophobic region
Chapter 23
Lipids, continued
Fatty Acids and Triglycerides, continued
Triglycerides are formed by condensation reactions in
which three fatty acid molecules bond to one glycerol (a
type of alcohol) molecule.
Fats and oils that are the most common group of lipids in your
diet.
Because they have a large amount of saturated fatty acids,
fats are solids at room temperature.
Oils have more unsaturated fatty acids than fats, and are
Fat
is stored in adipose tissue until it is needed as an
liquids
energy source.
Chapter 23
Lipids, continued
Fatty Acids and Triglycerides, continued
When a fat combines with NaOH, an acid-base reaction
called saponification occurs, and a salt and water
form.
This salt is made up of molecules that have long
carboxylic acid chains and is called soap.
Lipids that react with a base to form soap are called
saponifiable lipids, which include fats, oils, and fatty
acids.
Chapter 23
Lipids, continued
Other Important Lipids
Compound saponifiable lipids play an important
role in biochemical processes.
These lipids are structurally similar to triglycerides in that
at least one fatty acid is bonded to the central glycerol or
glycerol-like unit.
These molecules may also have phosphate groups,
sugar units, or nitrogen containing groups.
Phospholipids, are compound saponifiable lipids

and are the main structural component of cell
membranes.
Chapter 23
Lipids, continued
Other Important Lipids, continued
Phospholipids are arranged in a bilayer, or double layer,
at the surface of the cell.
Chapter 23
Lipids, continued
Other Important Lipids, continued
Nonsaponifiable lipids are nonpolar compounds that do
not form soap.
steroids, many vitamins, and bile acids
Cholesterol is a steroid present in animal cell
membranes and is a precursor of many hormones.
Chapter 23
Section 2 Amino Acids and Proteins
Preview
Lesson Starter
Objectives
Amino Acids
Proteins
Proteins as Enzymes
Chapter 23
Lesson Starter
carboxylic acid
RCOH
amine
RNR
R
condensation reaction to form dipeptide bond

R
H
N
H
H
OH
C
O
OH
H
N
H
H
+ H2O
OH
C
O
Chapter 23
Objectives
Describe the basic structure of amino acids and the
formation of polypeptides.
Determine the significance of amino acid side chains
to the three-dimensional structure of a protein and
the function of a protein.
Describe the functions of proteins in cells.
Identify the effects of enzymes on biological
molecules.
Chapter 23
Amino acid molecules are the basic building blocks

of proteins.
More than 700 types of amino acids occur in nature.
Only 20 types of amino acids are found in human
proteins.
The human body can synthesize only 11 of the 20
amino acids as needed.
The other nine, called the essential amino acids,
have to be supplied by the food that we eat.
Chapter 23
Amino Acids
Amino acids are organic molecules that contain two

functional groups: a basic NH2 amino group and an
acidic COOH carboxylic acid group.
R
OH
H
N
H
H
or
C
O
H2 N
COOH
The R-groups of the amino acids present in a

protein determine the proteins biological activity.
Chapter 23
Structures of Amino Acids
Chapter 23
Amino Acid
Visual Concept
Chapter 23
Amino Acids, continued

Amino Acid Reactions
Two amino acids can react with each other in an acidbase reaction.
The basic amino group of one amino acid reacts with
the acidic carboxylic acid group of another amino acid
to form a peptide, and a molecule of water is lost.
This reaction is classified as a condensation
reaction
The bond formed is called a peptide bond.
The product is a dipeptide.
Chapter 23
Formation of Dipeptides and Polypeptides

