Bio Macro Molecules

Chapter
3
The Molecules of Life
PowerPoint® Lectures created by Edward J. Zalisko for

Campbell Essential Biology, Sixth Edition, and
Campbell Essential Biology with Physiology, Fifth Edition
– Eric J. Simon, Jean L. Dickey, Kelly A. Hogan, and Jane B. Reece © 2016 Pearson Education, Inc.
Organic Compounds
• A cell is mostly water.

• The rest of the cell consists mainly of carbon-based
molecules.
• Carbon forms large, complex, and diverse
molecules necessary for life’s functions.
• Organic compounds are carbon-based
molecules.
© 2016 Pearson Education, Inc.

Carbon: The Central Atom
• Carbon atoms participate in four covalent bonds.
– Has four electrons in the outer energy level
– Can make double bonds with oxygen
– Can double or triple bonds with other carbon atoms

Figure 3.1
Double bond
Carbon skeletons vary in length Carbon skeletons may
have double bonds,
which can vary in location
Carbon skeletons may be Carbon skeletons may

unbranched or branched be arranged in rings
Figure 3.2
Structural formula Ball-and-stick model Space-filling model

Figure 3.3
Octane Dietary fat

Functional
Groups

Isomers

Isomers
Organic molecules can have the same number and

composition of atoms, but can have different
arrangements.
These are called isomers.

Molecules with the same empirical formula but
different structural formulas

Hexose Isomers

Carbon Chemistry
• Carbon is a versatile molecule.

• Carbon can share electrons with other atoms in four
covalent bonds.
• Because carbon can use one or more of its bonds to
attach to other carbon atoms, it is possible to
construct an endless diversity of carbon skeletons
varying in
• size and
• branching pattern.

Carbon Chemistry
• The carbon atoms of organic compounds can also

bond with other elements, most commonly
• hydrogen,
• oxygen, and
• nitrogen.

Carbon Chemistry
• One of the simplest organic compounds is

methane, CH4, with a single carbon atom bonded
to four hydrogen atoms.
• Methane is abundant in natural gas and is
produced
• by prokaryotes that live in swamps (i.e., swamp gas)
and
• in the digestive tracts of grazing animals, such as
cows.

Carbon Chemistry
• Larger organic compounds

• are the main molecules in the gasoline we burn in
cars and other machines and
• are important fuels in your body.
• The energy-rich parts of fat molecules have a

structure similar to gasoline.

Carbon Chemistry
• The unique properties of an organic compound

depend on
• its carbon skeleton and
• the atoms attached to the skeleton.

Carbon Chemistry
• In an organic compound, the groups of atoms

directly involved in chemical reactions are called
functional groups.
• Each functional group plays a particular role during
chemical reactions.
• Many biological molecules have two or more
functional groups.

Large Biological Molecules
• There are four categories of large biological

molecules found in all living creatures:
1. carbohydrates,
2. lipids,
3. proteins, and
4. nucleic acids.

OH H
Short polymer Monomer
Dehydration
H2O
reaction
Longer polymer
(a) Building a polymer chain
Figure 3.4-1

H2O
Hydrolysis
OH H
(b) Breaking a polymer chain
Figure 3.4-2

Giant Molecules from Smaller Building Blocks
• Macromolecules are polymers.

• Polymers are made by stringing together many
smaller molecules called monomers.
• A dehydration reaction
• links two monomers together and
• removes a molecule of water.

• Organisms also have to break down

macromolecules.
• Digestion breaks down macromolecules to make
monomers available to your cells.

• Hydrolysis
• breaks bonds between monomers,
• adds a molecule of water, and
• reverses the dehydration reaction.

Carbohydrates
• Organic molecules composed of carbon, hydrogen and

oxygen
• All have the general formula CH2O
• Names end in –ose
• Serve as the primary energy source for most living things
• Also serve as structural support
– Plant cell walls
• Important components of nucleic acids
– DNA and RNA
3-23
Figure 3.5-1
Mono-
saccharides
Glucose Fructose
C6H12O6 C6H12O6
Isomers
(same formula, different arrangements)
Figure 3.6
(a) Linear and ring structures (b) Abbreviated ring

structure

Figure 3.7-1
OH H
Glucose Galactose
H2O
Lactose
Polymers
3-27
Figure 3.9
Starch granules
in potato tuber cells
(a) Starch
Glucose
Glycogen granules monomer
in muscle
tissue
(b) Glycogen
Cellulose microfibrils
(c) Cellulose
in a plant cell wall
Cellulose
molecules
Hydrogen bonds

Carbohydrates
• Carbohydrates include sugars and polymers of

sugar. Examples are
• small sugar molecules in soft drinks and
• long starch molecules in spaghetti and bread.

