Session NP 2

1.2 The Structure and Function of Proteins

Book Chapters: 5 Campbell7,9

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Concept 1.2: 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

Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings

Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
 Animation: Structural Proteins Animation: Hormonal Proteins

Animation: Storage Proteins Animation: Sensory Proteins

Animation: Transport Proteins Animation: Gene Regulatory Proteins

Animation: Receptor Proteins

Animation: Contractile Proteins

Animation: Defensive Proteins

Animation: Enzymes

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• Enzymes are a type of protein that acts as a catalyst, speeding up
chemical reactions
• Enzymes can perform their functions repeatedly, functioning as
workhorses that carry out the processes of life

Substrate
(sucrose)

Glucose
Enzyme
(sucrase)
Fructose

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Polypeptides
• Polypeptides are polymers of amino acids
• A protein consists of one or more polypeptides

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
• Cells use 20 amino acids to make thousands of proteins

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 monomers to more than a
thousand
• Each polypeptide has a unique linear sequence of amino acids
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 α carbon

PowerPoint Lectures for

Biology, Seventh Edition Carboxyl
Amino
Neil Campbell and Jane Reece
group group

Lectures by Chris Romero

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

Nonpolar

PowerPoint Lectures for

Methionine
Biology, Seventh (Met)
Edition Phenylalanine (Phe) Tryptophan (Trp) Proline (Pro)

Neil Campbell and Jane Reece

Lectures by Chris Romero

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 Polar

Serine (Ser) Threonine (Thr) Cysteine (Cys) Tyrosine (Tyr) Asparagine (Asn) Glutamine (Gln)

Acidic Basic

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Electrically Lectures for
charged
Biology, Seventh Edition
Neil Campbell and Jane Reece

Aspartic acid (Asp) Glutamic acid (Glu) Lysine (Lys) Arginine (Arg) Histidine (His)
Lectures by Chris Romero
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Protein Conformation and Function

• A functional protein
consists of one or more
polypeptides twisted,
folded, and coiled into a Groove
unique shape
• The sequence of amino
acids determines a
A ribbon model
protein’s three-dimensional
conformation
• A protein’s conformation
determines its function
• Ribbon models and space- Groove
filling models can depict a
protein’s conformation
A space-filling model
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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

β pleated sheet
+H N
3
Amino end Amino acid
subunits

α helix

Animation: Protein Structure Introduction

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 Amino end Amino acid
subunits

• 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

Carboxyl end
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
• 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 alpha helix and a
folded structure called a beta pleated sheet
Animation: Secondary Protein Structure

β pleated sheet

Amino acid
subunits

α helix

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• Tertiary structure is
determined by interactions
between R groups, rather
than interactions between
backbone constituents
• These interactions between
Hydrophobic
R groups include hydrogen interactions and
bonds, ionic bonds, van der Waals
interactions
hydrophobic interactions, Polypeptide
and van der Waals backbone

interactions Hydrogen
bond

• Strong covalent bonds called

Disulfide bridge
disulfide bridges may
reinforce the protein’s
conformation Ionic bond

Animation: Tertiary Protein Structure

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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
• Hemoglobin is a globular protein consisting of four polypeptides: two alpha
and two beta chains Animation: Quaternary Protein Structure
Polypeptide chain
β Chains

Iron
Heme
α Chains
Polypeptide chain Collagen Hemoglobin
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Sickle-Cell Disease: A Simple Change in
Primary Structure
• 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

10 µm 10 µm

Red blood Normal cells are Red blood Fibers of abnormal

cell shape full of individual cell shape hemoglobin deform
hemoglobin cell into sickle
molecules, each shape.
carrying oxygen.

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 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

PowerPointnotLectures
associate for interact with
with one one another to
Biology, Seventh Edition
another; each crystallize into
carries oxygen.
Neil Campbell and Jane Reece a fiber; capacity
to carry oxygen
is greatly reduced.

Lectures by Chris Romero

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