Chapter 5

The Structure and Function of

Macromolecules
I. Macromolecules
 Polymer = large molecule made by covalently
linking together many monomers
 Monomers = individual building blocks
 Classes of polymers:
 Polysaccharides (carbohydrates)
 Polypeptides (proteins)

 Polynucleotides (nucleic acids: DNA & RNA)

Other macromolecules - not technically polymers

 Lipids (fats)
The Synthesis and Breakdown
of Polymers
 Condensation reaction – joins two monomers
with a covalent bond
 dehydration reaction (remove a water molecule)
 Hydrolysis - reverse of the dehydration reaction;
break two monomers apart by adding back a
water molecule

Animation: Polymers
LE 5-2

Short polymer Unlinked monomer

Dehydration removes a water

molecule, forming a new bond

Longer polymer
Dehydration reaction in the synthesis of a polymer

Hydrolysis adds a water

molecule, breaking a bond

Hydrolysis of a polymer
The Diversity of Polymers
1 2 3 H HO
 Each cell has thousands of different kinds of
macromolecules & macromolecules vary among
cells of an organism, within a species, and even
more between species
 An immense variety of polymers can be built from
a small set of monomers
II. Carbohydrates ~
fuel and building material
 Carbohydrates ~ sugars
and sugar polymers
 Monosaccharides =
single sugars
 Polysaccharides =
polymers composed of
many monosaccharide
building blocks

Animation: Organic Models

Monosaccharide Sugars
Monosaccharides: CH2O
 Ex: Glucose C6H12 O6
Monosaccharide characteristics:
1. Hydroxyl groups (-OH)

2. Carbonyl group (p. 70)

 Aldoses (aldehyde)
 Ketoses (ketone)
1. Linear or rings (in water)
2. Names end in “-ose”
 # C – triose, pentose, hexose
 Ex: glucose is a hexose & aldose monossacharide
Disaccharides
 Disaccharide = dehydration reaction joins two
monosaccharides
 Bond = glycosidic linkage
Polysaccharides
 Polysaccharides = polymers of
many monosaccharide sugars
 The structure and function
(storage or structural) of a
polysaccharide are determined
by its sugar monomers and
the positions of glycosidic
linkages

Animation: Carbohydrates
Storage Polysaccharides
 Starch = storage polysaccharide of plants
 α-glucose monomers
 1-4 linkages
 Helical
 Ex: amylose (unbranched) & amylopectin (branched)
 Plants store surplus starch as granules within
chloroplasts and other plastids
LE 5-6a
Chloroplast Starch

1 µm

Amylose Amylopectin

Starch: a plant polysaccharide

 Glycogen = storage polysaccharide in animals
 α-glucose
 1-4 linkages
 Helical
 MORE EXTENSIVE BRANCHING than starch
 Humans and other vertebrates store glycogen
mainly in liver and muscle cells
LE 5-6b
Mitochondria Glycogen granules

0.5 µm

Glycogen

Glycogen: an animal polysaccharide

Structural Polysaccharides
 Cellulose = component of plant cell walls
 Β-glucose
 1-4 linkages
 Straight chains, unbranched
 Grouped into microfibrils
 Humans cannot digest cellulose (“fiber”)
 Some microbes can (symbiosis in herbivores)
LE 5-8

Cellulose microfibrils
in a plant cell wall
Cell walls Microfibril

0.5 µm

Plant cells

Cellulose
molecules

β Glucose
monomer
 Chitin = structural polysaccharide found in:
 exoskeleton of arthropods
 cell walls of many fungi
 Glucose monomers with nitrogen appendages
III. Lipids

 Lipids - class of large biological molecules that do

not form polymers
 The unifying feature of lipids: hydrophobic
 consist mostly of hydrocarbons, which form nonpolar
covalent bonds
 The most biologically important lipids:
 Fats
 Phospholipids
 Steroids
Animation: Lipids
Fats
 Fat = triglyceride
 Glycerol = 3-carbon alcohol
 3 Fatty acids = carboxyl group attached to a long carbon
skeleton
 Joined by an Ester Linkage
 LE 5-11b

Ester linkage

Fat molecule (triacylglycerol or triglyceride)

 Fatty acids can vary in :
 length (# carbons)
 number and locations of
double bonds
 Saturated fatty acids =
no double bonds (max
# H); solid fats
 Unsaturated fatty acids
= one or more double
bonds; liquid oils

 The major function of

fats is energy storage
and protection (adipose)
 Phospholipids
 Phospholipid = two fatty acids and a phosphate
group are attached to glycerol
 Solubility:
 Hydrophilic Head = charged phosphate group
 Hydrophobic Tails = the two fatty acids
Phospholipids
 In water, they form a bilayer
 hydrophobic tails pointing toward the interior
 Similar to arrangement found in cell membranes
Steroids
 Steroids = lipids with four fused carbon rings
 Ex: Cholesterol ~ a component in animal cell
membranes
 Precursor for steroid hormones
IV. Nucleic Acids
 Nucleic acids = polymers called polynucleotides
 Monomers are nucleotides
 Nucleotide = a nitrogenous base, a pentose sugar, and a
phosphate group
 Nucleoside = portion of a nucleotide w/out phosphate group

Nucleotide
Nitrogenous Bases
Nitrogenous bases: Attached
to 1st C of sugar
 Two classes:
 Pyrimidines = 1 ring

 Cytosine (C), Thymine

(T), Uracil (U)
 Purines = 2 rings fused

 Adenine (A), Guanine (G)

• Base Pairing:
A – T (or U) and C – G
Pentose Sugar & Phosphate
• Deoxyribose (DNA) or Ribose (RNA)