Carbohydrates
• In animals, carbohydrates are

• a primary source of dietary energy and
• raw material for manufacturing other kinds of
organic compounds.
• In plants, carbohydrates serve as a building

material for much of the plant body.

Monosaccharides
• Monosaccharides
• are the monomers of carbohydrates and
• cannot be broken down into smaller sugars.
• Common examples are glucose in sports drinks

and fructose found in fruit.
• Both of these simple sugars are also in honey.

Monosaccharides
• Glucose and fructose are isomers, molecules that

have the same molecular formula but different
structures.

Monosaccharides
• Monosaccharides, particularly glucose, are the

main fuels for cellular work.
• In water, many monosaccharides form rings.

Disaccharides
• A disaccharide is a double sugar constructed from

two monosaccharides by a dehydration reaction.

Disaccharides
• Disaccharides include
• lactose in milk, made from the monosaccharides
glucose and galactose,
• maltose in beer, malted milk shakes, and malted
milk ball candy, and
• sucrose in table sugar.

Disaccharides
• Sucrose is the main carbohydrate in plant sap.

• High-fructose corn syrup (HFCS) is made by a
commercial process that converts natural glucose
in corn syrup to much sweeter fructose.
• HFCS is often one of the first ingredients listed in
soft drinks.

Polysaccharides
• Polysaccharides
• are complex carbohydrates and
• are made of long chains of sugars—polymers of
monosaccharides.

Polysaccharides
• Starch
• is a familiar example of a polysaccharide,
• consists of long strings of glucose monomers, and
• is used by plant cells to store energy.
• Potatoes and grains are major sources of starch in

our diet.

Polysaccharides
• Glycogen
• is used by animal cells to store energy and
• is broken down to release glucose when you need
energy.

Polysaccharides
• Cellulose
• is the most abundant organic compound on Earth,
• forms cable-like fibrils in the walls that enclose plant
cells, and
• cannot be broken by any enzyme produced by
animals.

• The average American consumes about 45 kg of
sugar (about 100 lb) per year, mainly as sucrose
and high-fructose corn syrup.
• Sugar
• is a major cause of tooth decay, and
• Overconsumption increases the risk of developing
type 2 diabetes and heart disease.

Large Biological Molecules
• There are four categories of large biological

molecules found in all living creatures:
1. carbohydrates,
2. lipids,
3. proteins, and
4. nucleic acids.

Figure 3.11-1
H HO
Fatty acid
H2O
Glycerol
(a) A dehydration reaction linking a fatty acid to glycerol

True (neutral) Fats
• Used to provide energy

• The building blocks of
fats
– A glycerol molecule
– Three fatty acids
3-44
Figure 3.11-2
(b) A fat molecule with a glycerol “head” and three

energy-rich hydrocarbon fatty acid “tails”

Saturated and Unsaturated
Fatty Acids
3-46
Phospholipids
• Are complex organic

molecules that resemble
fats but contain
phosphate groups
• Phospholipids are the

major components of
cell membranes.
3-47
Steroids

Figure 3.13
Cholesterol can be converted

by the body to
Testosterone A type of estrogen

Steroids

Figure 3.12
TYPES OF FATS
Saturated Fats Unsaturated Fats
Margarine
Plant oils Trans fats Omega-3 fats

Lipids
• Almost all carbohydrates are hydrophilic (“water-

loving”) molecules that dissolve readily in water.
• Lipids are hydrophobic, unable to mix with water.
• When you combine oil and vinegar, the oil, which is
a type of lipid, separates from the vinegar, which is
mostly water.

Lipids
• Lipids also differ from carbohydrates, proteins, and

nucleic acids in that they are neither huge
macromolecules nor are they necessarily polymers
built from repeating monomers.
• Lipids are a diverse group of molecules made from
different molecular building blocks.

