Professional Documents
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Chapter 5
Lectures by
Erin Barley
Kathleen Fitzpatrick
2011 Pearson Education, Inc.
Figure 5.1
Animation: Polymers
2011 Pearson Education, Inc.
Figure 5.2a
Unlinked monomer
Short polymer
Dehydration removes
a water molecule,
forming a new bond.
Longer polymer
Figure 5.2b
Hydrolysis adds
a water molecule,
breaking a bond.
Sugars
Monosaccharides 1:2:1 ratio CHO
classified by
The location of the carbonyl group
(as aldose or ketose)
The number of carbons in the carbon
skeleton
Figure 5.3
Aldoses (Aldehyde Sugars)
Glyceraldehyde
Dihydroxyacetone
Ribose
Ribulose
Glucose
Galactose
Fructose
Figure 5.3c
Glucose
Galactose
Fructose
Figure 5.4
1
2
3
4
4
5
1
3
6
5
4
1
3
1
3
Figure 5.5
14
glycosidic
1 linkage 4
Glucose
Glucose
Maltose
12
glycosidic
1 linkage 2
Glucose
Fructose
Sucrose
Polysaccharides
Polysaccharides
storage
structural roles
Storage Polysaccharides
Figure 5.6
Chloroplast
Starch granules
Amylopectin
Amylose
(a) Starch:
1 m
a plant polysaccharide
Mitochondria
Glycogen granules
Glycogen
(b) Glycogen:
0.5 m
an animal polysaccharide
Figure 5.6a
Chloroplast
Starch granules
1 m
Figure 5.6b
Mitochondria
Glycogen granules
0.5 m
Structural Polysaccharides
cellulose is a major component of the tough
wall of plant cells
polymer of glucose with different glycosidic
linkages differ
The difference is based on two ring forms for
glucose: alpha () and beta ()
Animation: Polysaccharides
2011 Pearson Education, Inc.
Figure 5.7
Glucose
Glucose
1 4
1 4
Figure 5.8
Cellulose
microfibrils in a
plant cell wall
Cell wall
Microfibril
10 m
0.5 m
Cellulose
molecules
Glucose
monomer
Figure 5.9
The structure
of the chitin
monomer
Figure 5.10
Fatty acid
(in this case, palmitic acid)
Glycerol
(a) One of three dehydration reactions in the synthesis of a fat
Ester linkage
Figure 5.11
Structural
formula of a
saturated fat
molecule
Space-filling
model of stearic
acid, a saturated
fatty acid
Structural
formula of an
unsaturated fat
molecule
Space-filling model
of oleic acid, an
unsaturated fatty
acid
Cis double bond
causes bending.
Hydrogenation
trans fats
Energy storage
Omega-3
Adipose tissue
Hydrophobic tails
Hydrophilic head
Figure 5.12
Choline
Phosphate
Glycerol
Fatty acids
Hydrophilic
head
Hydrophobic
tails
Hydrophobic tails
Hydrophilic head
Figure 5.12a
Choline
Phosphate
Glycerol
Fatty acids
Figure 5.13
Hydrophilic
head
Hydrophobic
tail
WATER
WATER
Figure 5.14
Concept 5.4:
Proteins
50% of the dry mass of most cells
functions
a. structural support
b. Storage
c. Transport
d. cellular communications
e. Movement
f. defense against foreign substances
Figure 5.15a
Enzymatic proteins
Function: Selective acceleration of chemical reactions
Example: Digestive enzymes catalyze the hydrolysis
of bonds in food molecules.
Enzyme
Figure 5.15b
Storage proteins
Function: Storage of amino acids
Examples: Casein, the protein of milk, is the major
source of amino acids for baby mammals. Plants have
storage proteins in their seeds. Ovalbumin is the
protein of egg white, used as an amino acid source
for the developing embryo.
Ovalbumin
Amino acids
for embryo
Figure 5.15c
Hormonal proteins
Function: Coordination of an organisms activities
Example: Insulin, a hormone secreted by the
pancreas, causes other tissues to take up glucose,
thus regulating blood sugar concentration
High
blood sugar
Insulin
secreted
Normal
blood sugar
Figure 5.15d
Actin
Muscle tissue
100 m
Myosin
Figure 5.15e
Defensive proteins
Function: Protection against disease
Example: Antibodies inactivate and help destroy
viruses and bacteria.
Antibodies
Virus
Bacterium
Figure 5.15f
Transport proteins
Function: Transport of substances
Examples: Hemoglobin, the iron-containing protein of
vertebrate blood, transports oxygen from the lungs to
other parts of the body. Other proteins transport
molecules across cell membranes.
