Chapter 5
The Structure and Function of
Large Biological Molecules
PowerPoint® Lecture Presentations for
Biology
Eighth Edition
Neil Campbell and Jane Reece
Lectures by Chris Romero, updated by Erin Barley with contributions from Joan Sharp
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Concept 5.4: Proteins have many structures,
resulting in a wide range of functions
• Proteins account for more than 50% of the dry
mass of most cells
• Protein functions include structural support,
storage, transport, cellular communications,
movement, and defense against foreign
substances
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Table 5-1
• Enzymes are a type of protein that acts as a
catalyst to speed up chemical reactions
• Enzymes can perform their functions
repeatedly, functioning as workhorses that
carry out the processes of life
Animation: Enzymes
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Fig. 5-16
Substrate
(sucrose)
Glucose
Enzyme
(sucrase)
OH
H2O
Fructose
HO
Polypeptides
• Polypeptides are polymers built from the
same set of 20 amino acids
• A protein consists of one or more polypeptides
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Amino Acid Monomers
• Amino acids are organic molecules with
carboxyl and amino groups
• Amino acids differ in their properties due to
differing side chains, called R groups
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Fig. 5-UN1
carbon
Amino Carboxyl
group group
Fig. 5-17
Nonpolar
Glycine Alanine Valine Leucine Isoleucine
(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)
Methionine Phenylalanine Trypotphan Proline
(Met or M) (Phe or F) (Trp or W) (Pro or P)
Polar
Serine Threonine Cysteine Tyrosine Asparagine Glutamine
(Ser or S) (Thr or T) (Cys or C) (Tyr or Y) (Asn or N) (Gln or Q)
Electrically
charged
Acidic Basic
Aspartic acid Glutamic acid Lysine Arginine Histidine
(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)
Fig. 5-17a
Nonpolar
Glycine Alanine Valine Leucine Isoleucine
(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)
Methionine Phenylalanine Tryptophan Proline
(Met or M) (Phe or F) (Trp or W) (Pro or P)
Fig. 5-17b
Polar
Serine Threonine Cysteine Tyrosine Asparagine Glutamine
(Ser or S) (Thr or T) (Cys or C) (Tyr or Y) (Asn or N) (Gln or Q)
Fig. 5-17c
Electrically
charged
Acidic Basic
Aspartic acid Glutamic acid Lysine Arginine Histidine
(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)
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 to
more than a thousand monomers
• Each polypeptide has a unique linear sequence
of amino acids
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Fig. 5-18
Peptide
bond
(a)
Side chains
Peptide
bond
Backbone
Amino end Carboxyl end
(b) (N-terminus) (C-terminus)
Protein Structure and Function
• A functional protein consists of one or more
polypeptides twisted, folded, and coiled into a
unique shape
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Fig. 5-19
Groove
Groove
(a) A ribbon model of lysozyme (b) A space-filling model of lysozyme
Fig. 5-19a
Groove
(a) A ribbon model of lysozyme
Fig. 5-19b
Groove
(b) A space-filling model of lysozyme
• The sequence of amino acids determines a
protein’s three-dimensional structure
• A protein’s structure determines its function
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Fig. 5-20
Antibody protein Protein from flu virus
Four Levels of Protein Structure
• The primary structure of a protein is its unique
sequence of amino acids
• Secondary structure, found in most proteins,
consists of coils and folds in the polypeptide
chain
• Tertiary structure is determined by interactions
among various side chains (R groups)
• Quaternary structure results when a protein
consists of multiple polypeptide chains
Animation: Protein Structure Introduction
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
• Primary structure, the sequence of amino
acids in a protein, is like the order of letters in a
long word
• Primary structure is determined by inherited
genetic information
Animation: Primary Protein Structure
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-21
Primary Secondary Tertiary Quaternary
Structure Structure Structure Structure
pleated sheet
+H
3N
Amino end
Examples of
amino acid
subunits
helix
Fig. 5-21a
Primary Structure
1
+H N 5
3
Amino end
10
15 Amino acid
subunits
20
25
Fig. 5-21b 1
+H
5
3N
Amino end
10
15 Amino acid
subunits
20
25
75
80
85 90
95
105
100
110
115
120
125
Carboxyl end
• The coils and folds of secondary structure
result from hydrogen bonds between repeating
constituents of the polypeptide backbone
• Typical secondary structures are a coil called
an helix and a folded structure called a
pleated sheet
Animation: Secondary Protein Structure
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Fig. 5-21c
Secondary Structure
pleated sheet
Examples of
amino acid
subunits
helix
Fig. 5-21d
Abdominal glands of the
spider secrete silk fibers
made of a structural protein
containing pleated sheets.
The radiating strands, made
of dry silk fibers, maintain
the shape of the web.
The spiral strands (capture
strands) are elastic, stretching
in response to wind, rain,
and the touch of insects.
