BIOLOGY TENTH EDITION

Global Edition

Campbell • Reece • Urry • Cain • Wasserman • Minorsky • Jackson

5
Biological Macromolecules and Lipids
Topic 1 Biological Molecules
(Protein)
Lecture Presentation by
Nicole Tunbridge and
Kathleen Fitzpatrick

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 Learning Outcomes
1. Identify different types of protein and their functions
2. Describe the general structure of an amino acid &
peptide bond formation
3. Explain primary, secondary, tertiary and quaternary
structure levels of proteins
4. Relate the structure of globular protein and fibrous
protein to their functions

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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
• Examples of protein functions:
1. Enzymes 5. Signaling (hormones)
2. Storage 6. Contractile / Movement
3. Defense 7. Receptor
4. Transport 8. Structural support

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Enzymatic proteins
Function: Acceleration of chemical reactions.

Example: Digestive enzymes catalyze the hydrolysis

of bonds in food molecules.

Enzyme

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Storage proteins
Function: Storage of amino acids
Examples: Ovalbumin is the protein of egg white,
used as an amino acid source for the developing embryo.

Ovalbumin Amino acids

for embryo

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Defensive proteins
Function: Protection against disease
Example: Antibodies inactivate and help destroy viruses
and bacteria.
Antibodies

Virus Bacterium

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Transport proteins
Function: Transport of substances
Examples: Hemoglobin transports oxygen from
the lungs to other parts of the body. Other proteins
transport molecules across membranes, as shown here.

Transport
protein

Cell membrane

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Hormonal proteins
Function: Coordination of an organism’s activities

Example: Insulin causes other tissues to take up glucose,

thus regulating blood sugar level.

Insulin
High secreted Normal
blood sugar blood sugar

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Contractile and motor proteins
Function: Movement
Examples: Actin and myosin proteins are responsible
for muscle contraction.
Actin Myosin

Muscle
30 µm
tissue

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Receptor proteins
Function: Response of cell to chemical stimuli

Example: Receptors built into the membrane of a nerve

cell detect signaling molecules released by other
nerve cells.

Receptor
Signaling protein
molecules

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Structural proteins
Function: Support
Examples: Keratin is the protein of hair, horns, feathers,
and other skin appendages. Collagen provides a fibrous
framework in animal connective tissues.

Collagen

Connective
tissue 60 µm

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Amino Acid Monomers

• Amino acids are organic molecules with amino and

carboxyl groups
• Amino acids differ in their properties due to differing
side chains, called R groups

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Figure 5.UN01

Side chain (R group)

𝛂 carbon

X Y

What is this molecule called?

What groups are X & Y?

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Figure 5.14a

Nonpolar side chains; hydrophobic

Side chain (R group)

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)

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Figure 5.14b

Polar side chains; hydrophilic

Serine Threonine Cysteine

(Ser or S) (Thr or T) (Cys or C)

Tyrosine Asparagine Glutamine

(Tyr or Y) (Asn or N) (Gln or Q)

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Figure 5.14c

Electrically charged side chains; hydrophilic

Basic (positively charged)

Acidic (negatively charged)

Aspartic acid Glutamic acid Lysine Arginine Histidine

(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)

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Polypeptides (Amino Acid Polymers)

• Amino acids are linked by covalent bonds called

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, with a carboxyl end (C-terminus) and
an amino end (N-terminus)

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 • Proteins are all constructed from the same set of 20
amino acids
• Polypeptides are unbranched polymers built from
these amino acids
• A protein is a biologically functional molecule that
consists of one or more polypeptides

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 (a) (b)
What type of
reaction is this?

What is the name of

Peptide bond
bond W?