Visual Concept
Chapter 23

Amino Acid Reactions, continued
R
OH
H
N
OH
H
N
H
H
OH
+ H 2O
C
O
Chapter 23

Amino Acid Reactions
Longer chains of amino acids are called
polypeptides.
Chains of 50 or more amino acids are called
proteins.
Peptide bonds can be broken, or hydrolyzed, by
enzymes called proteases.
Chapter 23
Proteins
Proteins are the most complex and varied class of
biochemical molecules.
A protein is an organic biological polymer that is
made up of polypeptide chains of 50 or more amino
acids and is an important building block of all cells.
Proteins are made up of specific sequences of amino acids.
They have molecular masses that range from 6000 to more
milliondifferent
atomic protein
mass units.
than
About9 9000
molecules are found in
cells in the human body.
Chapter 23
Proteins
Visual Concept
Chapter 23
Proteins, continued
Nitrogen accounts for about 15% of the mass of a
protein molecule. Most proteins also contain sulfur.
Some contain phosphorus or other elements, such as
iron, zinc, and copper.
Proteins have many important catalytic, structural,
regulatory, and antibody defense functions.
Keratin is the main component of hair and fingernails.
Enzymes catalyze biochemical reactions.
Hemoglobin carries oxygen in the blood.
Insulin regulates glucose levels.
Antibodies protect the body from foreign substances.
Chapter 23
Proteins, continued
Arrangement of Amino Acids in Peptides and Proteins
Each peptide, polypeptide, or protein is made up of a
special sequence of amino acids.
A simple set of three-letter abbreviations is used to
represent each amino acid in these kinds of molecules.
The tripeptide made up of valine, asparagine, and histidine
would be written as ValAspHis.
Polypeptide and protein function depend not only on

the kinds and number of amino acids but also on
their order.
Chapter 23
Proteins, continued
Amino Acid Side-Chain Reactions
The properties of amino acidsand ultimately
polypeptides and proteinsdepend on the
properties of the side chains present.
The side chain of glutamic acid is acidic.
The side chain of histidine is basic.
The side chains of asparagine and several other amino
acids are polar.
Some amino acid side chains can form ionic or covalent
bonds with other side chains.
Chapter 23
Proteins, continued
Amino Acid Side-Chain Reactions, continued
Cysteine is a unique amino acid, because the SH
group in cysteine can form a covalent bond with
another cysteine side chain to form a disulfide bridge.
Chapter 23
Proteins, continued
Shape and Structure of Protein Molecules
The interaction of amino acid side chains determines
the shape and structure of proteins.
These are important to the proteins biological
functions.
In a polypeptide chain or protein, the sequence of the
amino acids is called the primary (1) structure.
The secondary (2) structure describes how the chain
is coiled or otherwise arranged in space.
Chapter 23
Proteins, continued
Shape and Structure of Protein Molecules, continued
Secondary structures form because hydrogen
bonding occurs between a hydrogen atom attached to
the nitrogen atom in one peptide bond and the
oxygen atom of another peptide bond farther down
the backbone of the protein.
The alpha () helix is a secondary structure that
resembles a coiled spring.
The beta () pleated sheet is a secondary
structure that has accordion-like folds.
Chapter 23
Proteins, continued
A proteins characteristic three-dimensional shape is
called its tertiary (3) structure.
Side-chain interactions at various positions along
the protein backbone cause the tertiary structure.
The side-chain interactions can include
hydrogen bonding
salt bridges
cysteine-cysteine disulfide bonds
hydrophobic interactions between nonpolar side chains
Chapter 23
Proteins, continued
Nonpolar side groups tend to be found in the interior
of the protein where contact with water is minimal.
Polar and ionic side chains tend to be on the protein
surface, where they are in contact with water.
In some proteins, different polypeptides, each of
which has its own 3 structure, come together.
In the case of hemoglobin, four different
polypeptides make up the quaternary (4)
structure.
Chapter 23
Levels of Protein Structure
Chapter 23
Proteins, continued
Biological Functions of Proteins
Chapter 23
Proteins, continued
Biological Functions of Proteins, continued
Fibrous proteins are insoluble in water and are long,
thin, and physically strong.
Fibrous proteins give strength and protection to structures in
living things.
Keratin has a secondary structure is almost entirely alpha
helical in shape.
Collagen is a triple helix of three intertwined alpha helices. It
found in bone and tendons.
Fibrin found in silk has a beta-pleated sheet structure.
Elastins in blood tissue, fibrins in blood clots, and myosins
found in muscle tissue are other kinds of fibrous proteins.
Chapter 23
Proteins, continued
Biological Functions of Proteins, continued
Globular proteins are generally soluble in water and are
twisted and folded into a globe-like shape.
Globular proteins regulate body functions, catalyze reactions,
and transport substances.
Insulin is a small protein of 51 amino acids in two polypeptide
chains.
Myoglobin transports oxygen in the muscles.
Hemoglobin transports oxygen in the blood.
Casein, found in milk and used for food. It contains
phosphorus, which is needed for bone growth.
Chapter 23
Proteins, continued
Amino Acid Substitution
A single substitution of one amino acid for another can
change the shape and function of a protein.
The genetic disease sickle cell anemia can happen
when glutamic acidis replaced by valine.
Chapter 23
Sickle Cell Anemia