Fats
• A typical fat, or triglyceride, consists of a glycerol

molecule joined with three fatty acid molecules via
a dehydration reaction.

Fats
• Fats perform essential functions in the human body

including
• energy storage,
• cushioning, and
• insulation.

Fats
• If the carbon skeleton of a fatty acid has fewer than

the maximum number of hydrogens at the double
bond, it is unsaturated.
• If it has the maximum number of hydrogens,
it is saturated.
• A saturated fat has all three of its fatty acids
saturated.

Fats
• Most animal fats

• have a relatively high proportion of saturated fatty
acids,
• can easily stack, tending to be solid at room
temperature, and
• contribute to atherosclerosis, in which lipid-
containing plaques build up along the inside walls of
blood vessels.

Fats
• Most plant and fish fats tend to be

• high in unsaturated fatty acids and
• liquid at room temperature.

Fats
• Hydrogenation
• adds hydrogen,
• converts unsaturated fats to saturated fats,
• makes liquid fats solid at room temperature, and
• creates trans fats, a type of unsaturated fat that is
particularly bad for your health.

Steroids
• Steroids are very different from fats in structure

and function.
• The carbon skeleton has four fused rings.
• Steroids vary in the functional groups attached to
this set of rings, and these chemical variations affect
their function.

Steroids
• Cholesterol is
• a key component of cell membranes and
• the “base steroid” from which your body produces
other steroids, such as estrogen and testosterone.

Steroids
• Synthetic anabolic steroids

• are variants of testosterone,
• mimic some of its effects,
• may be prescribed to treat diseases such as cancer
and AIDS,
• are abused by athletes to build up their muscles
quickly, and
• can cause serious physical and mental problems.

Steroids
• Most athletic organizations ban the use of anabolic

steroids because of their many potential health
hazards coupled with the unfairness of an artificial
advantage.

Proteins
• Proteins
• are polymers of amino acid monomers,
• account for more than 50% of the dry weight of most
cells, and
• are instrumental in almost everything cells do.

Figure 3.15
MAJOR TYPES OF PROTEINS

Structural Proteins Storage Proteins Contractile Transport Proteins Enzymes
(provide support) (provide amino Proteins (help transport (help chemical
acids for growth) (help movement) substances) reactions)

Examples of Protein structures

Structural Proteins: provide support
Storage Proteins: provide amino acids for growth
Contractile Proteins: help movement
Transport Proteins: help transport substances
Enzymes: help chemical reactions

Figure 3.16-1
Amino Carboxyl
group group
Side
chain
(a) The general structure of an amino acid

The Monomers of Proteins: Amino Acids
• All proteins are made by stringing together a

common set of 20 kinds of amino acids.
• Every amino acid consists of a central carbon
atom bonded to four covalent partners.

• Three of those attachment groups are common to

all amino acids:
1. a carboxyl group (COOH),
2. an amino group (NH2), and
3. a hydrogen atom.
• The variable component of amino acids

• is called the side chain and
• is attached to the fourth bond of the central carbon.

• Each type of amino acid has a unique side chain,

which gives that amino acid its special chemical
properties.

Figure 3.16-2
Hydrophobic Hydrophilic
side chain side chain
Leucine Serine
(b) Examples of amino acids with hydrophobic and hydrophilic
side chains

Structure/Function: Protein Shape
• Cells link amino acids together by dehydration

reactions,
• forming peptide bonds, and
• creating long chains of amino acids called
polypeptides.
• A functional protein is one or more polypeptide

chains precisely twisted, folded, and coiled into a
molecule of unique shape.

Figure 3.17-s1
Carboxyl Amino
group group
OH H
Side Side
chain chain
Amino acid Amino acid

Figure 3.17-s2
Carboxyl Amino
group group
OH H
Side Side
chain chain
Amino acid Amino acid
Dehydration reaction
H2O
Side Side
chain chain
Peptide bond
Figure 3.4-3

Denaturation of a Protein

Form and Function
• The protein’s overall shape
determines its job.
• If a protein is not shaped
properly, it likely will not work
properly.
• Example:
– Sickle cell anemia
– A mutation in the gene
causes the protein to have a
different shape.
– This shape change results
in a change in function.
• Denaturation:
– When heat or other
environmental conditions
break the bonds that
stabilize tertiary structure.
3-86
• How is it possible to make the huge variety of

proteins found in your body from just 20 kinds of
amino acids?
• Like the English alphabet used to make different
words by varying the sequent of just 26 letters,
proteins use 20 different “letters” (amino acids) to
create polypeptides hundreds or thousands of
amino acids in length.