Transport
protein
Cell membrane
Figure 5.15g
Receptor proteins
Function: Response of cell to chemical stimuli
Signaling
molecules
Receptor
protein
Figure 5.15h
Structural proteins
Function: Support
Examples: Keratin is the protein of hair, horns,
feathers, and other skin appendages. Insects and
spiders use silk fibers to make their cocoons and webs,
respectively. Collagen and elastin proteins provide a
fibrous framework in animal connective tissues.
Collagen
Connective
tissue
60 m
Figure 5.UN01
Amino
group
Carboxyl
group
Figure 5.16
Nonpolar side chains; hydrophobic
Side chain
(R group)
Glycine
(Gly or G)
Alanine
(Ala or A)
Methionine
(Met or M)
Isoleucine
(Ile or I)
Leucine
(Leu or L)
Valine
(Val or V)
Phenylalanine
(Phe or F)
Tryptophan
(Trp or W)
Proline
(Pro or P)
Serine
(Ser or S)
Threonine
(Thr or T)
Cysteine
(Cys or C)
Tyrosine
(Tyr or Y)
Asparagine
(Asn or N)
Glutamine
(Gln or Q)
Aspartic acid
(Asp or D)
Glutamic acid
(Glu or E)
Lysine
(Lys or K)
Arginine
(Arg or R)
Histidine
(His or H)
Figure 5.17
Peptide bond
New peptide
bond forming
Side
chains
Backbone
Amino end
(N-terminus)
Peptide
bond
Carboxyl end
(C-terminus)
Figure 5.18
Groove
Groove
Figure 5.19
Antibody protein
primary structure
Secondary structure
Tertiary
Quaternary
Figure 5.20a
Primary structure
Amino
acids
Amino end
Carboxyl end
Figure 5.20b
Tertiary
structure
Secondary
structure
Quaternary
structure
helix
Hydrogen bond
pleated sheet
strand
Hydrogen
bond
Transthyretin
polypeptide
Transthyretin
protein
Figure 5.20c
Secondary structure
helix
pleated sheet
Hydrogen bond
strand, shown as a flat
arrow pointing toward
the carboxyl end
Hydrogen bond
Figure 5.20d
Figure 5.20f
Hydrogen
bond
Hydrophobic
interactions and
van der Waals
interactions
Disulfide
bridge
Ionic bond
Polypeptide
backbone
Figure 5.20g
Quaternary structure
Transthyretin
protein
(four identical
polypeptides)
Figure 5.20h
Collagen
Figure 5.20i
Heme
Iron
subunit
subunit
subunit
subunit
Hemoglobin
Figure 5.20j
Figure 5.21
Sickle-cell hemoglobin
Normal hemoglobin
Primary
Structure
1
2
3
4
5
6
7
Secondary
and Tertiary
Structures
Quaternary
Structure
Function
Molecules do not
associate with one
another; each carries
oxygen.
Normal
hemoglobin
subunit
Red Blood
Cell Shape
10 m
1
2
3
4
5
6
7
Exposed
hydrophobic
region
Sickle-cell
hemoglobin
subunit
Molecules crystallize
into a fiber; capacity
to carry oxygen is
reduced.
10 m
Figure 5.21a
10 m
Figure 5.21b
10 m
Figure 5.22
aturat ion
n
e
D
Normal protein
Re
na
t ura t i on
Denatured protein
Figure 5.23b
Polypeptide
Correctly
folded
protein
Figure 5.24
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
Crystal
Digital detector
X-ray diffraction
pattern
RESULTS
RNA
DNA
RNA
polymerase II
Figure 5.25-1
DNA
1 Synthesis of
mRNA
mRNA
NUCLEUS
CYTOPLASM
Figure 5.25-2
DNA
1 Synthesis of
mRNA
mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into
cytoplasm
Figure 5.25-3
DNA
1 Synthesis of
mRNA
mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into
cytoplasm
Ribosome
3 Synthesis
of protein
Polypeptide
Amino
acids
Figure 5.26
5 end
Sugar-phosphate backbone
Nitrogenous bases
Pyrimidines
5C
3C
Nucleoside
Nitrogenous
base
5C
1C
5C
3C
Phosphate
group
3C
Sugar
(pentose)
Guanine (G)
Adenine (A)
(b) Nucleotide
3 end
Sugars
Figure 5.27
Sugar-phosphate
backbones
Hydrogen bonds
(a) DNA
Figure 5.UN02
Figure 5.UN02a
Figure 5.UN02b
Figure 5. UN03
Figure 5. UN04
Figure 5. UN05
Figure 5. UN06
Figure 5. UN07
Figure 5. UN08
Figure 5. UN09
Figure 5. UN10
Figure 5. UN11
Figure 5. UN12
Figure 5. UN13