Visual Concept
Chapter 23
Structures and Roles of Several Amino Acids
Chapter 23
Proteins as Enzymes
An enzyme is a protein that catalyzes a biochemical
reaction.
Enzymes make up the largest and most highly
specialized class of proteins.
Most enzymes are water-soluble, globular proteins.
The amino acid side chains and the three-dimensional
shape of enzymes play a very important role in the
enzymatic activity.
Chapter 23
Proteins as Enzymes, continued

An enzyme also does not change the amount of
product that is formed in a reaction; it only
decreases the time it takes to form the product.
Enzymes catalyze both decomposition and
synthesis reactions.
Enzymes are very efficient.
A single molecule of carbonic anhydrase can break down
36 million carbonic acid molecules in 1 minute.
Chapter 23

Enzyme Specificity
Enzymes are very specific and often catalyze just a
single reaction.
Enzymes act by binding to a specific substrate
molecule.
The shape of the enzyme is such that the substrate can
fit into the enzyme at a specific part of the enzyme
molecule, called the active site.
Chapter 23

Enzyme Specificity
The resulting compound is called the enzyme-substrate
complex.
This model of enzyme action is called the lock and key
model.
Chapter 23
Enzyme Mechanism
Chapter 23
Enzyme
Visual Concept
Chapter 23

Enzymes and Reaction Rates
The presence of an enzyme in a chemical reaction can
increase the rate of a reaction by a factor of up to 10 20.
Only collisions that have enough energy to overcome
the activation energy and have the proper orientation
change reactants into products.
Enzymes lower the activation energy by forming the
enzyme-substrate complex, which makes breaking
bonds in the reactants and forming new bonds in the
products easier.
Chapter 23
Activation Energy With and Without an Enzyme
Chapter 23

Temperature and Enzyme Activity
Enzymes typically have
maximum activity within
a relatively narrow range
of temperatures.
Enzymes in the human
body work optimally at
the normal body
temperature of 37C
(98.6F).
Chapter 23

Temperature and Enzyme Activity
High heat can denature, or alter, the shape of a protein,
which in turn alters the proteins function.
Denaturation is a change in a proteins characteristic
three-dimensional shape due to changes of its
secondary, tertiary, and quaternary structure.
example: cooking an egg
Chapter 23

pH and Enzyme Activity
The optimal pH for normal cell enzyme functions is
almost neutral, about 7.3 to 7.4.
Changes in pH can cause changes in protein structure
and shape.
Most enzymes become inactivated, or no longer work,
because of denaturation when the pH changes.
Chapter 23

pH and Enzyme Activity, continued
Pre-enzymes, inactive forms of protein-digesting
enzymes, become activated by the stomachs low pH
of 1.5 to 2.0. This prevents the active form of the
enzymes from digesting the stomach lining.
Pepsin is a stomach enzyme found in adults.
Chapter 23
Section 3 Metabolism
Preview
Lesson Starter
Objectives
ATP: Energy for the Cell
Energy Activities
Catabolism
Anabolism
Chapter 23
Lesson Starter
What do you think metabolism is?
How does your body obtain energy?
Metabolism consists of all chemical reactions that
occur within an organism.
Chapter 23
Objectives
Describe the role of ATP in cells.
Explain how energy is released by metabolic
reactions.
Summarize the relationship between anabolism and
catabolism.
Chapter 23
Metabolism is the sum of all the chemical processes

that occur in an organism.
Complex molecules are broken down into smaller
ones through catabolism.
Simple molecules are used to build bigger ones
through a process called anabolism.
A metabolic pathway is a series of linked chemical
reactions that occur within a cell and result in a
specific product.
Chapter 23
ATP: Energy for the Cell

Cells require energy to make the proteins,
carbohydrates, lipids, and nucleic acids that are
necessary for life.
The original source for almost all of the energy
needed by living systems is the sun.
Autotrophs, such as plants and photosynthetic
bacteria, use sunlight, water, and CO2 to make
carbon-containing biomolecules.
This process is called photosynthesis.
Chapter 23
Photosynthesis
Visual Concept
Chapter 23
ATP: Energy for the Cell, continued