• The amino acid sequence of each polypeptide

determines the three-dimensional structure of the
protein.
• A protein’s three-dimensional structure enables the
molecule to carry out its specific function.
• Nearly all proteins work by recognizing and binding
to some other molecule.

Figure 3.21
Gene
DNA
Nucleic
acids
RNA
Amino acid
Protein
Primary Structure
• The sequence of amino acids in a polypeptide constitutes

the primary structure of the protein.
• This sequence is dictated by information in genes (DNA).
• All levels of protein structure depend on the primary
sequence.
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
3-91
ALPHA HELIX

BETA STRAND and BETA SHEET

Secondary Structure
• Polypeptides twist and fold into
their secondary structure.
– Some sequences of amino
acids twist into a helix.
• This is called an alpha
helix.
– Some sequences of amino
acids remain straight and
fold back on themselves.
• This is called a beta-
pleated sheet.
3-94
Myoglobin: An example of a tertiary structure

Myoglobin: An example of a tertiary structure

Figure 3.18
One amino acid

(alanine)
1
Here you can see how the polypeptide
folds into a compact shape.
129
The amino acid sequence of lysozyme
This model allows you to see the details

of the protein’s structure.

Tertiary Structure
• The various alpha helices
and beta pleated sheets
interact to form a globular
structure.
• This globular structure is
unique for each
polypeptide.
3-98
A computer simulated pathway of folding of villin protein (36AA long polypeptide)

Form and Function
Sickle cell anemia

Figure 3.19
SEM
Amino acid sequence Normal peptide Normal red
blood cell
(a) Normal hemoglobin
SEM
Amino acid sequence Sickle-cell Sickled red
polypeptide blood cell
(b) Sickle-cell hemoglobin
Diseases of Protein Folding
• Mad Cow Disease: Prion

Protein misfolding
• Alzheimer’s Disease:
Amyloid Beta Protein
• Cystic Fibrosis: CFTR Phe

deletion mutation
• Parkinson’s Disease:
misfolding of alpha-synuclein

Figure 3.20
Normal
protein
Prion
Clusters
of prions
Skull
Prion Prion
converts proteins
Brain normal clump
proteins together
Bovine spongiform Kuru Fatal weight loss in

encephalopathy deer, elk, and moose
(BSE)
Prions

Prions

• A slight change in the amino acid sequence can

affect a protein’s ability to function.
• The substitution of one amino acid for another at a
particular position in hemoglobin, the blood protein
that carries oxygen, causes sickle-cell disease, an
inherited blood disorder.

• A protein’s shape is sensitive to the environment.

An unfavorable change in temperature, pH, or
some other factor can cause a protein to unravel.

• One difference in sequence is enough to cause the

protein to fold into a different shape, which alters its
function, which in turn causes disease.
• Misfolded proteins are associated with many
diseases, including some severe nervous system
disorders.
• The diseases shown in Figure 3.20 are all caused
by prions, misfolded versions of normal brain
proteins.

•
Proteins
are polymers of amino acid monomers,
• account for more than 50% of the dry weight of most cells, and
• are instrumental in almost everything cells do.
• All proteins are made by stringing together a common set of 20 kinds of amino
acids.
• Every amino acid consists of a central carbon atom bonded to four covalent
partners.
• Three of those attachment groups are common to all amino acids:
1. a carboxyl group (COOH),
2. an amino group (NH2), and
3. a hydrogen atom.
©
• The variable component of amino acids
2016
Pear • is called the side chain and
son • is attached to the fourth bond of the central carbon.
Edu • Each type of amino acid has a unique side chain, which gives that amino acid
cati its special chemical properties.
on,
Inc.
• Cells link amino acids together by dehydration reactions,
– forming peptide bonds, and
– creating long chains of amino acids called polypeptides.
• A functional protein is one or more polypeptide chains precisely twisted, folded, and
coiled into a molecule of unique shape.
• How is it possible to make the huge variety of proteins found in your body from just 20
kinds of amino acids?
• Like the English alphabet used to make different words by varying the sequence of
just 26 letters, proteins use 20 different “letters” (amino acids) to create
polypeptides hundreds or thousands of amino acids in length.
• The amino acid sequence of each polypeptide determines the three-dimensional

structure of the protein.
• A protein’s three-dimensional structure enables the molecule to carry out its specific
function.
• Nearly all proteins work by recognizing and binding to some other molecule.