(c) New peptide

bond forming
Which is an example
Side
chains of a ‘dipeptide’ &
‘tripeptide’?
Back-
bone

Amino end W Carboxyl end

(N-terminus) (C-terminus)
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Protein Structure and Function

• A functional protein consists of one or more

polypeptides precisely twisted, folded, and coiled into
a unique three-dimensional (3D) structure
• The sequence of amino acids determines a protein’s
3D structure
• A protein’s 3D structure determines how it works
• The function of a protein usually depends on
its ability to recognize and bind to some other
molecule

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Figure 5.17

Antibody protein Protein from flu virus

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 Animation: Protein Structure
Introduction

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 Animation :
Protein Structure Introduction

1. What shape are most proteins?

2. What is the name given to a protein polymer?

3. What is a protein monomer called?

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Four Levels of Protein Structure

• 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

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Animation: Primary Protein Structure

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 a) The primary structure of a protein is its sequence of
amino acids
b) Primary structure is like the order of letters in a long
word
c) Primary structure is determined by inherited genetic
information
Primary Structure
Amino
acids

1 5 10

Amino end
30 25 20 15

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Figure 5.18a
Primary Structure

Primary structure Amino

of transthyretin
acids

1 5 10

Function: Amino end

Transport vitamin A & 30 25 20 15

one of the thyroid

hormones in blood
35 40 45 50

Primary structure of transthyretin

55
70 65 60

75
80 85 90

95

115 110 105 100

120 125
Carboxyl end
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Proteins

What bonds are involved in primary structure?

Which parts of two amino acids are involved per bond?

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Animation: Secondary Protein Structure

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 Animation:
Secondary Protein Structure

What shapes can you see in secondary structure?

What bonds are responsible for producing such

shapes?

Which atoms are involved in such bonds?

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 • 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

𝛂 helix

Hydrogen bond
𝛃 strand
Hydrogen
bond

𝛃 pleated sheet

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 Abdominal glands of the
spider secrete silk fibers
made of a structural protein
containing β 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.

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Animation: Tertiary Protein Structure

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• Tertiary structure, the overall shape of a
polypeptide, results from interactions between
R groups
• These interactions include hydrogen bonds,
ionic bonds, hydrophobic interactions, and
van der Waals interactions
• Strong covalent bonds called disulfide bridges may
reinforce the protein’s structure

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Figure 5.18d

Hydrogen
bond
Hydrophobic
interactions and
Van der Waals
interactions
Disulfide
bridge
Ionic bond

Polypeptide
backbone

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Animation: Quaternary Protein Structure

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 Animation :
Quaternary Protein Structure

How many poly peptides are involved?

What type of bonds give rise to Quaternary Structure?

Are these intra- or inter-polypeptide bonds?

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 • 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

Collagen

• Hemoglobin is a globular protein consisting of

four polypeptides: two alpha and two beta chains
Hemoglobin

Heme
Iron
𝛃 subunit
𝛂 subunit
𝛂 subunit
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𝛃 subunit
What’s the difference between the 2 structures below?

Tertiary Structure Quaternary Structure

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Which levels of protein structure are represented below?

Polypeptide  Chains
chain

Iron
Heme

α Chains

Collagen
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Hemoglobin
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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Figure 5.19

Secondary
Primary Quaternary Function Red Blood Cell
and Tertiary
Structure Structure Shape
Structures
1 Normal 𝛃 Normal Proteins do not associate
subunit hemoglobin with one another; each
2
carries oxygen.
3
𝛃
Normal

4
5 𝛂
6
7 5 µm
𝛃 𝛂

1 Sickle-cell 𝛃 Sickle-cell Proteins aggregate into a

subunit hemoglobin fiber; capacity to
2
carry oxygen
3 𝛃
Sickle-cell

is reduced.
4
5 𝛂
6
7 5 µm
𝛃 𝛂

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 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.
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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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Figure 5.20-3

Normal protein Denatured protein

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 Match the terms with respective definitions.

Term Definition

Protein? 1. two or more amino acids joined.

Polypeptide? 2. linear polymer composed of multiple amino
Peptide? acids.
3. not-yet functional product.
4. large polypeptides.
5. a functional product after undergoing
subsequent chemical modification.

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