Photosynthesis occurs in the cells of plants and
algae, within structures called chloroplasts.
Chloroplasts contain chlorophyll, an organic molecule
that absorbs solar energy.
This energy is captured immediately in the bonds of
two compounds, one of which is adenosine
triphosphate (ATP).
Chapter 23
Chlorophyll a and b
Visual Concept
Chapter 23
ATP: Energy for the Cell, continued

ATP is a high-energy molecule that plant cells use to
make carbohydrates.
The other compound, known as NADPH, is also used
in carbohydrate-forming reactions.
Living things, including most microorganisms, which
depend on plants or other animals for food, are called
heterotrophs.
Heterotrophs use the energy obtained in the breakdown of
complex molecules to drive chemical reactions in cells.
Chapter 23
Linking Photosynthesis and Respiration

Visual Concept
Chapter 23
ATP/ADP Cycle
Chapter 23
Energy Activities
The cycle between ATP and ADP, adenosine
diphosphate, is the primary energy exchange
mechanism in the body.
ATP is the molecule that serves to carry energy from
energy-storing molecules, carbohydrates, lipids, and
proteins to specific energy-requiring processes in
cells.
When ATP is hydrolyzed to ADP, energy is released to
power the cells activities.
Chapter 23
Comparing ADP and ATP

Chapter 23
Hydrolysis of ATP
Chapter 23
Catabolism
The energy that your body needs to maintain its
temperature and drive its biochemical reactions is
provided through catabolic processes.
Catabolism is the part of metabolism in which
complex compounds break down into simpler ones
and is accompanied by the release of energy.
First, enzymes break down the complex compounds
in foodcarbohydrates, fats, and proteinsinto
simpler molecules.
Chapter 23
Catabolic Pathways
Chapter 23
Catabolism, continued
Carbohydrate digestion begins in the mouth, where
the enzyme amylase in saliva begins to break down
polysaccharides.
Carbohydrates are broken down intoglucose and other
monosaccharides.
Digestion of fats occurs only in the small intestine.

Fats are broken down into fatty acids and glycerol.
Protein digestion begins in the stomach and is

completed in the small intestine.
Proteins are broken down into amino acids.
Chapter 23
Catabolism, continued
Once in the cells, glucose and other
monosaccharides, fatty acids, some amino acids, and
glycerol enter the mitochondria and feed into a
complex series of reactions called the citric acid
cycle, or Krebs cycle.
The citric acid cycle produces carbon dioxide and
other molecules, such as NADH and ATP.
This NADH and ATP then move through another set
of reactions to produce more ATP and water.
Chapter 23
Energy Yield in Aerobic Respiration

Visual Concept
Chapter 23
Anabolism
Cells use the simple molecules that result from the
breakdown of food to make larger, more complex
molecules.
Anabolic processes are the energy-consuming
pathways by which cells produce the molecules that
they need for sustaining life and for growth and repair.
The conversion of small biomolecules into larger ones
is called anabolism.
Chapter 23
Anabolism, continued
In an anabolic pathway, small precursor molecules
are converted into complex molecules, including
lipids, polysaccharides, proteins, and nucleic acids.
Energy from ATP and NADH is necessary for these
biosynthesis reactions to occur.
Catabolism and anabolism occur simultaneously.
ATP and NADH serve as chemical links between the
two processes.
Chapter 23
Anabolism, continued
One important anabolic pathway that is common to
animals, plants, fungi, and microorganisms is
gluconeogenesis.
Glucose is synthesized in this pathway from noncarbohydrate substances.
In mammals, glucose from the blood is a fuel source.
Chapter 23
Cellular Respiration
Chapter 23
Section 4 Nucleic Acids
Preview
Lesson Starter
Objectives
Nucleic Acid Structure
DNA: Deoxyribonucleic Acid
RNA: Ribonucleic Acid
Technology and Genetic Engineering
Chapter 23
Lesson Starter
To understand how DNA replicates itself and passes
genetic information to RNA to make proteins, it is
important to understand hydrogen bonding.
DNA does not duplicate itself by making an identical
DNA molecule.
It replicates by unfolding its two strands, which then
pair up with complementary nucleotides.
Each DNA molecule has one new strand and one
original strand that are complementary.
Chapter 23
Objectives
Describe the role of ATP in cells.
Explain how energy is released by metabolic
reactions.
Summarize the relationship between anabolism and
catabolism.
Chapter 23
Nucleic acids contain all of the genetic information of

an organism.
They are the means by which a living organism
stores and conveys instructional information for all of
its activities.
The two nucleic acids found in organisms are
deoxyribonucleic acid (DNA)
ribonucleic acid (RNA)
Chapter 23