• A slight change in the amino acid sequence can affect a protein’s ability to
function.
• The substitution of one amino acid for another at a particular position in
hemoglobin, the blood protein that carries oxygen, causes sickle-cell disease,
an inherited blood disorder.
• A protein’s shape is sensitive to the environment. An unfavorable change in
temperature, pH, or some other factor can cause a protein to unravel.
• One difference in sequence is enough to cause the protein to fold into a

© different shape, which alters its function, which in turn causes disease.
2016
Pear • Misfolded proteins are associated with many diseases, including some severe
son nervous system disorders.
Edu
cati
on,
Inc.
The Functions of DNA
3-
114 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Nucleic Acids
• Nucleic acids are macromolecules that

• store information and
• provide the instructions for building proteins.
• They consist of two types:

1. DNA (deoxyribonucleic acid) and
2. RNA (ribonucleic acid).

Nucleic Acids
• The genetic material that humans and all other

organisms inherit from their parents consists of
giant molecules of DNA.
• The DNA resides in the cell as one or more very
long fibers called chromosomes.

Nucleic Acids
• A gene is a unit of inheritance encoded in a

specific stretch of DNA that programs the amino
acid sequence of a polypeptide.
• Those programmed instructions are written in a
chemical code that must be translated
• from “nucleic acid language”
• to “protein language.”

Nucleic Acids
• Nucleic acids are polymers made from monomers

called nucleotides.
• Each nucleotide has three parts:
1. a five-carbon sugar,
2. a phosphate group, and
3. a nitrogen-containing base.

Figure 3.22
Nitrogenous base
(can be A, G, C, or T)
Connection
to the next
nucleotide
in the chain
Thymine (T)
Phosphate
group Phosphate
Base
Sugar
Connection to the (deoxyribose)
next nucleotide in Sugar
the chain
(a) Atomic structure (b) Symbol used in this book

Components of Nucleotides
5-carbon sugar
DNA RNA
Components of Nucleotides
Nitrogenous
base * *
T
A DNA
G
RNA
Nitrogen attaches
* with sugar molecule
C U
Sugar-phosphate
backbone
Base
Nucleotide pair
Hydrogen
bond
Bases
(b) Double helix

(a) DNA strand (two polynucleotide strands)
(polynucleotide) Space-filling model of DNA
Nucleic Acids
• Each DNA nucleotide has one of four possible

nitrogenous bases:
1. adenine (A),
2. guanine (G),
3. thymine (T), or
4. cytosine (C).

Figure 3.23
Adenine (A)
Guanine (G)
Thymine (T)
Adenine (A) Guanine (G) Cytosine (C)
Thymine (T) Cytosine (C) Space-filling model of DNA

Figure 3.23-1
Adenine (A) Guanine (G)
Thymine (T) Cytosine (C)

Nucleic Acids
• Dehydration reactions
• link nucleotide monomers into long chains called
polynucleotides,
• form covalent bonds between the sugar of one
nucleotide and the phosphate of the next, and
• form a sugar-phosphate backbone.
• Bases (A, T, C, or G) hang off the backbone like

appendages.

Figure 3.24
Sugar-phosphate
backbone
Base
Nucleotide pair
Hydrogen
bond
Bases
(a) DNA strand (b) Double helix

(polynucleotide) (two polynucleotide strands)
Nucleic Acids
• A molecule of cellular DNA is double-stranded, with

two polynucleotide strands coiled around each other
to form a double helix.
• Bases along one DNA strand hydrogen-bond to
bases along the other strand.
• The functional groups hanging off the base
determine which bases pair up:
• A only pairs with T and
• G can only pair with C.