• Tertiary structure is determined by
interactions between R groups, rather than
interactions between backbone constituents
• These interactions between R groups include
hydrogen bonds, ionic bonds, hydrophobic
interactions, and van der Waals interactions
• Strong covalent bonds called disulfide
bridges may reinforce the protein’s structure
Animation: Tertiary Protein Structure
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-21e
Tertiary Structure Quaternary Structure
Fig. 5-21f
Hydrophobic
interactions and
van der Waals
interactions
Polypeptide
backbone
Hydrogen
bond
Disulfide bridge
Ionic bond
Fig. 5-21g
Polypeptide Chains
chain
Iron
Heme
Chains
Hemoglobin
Collagen
• Quaternary structure results when two or
more polypeptide chains form one
macromolecule
• 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 beta
chains
Animation: Quaternary Protein Structure
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Sickle-Cell Disease: A Change in
Primary Structure
• A slight change in primary structure can affect
a protein’s structure and ability to function
• Sickle-cell disease, an inherited blood disorder,
results from a single amino acid substitution in
the protein hemoglobin
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Fig. 5-22
Normal hemoglobin Sickle-cell hemoglobin
Val His Leu Thr Pro Glu Glu
Primary
Primary Val His Leu Thr Pro Val Glu
structure
structure 1 2 3 4 5 6 7 1 2 3 4 5 6 7
Exposed
Secondary Secondary hydrophobic
and tertiary subunit and tertiary region subunit
structures structures
Quaternary Normal Quaternary Sickle-cell
structure hemoglobin structure hemoglobin
(top view)
Function Molecules do Function Molecules
not associate interact with
with one one another and
another; each crystallize into
carries oxygen. a fiber; capacity
to carry oxygen
is greatly reduced.
10 µm 10 µm
Red blood Normal red blood Red blood Fibers of abnormal
cell shape cells are full of cell shape hemoglobin deform
individual red blood cell into
hemoglobin sickle shape.
moledules, each
carrying oxygen.
Fig. 5-22a
Normal hemoglobin
Primary Val His Leu Thr Pro Glu Glu
structure 1 2 3 4 5 6 7
Secondary
and tertiary subunit
structures
Quaternary Normal
structure hemoglobin
(top view)
Function Molecules do
not associate
with one
another; each
carries oxygen.
Fig. 5-22b
Sickle-cell hemoglobin
Primary Val His Leu Thr Pro Val Glu
structure
1 2 3 4 5 6 7
Exposed
Secondary hydrophobic
and tertiary region subunit
structures
Quaternary Sickle-cell
structure hemoglobin
Function Molecules
interact with
one another and
crystallize into
a fiber; capacity
to carry oxygen
is greatly reduced.
Fig. 5-22c
10 µm 10 µm
Normal red blood Fibers of abnormal
cells are full of hemoglobin deform
individual red blood cell into
hemoglobin sickle shape.
molecules, each
carrying oxygen.
What Determines Protein Structure?
• In addition to primary structure, physical and
chemical conditions can affect structure
• Alterations in pH, salt concentration,
temperature, or other environmental factors
can cause a protein to unravel
• This loss of a protein’s native structure is called
denaturation
• A denatured protein is biologically inactive
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Fig. 5-23
Denaturation
Normal protein Renaturation Denatured protein
Protein Folding in the Cell
• It is hard to predict a protein’s structure from its
primary structure
• Most proteins probably go through several
states on their way to a stable structure
• Chaperonins are protein molecules that assist
the proper folding of other proteins
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-24
Correctly
folded
protein
Polypeptide
Cap
Hollow
cylinder
Chaperonin Steps of Chaperonin 2 The cap attaches, causing the 3 The cap comes
(fully assembled) Action: cylinder to change shape in off, and the properly
1 An unfolded poly- such a way that it creates a folded protein is
peptide enters the hydrophilic environment for released.
cylinder from one end. the folding of the polypeptide.
Fig. 5-24a
Cap
Hollow
cylinder
Chaperonin
(fully assembled)
Fig. 5-24b
Correctly
folded
protein
Polypeptide
Steps of Chaperonin 2 The cap attaches, causing the 3 The cap comes
Action: cylinder to change shape in off, and the properly
1 An unfolded poly- such a way that it creates a folded protein is
peptide enters the hydrophilic environment for released.
cylinder from one end. the folding of the polypeptide.
• Scientists use X-ray crystallography to
determine a protein’s structure
• Another method is nuclear magnetic resonance
(NMR) spectroscopy, which does not require
protein crystallization
• Bioinformatics uses computer programs to
predict protein structure from amino acid
sequences
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Fig. 5-25
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
Crystal Digital detector X-ray diffraction
pattern
RESULTS
RNA
polymerase II
DNA
RNA
Fig. 5-25a
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
Crystal Digital detector X-ray diffraction
pattern
Fig. 5-25b
RESULTS
RNA
polymerase II
DNA
RNA