• Phosphate – attached to 5’ C of sugar

Types of Polynucleotides
2 types of nucleic acids:
 Deoxyribonucleic acid (DNA)
 Unit of inheritance = gene
 Provides own directions for replication
 Ribonucleic acid (RNA)
 DNA directs synthesis of messenger RNA
(mRNA) and, through mRNA, controls protein
synthesis
DNA  RNA  protein

Phosphodiester linkage between nucleotides

between –OH group on the 3´ C of one
nucleotide and the phosphate on 5´ C on the
next
LE 5-25
DNA

Synthesis of
mRNA in the nucleus
mRNA

NUCLEUS
CYTOPLASM

mRNA
Movement of
mRNA into cytoplasm
Ribosome
via nuclear pore

Animation: Nucl
Synthesis
of protein

Amino
Polypeptide acids
Polynucleotides
(Nucleic Acids)
 DNA
 Genetic code
 Deoxyribose sugar
 Helical & double* stranded (antiparallel)
 Hydrogen bonds – hold 2 strands together
 RNA
 Ribose sugar
 Single* stranded
 Uracil instead of Thymine (bases)
Animation: DNA & RN
*usually 
 DNA and Evolution
 The linear sequences of nucleotides in DNA
molecules are passed from parents to offspring
 Two closely related species are more similar in
DNA than are more distantly related species
 Molecular biology can be used to assess
evolutionary kinship
 V. Proteins
 Proteins - more than 50% of
dry mass of cells
 Functions include:
 Enzymes
 Structural
 Storage
 Transport
 Hormonal (cellular
communication)
 Receptor Proteins in mouse cells
 Contractile (movement)
 Defensive Animation: Protein Functions
 Enzyme - protein that acts as a catalyst, speeding
up chemical reactions
Polypeptides

 Polypeptides = polymers of amino acids

 Protein = one or more polypeptides
 Monomers = Amino Acids ~ an asymmetric
carbon with:
 carboxyl group
 Amino group
 H atom
 R group (different side chains)
Amino Acids
 20 different amino acids
 Chemistry of side chain (R-group) determine
characteristics
 Nonpolar ~ hydrophobic
 Polar ~ hydrophilic
 Acidic (-) ~ hydrophilic
 Basic (+) ~ hydrophilic
Amino Acid Polymers
 Amino acids are linked by
peptide bonds to make a
polypeptide chain
 Conformation = the
unique 3-D shape
determined by the
sequence of amino acids
 A protein’s conformation
determines its function
Four Levels of Protein
Structure
 Primary ~ sequence of amino acids
 A gene codes for each sequence
 Secondary ~ repeated coils (α-helix) and/or folds
(β-pleated sheets) in the polypeptide chain
 Due to H-bonding along backbone
 Tertiary ~ irregular folding
 Due to side chain (R-group) interactions
 Ex: hydrophobic; disulfide bridges; H-bonds, ionic
 Quaternary ~ 2 or more polypeptide chains
interact to make a functional protein
 Ex: collagen and hemoglobin
Animation: Protein Structure
Sickle-Cell Disease
 A slight change in primary structure can affect a
protein’s conformation and ability to function
 Sickle-cell disease, an inherited blood disorder,
results from a single amino acid substitution in
the protein hemoglobin
LE 5-21b

Normal hemoglobin Sickle-cell hemoglobin

Primary Val His Leu Thr Pro Glu Glu Primary Val His Leu Thr Pro Val Glu
structure 1 2 3 4 5 6 7 structure 1 2 3 4 5 6 7
Exposed
Secondary Secondary hydrophobic
and tertiary β subunit and tertiary region β subunit
structures structures

β α
α
β
Quaternary Normal Quaternary Sickle-cell
structure hemoglobin structure hemoglobin α
(top view) β
β α

Function Molecules do Function Molecules

not associate interact with
with one one another to
another; each crystallize into
carries oxygen. a fiber; capacity
to carry oxygen
is greatly reduced.
What Determines Protein
Conformation?
 Physical and chemical conditions can affect
conformation
 Alternations in pH, salt concentration,
temperature, or other environmental factors can
cause a protein to unravel, or denature, and
become biologically inactive
 Denaturation = loss of a protein’s native
conformation due to disrupted secondary, tertiary
and quaternary structure
 PRIMARY STRUCTURE IS STILL INTACT
 can fold into correct conformation in right environment
 LE 5-22

Denaturation

Normal protein Denatured protein

Renaturation
 LE 5-4

Linear and Abbreviated ring

ring forms structure
 LE 5-17a

Glycine (Gly) Alanine (Ala) Valine (Val) Leucine (Leu) Isoleucine (Ile)

Nonpolar

Methionine (Met) Phenylalanine (Phe) Tryptophan (Trp) Proline (Pro)

 LE 5-17b

Polar

Serine (Ser) Threonine (Thr) Cysteine (Cys) Tyrosine (Tyr) Asparagine (Asn) Glutamine (Gln)
 LE 5-17c

Acidic Basic

Electrically
charged

Aspartic acid (Asp) Glutamic acid (Glu) Lysine (Lys) Arginine (Arg) Histidine (His)
LE 5-20a

Amino end Amino acid

subunits

Carboxyl end
 LE 5-20b

β pleated sheet

Amino acid
subunits

α helix
LE 5-20d

Hydrophobic
interactions and
van der Waals
interactions
Polypeptide
backbone
Hydrogen
bond

Disulfide bridge

Ionic bond
LE 5-20e

Polypeptide
chain β Chains

Iron
Heme

α Chains
Polypeptide chain Collagen Hemoglobin