The Structure of DNA
3-
129 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Nucleic Acids
• There are many similarities between DNA and

RNA.
• Both are polymers of nucleotides and
• both are made of nucleotides consisting of
• a sugar,
• a phosphate, and
• a base.

Nucleic Acids
• There are three important differences between

DNA and RNA.
1. As its name ribonucleic acid denotes, the RNA
sugar is ribose rather than deoxyribose in DNA.
2. Instead of the base thymine, RNA has a similar
but distinct base called uracil (U).
3. RNA is usually found in single-stranded form,
whereas DNA usually exists as a double helix.

Figure 3.UN02a
Carbohydrates
Functions Components Examples
Monosaccharides:
glucose, fructose;
Dietary energy; disaccharides:
storage; plant lactose, sucrose;
structure polysaccharides:
starch, cellulose
Monosaccharide

Figure 3.UN02b
Lipids
Long-term
Fatty acid
Fats (triglycerides);
energy storage
steroids
(fats);
Glycerol (testosterone,
hormones
Components of estrogen)
(steroids)
a triglyceride

Figure 3.UN02c
Proteins
Amino Carboxyl
group group
Lactase
Enzymes, structure,
(an enzyme);
storage, contraction,
hemoglobin
transport, etc. Side (a transport protein)
chain
Amino acid

Figure 3.UN02d
Nucleic acids
Phosphate
Base
Information
storage DNA, RNA
Sugar
Nucleotide

Figure 3.UN02
Large Biological Functions Components Examples
Molecules
Monosaccharides:
glucose, fructose;
Dietary energy;
disaccharides:
Carbohydrates storage; plant
lactose, sucrose;
structure
polysaccharides:
starch, cellulose
Monosaccharide
Long-term
Fats (triglycerides);
energy storage Fatty acid
steroids
Lipids (fats);
Glycerol (testosterone,
hormones
Components of estrogen)
(steroids)
a triglyceride
Amino Carboxyl
group group
Lactase
Enzymes, structure,
(an enzyme);
Proteins storage, contraction,
hemoglobin
transport, etc. Side (a transport protein)
chain
Amino acid
Phosphate
Base
Information
Nucleic acids storage DNA, RNA
Sugar
Nucleotide

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Chapter

PowerPoint® Lectures created by Edward J. Zalisko for

• A cell is mostly water.

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

Carbon skeletons may be Carbon skeletons may

Structural formula Ball-and-stick model Space-filling model

© 2016 Pearson Education, Inc.

Octane Dietary fat

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

Organic molecules can have the same number and

These are called isomers.

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

• Carbon is a versatile molecule.

© 2016 Pearson Education, Inc.

• The carbon atoms of organic compounds can also

© 2016 Pearson Education, Inc.

• One of the simplest organic compounds is

© 2016 Pearson Education, Inc.

• Larger organic compounds

• The energy-rich parts of fat molecules have a

© 2016 Pearson Education, Inc.

• The unique properties of an organic compound

© 2016 Pearson Education, Inc.

• In an organic compound, the groups of atoms

© 2016 Pearson Education, Inc.

• There are four categories of large biological

© 2016 Pearson Education, Inc.

Short polymer Monomer

© 2016 Pearson Education, Inc.

(b) Breaking a polymer chain

© 2016 Pearson Education, Inc.

• Macromolecules are polymers.

© 2016 Pearson Education, Inc.

• Organisms also have to break down

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

• Organic molecules composed of carbon, hydrogen and

(a) Linear and ring structures (b) Abbreviated ring

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

• Carbohydrates include sugars and polymers of

© 2016 Pearson Education, Inc.

• In animals, carbohydrates are

• In plants, carbohydrates serve as a building

© 2016 Pearson Education, Inc.

• Common examples are glucose in sports drinks

© 2016 Pearson Education, Inc.

• Glucose and fructose are isomers, molecules that

© 2016 Pearson Education, Inc.

• Monosaccharides, particularly glucose, are the

© 2016 Pearson Education, Inc.

• A disaccharide is a double sugar constructed from

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

• Sucrose is the main carbohydrate in plant sap.

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.

• Potatoes and grains are major sources of starch in

© 2016 Pearson Education, Inc.

© 2016 Pearson Education, Inc.