A nucleic acid is an organic compound, either RNA
or DNA, whose molecules carry genetic information
and is made up of one or two chains of monomer
units called nucleotides.
A nucleotide molecule is composed of a five-carbon
sugar unit that is bonded to both a phosphate group
and a cyclic organic base containing nitrogen.
phosphatesugarphosphatesugar
base
base
Chapter 23
Nucleic Acid
Visual Concept
Chapter 23

The sugar unit in DNA is deoxyribose.
The sugar unit in RNA is ribose.
The five nitrogenous bases found in nucleic acids are
adenine (A), guanine (G), cytosine (C), thymine (T),
and uracil (U)
Adenine (A), guanine (G), and cytosine (C) are found in
both DNA and RNA.
Thymine (T) is found only in DNA.
Chapter 23
Examples of Nucleotides
Visual Concept
Chapter 23
Nitrogenous Bases of Nucleic Acids
Chapter 23
DNA: Deoxyribonucleic Acid

Every single instruction for all of the traits that you
have inherited and all of the life processes that occur
in your cells is contained in your DNA.
Human cells contain 46 relatively large DNA
molecules.
Each human cell contains about 2 m of DNA, which is
divided and packed into the cells 46 chromosomes.
Chapter 23
DNA Overview
Chapter 23
DNA: Deoxyribonucleic Acid, continued

DNA is a double helix. In this structure, two strands of
the sugar-phosphate backbone are wound around
each other, and the nitrogenous bases point inward.
The sequence of these nitrogenous bases along the
phosphate-sugar backbone in DNA forms the code
responsible for transferring genetic information.
Hydrogen bonding between pairs of AT (adeninethymine) or GC (guanine-cytosine) bases makes
the double helix stable.
Chapter 23
Structure of DNA
Chapter 23

Nitrogenous Base Pairs
In the DNA double helix, base pairing exists only
between AT and between CG.
The interaction between base pairs accounts for the
ability of DNA to replicate itself.
Combinations of the four-letter alphabet of A,T,G, and
C form the genes that define our heredity.
Each gene is a section of DNA that contains a specific
sequence of four bases (A,G,T, and C) and typically
contains about 1000 to 2000 base pairs.
Chapter 23
Hydrogen Bonding in DNA
Chapter 23
Gene
Visual Concept
Chapter 23

DNA Replication
The two strands of the double helix of DNA are not
identical.
A base on one strand is paired through hydrogen bonding to
its complementary base on the other strand.
Each time a cell divides, an exact copy of the DNA of

the parent cell is reproduced for the daughter cells.
The process by which an identical copy of the original
DNA is formed is called DNA replication.
Chapter 23
DNA Replication
Chapter 23
DNA Replication
Chapter 23
Ribonucleic Acid (RNA)

Chapter 23
RNA: Ribonucleic Acid
Molecules of RNA make up about 5% to 10% of the

mass of a cell.
RNA molecules are responsible for the synthesis of

proteins.
RNA differs from DNA in four basic ways:

1. the sugar unit in the backbone of RNA is ribose
rather than deoxyribose
2. RNA contains the base uracil, U, instead of
thymine, which occurs in DNA
Chapter 23
RNA: Ribonucleic Acid, continued

3. RNA is a single-stranded molecule rather than
a double-stranded helix like DNA
4. RNA molecules typically consist of 75 to a few
thousand nucleotide units rather than the
millions that exist in DNA.
It is not uncommon for up to 50% of an RNA

molecule to have a double-helix structure.
The base sequences along the helical regions of the

RNA strand are complementary.
Chapter 23
Comparing DNA and RNA

Visual Concept
Chapter 23

Synthesis of RNA
RNA is synthesized in the nucleus of the cell
DNA and protein molecules actually help
synthesize specific RNA molecules.
As RNA is synthesized, the information contained in
the DNA is transferred to the RNA molecules.
The genetic information of RNA is carried in its
nucleotide sequence.
Chapter 23

Synthesis of RNA, continued
One type of RNA molecule is called messenger RNA
(mRNA) because it carries the instructions for making
proteins out into the cytosol, where proteins are
produced on ribosomes.
A ribosome is a cell organelle that is composed of
RNA and protein. Ribosomes are the main site of
protein production in cells.
Chapter 23

