Session NP 2
1.2 The Structure and Function of Proteins
Book Chapters: 5 Campbell7,9
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
• 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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
α carbon
PowerPoint Lectures for
Biology, Seventh Edition Carboxyl
Amino
Neil Campbell and Jane Reece
group group
Lectures by Chris Romero
Copyright©©2005
Copyright 2005Pearson
PearsonEducation,
Education,Inc.
Inc.publishing
publishingasasBenjamin
BenjaminCummings
Cummings
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
Copyright©©2005
Copyright 2005Pearson
PearsonEducation,
Education,Inc.
Inc.publishing
publishingasasBenjamin
BenjaminCummings
Cummings
Polar
Serine (Ser) Threonine (Thr) Cysteine (Cys) Tyrosine (Tyr) Asparagine (Asn) Glutamine (Gln)
Acidic Basic
PowerPoint
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
Copyright©©2005
Copyright 2005Pearson
PearsonEducation,
Education,Inc.
Inc.publishing
publishingasasBenjamin
BenjaminCummings
Cummings
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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
• 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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
• 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
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
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.
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
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
Copyright©©2005
Copyright 2005Pearson
PearsonEducation,
Education,Inc.
Inc.publishing
publishingasasBenjamin
BenjaminCummings
Cummings