The DNA template is also used to make two other types
of RNA molecules: ribosomal RNA (rRNA) and transfer
RNA (tRNA).
Both of these types of RNA also leave the nucleus and come
together in the ribosome where they help synthesize proteins.
Ribosomal RNA becomes part of the structure of the
ribosome.
Transfer RNA is used to transfer amino acids into the
ribosome.
Only mRNA carries the coded genetic information that is
translated into proteins.
Chapter 23
Types of RNA
Visual Concept
Chapter 23

The portion of DNA that holds the specific genetic
code for a single, specific mRNA molecule is a gene.
Each gene is typically a section of the DNA chain that
contains about 1000 to 2000 nucleotides.
A gene has the information necessary in this
sequence to direct RNA to produce several proteins
that have specific functions.
Chapter 23

RNA and Protein Synthesis
At a gene, a portion of DNA unwinds and RNA is
assembled using the same complementary base pairs
as DNA except that uracil replaces the thymine
As in DNA replication, the RNA sequence that forms
has the complementary base pairs of the DNA gene.
DNA strand: C C C C A C C C T A C G G T G
RNA strand: G G G G U G G G A U G C C A C
Chapter 23

A sequence of three bases in mRNA codes for a
specific amino acid.
The sequence CAG codes for glutamic acid.
The sequence GUC codes for valine.
There are 64 (43) unique combinations of threebase sequences made from four bases.
Because only 20 amino acids require codes, some
of the amino acids have more than one code.
Chapter 23

The genetic code is universal.
The stop signal in the gene is also a three-base
code: UAG, UAA, or UGA.
Chapter 23
Genetic Code
Chapter 23
Using the Genetic Code
Chapter 23
Technology and Genetic Engineering

Scientists in the field of genetic engineering study
how manipulation of an organisms genetic material
can modify the proteins that are produced and the
changes that result in the organism.
Today genetic engineering refers to recombinant DNA
technology that is used for cloning and the creation of
new forms of life.
Chapter 23
Genetic Engineering
Visual Concept
Chapter 23
Technology and Genetic Engineering, continued

DNA Fingerprinting
DNA is unique to an individual except for identical
twins.
This technology is used in criminal investigations,
paternity testing, and victim identification.
The technique of the polymerase chain reaction
(PCR) may be used to copy a DNA sample to supply
sufficient DNA for identification.
Chapter 23
DNA Fingerprint
Visual Concept
Chapter 23
Making a DNA Fingerprint

Visual Concept
Chapter 23
Polymerase Chain Reaction

Visual Concept
Chapter 23

Cloning
Cloning is the process of making an exact copy of an
organism.
Artificial cloning, using stem cells from animals or
meristem cells from plants, can produce identical
replicas of the parent cells or, under specialized
conditions, a complete organism that is identical to
the original organism.
Chapter 23
Cloning
Visual Concept
Chapter 23

Recombinant DNA Technology
Recombinant DNA technology has been used to
insert DNA from one organism into another.
The technique splices a gene from one organisms
DNA into a molecule of DNA from another organism.
When the spliced DNA is inserted into a cell, the cell
is able to make the protein that is coded by the
spliced gene.
Chapter 23
Using Plasmids to Produce Insulin

Visual Concept
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Modern Chemistry - Chapter 23

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Modern Chemistry - Chapter 23

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Chapter 23

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Biochemistry is the study of the chemicals and

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

A condensation reaction is a reaction in which two

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

They have hydrophilic polar heads, but their

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Phospholipids, are compound saponifiable lipids

Section 1 Carbohydrates and Lipids

Section 1 Carbohydrates and Lipids

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

condensation reaction to form dipeptide bond

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Amino acid molecules are the basic building blocks

Section 2 Amino Acids and Proteins

Amino acids are organic molecules that contain two

The R-groups of the amino acids present in a

Section 2 Amino Acids and Proteins

Structures of Amino Acids

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Amino Acids, continued

Section 2 Amino Acids and Proteins

Formation of Dipeptides and Polypeptides

Section 2 Amino Acids and Proteins

Amino Acids, continued

Section 2 Amino Acids and Proteins

Amino Acids, continued

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Polypeptide and protein function depend not only on

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Section 2 Amino Acids and Proteins

Levels of Protein Structure