6. Figure 5.2a
(a) Dehydration reaction: synthesizing a polymer
Short polymer Unlinked monomer
Dehydration removes
a water molecule,
forming a new bond.
Longer polymer
1 2 3 4
1 2 3
6
7. • Breakdown of Polymers to monomers :
– By hydrolysis reaction
• the reverse of the dehydration reaction ??
– ----------------------------------------
7
8. Figure 5.2b
(b) Hydrolysis: breaking down a polymer
Hydrolysis adds
a water molecule,
breaking a bond.
1 2 3 4
1 2 3
8
17. Figure 5.4
(a) Linear and ring forms
(b) Abbreviated ring structure
1
2
3
4
5
6
6
5
4
3
2
1 1
2
3
4
5
6
1
23
4
5
6
17
18. Disaccharide
• A disaccharide is formed when
– a dehydration reaction joins two monosaccharides
• This covalent bond is called a glycosidic linkage
– Example:
• Maltose ( malt sugar )
• Sucrose ( --------------)
• ----------- ( --------------)
18
19. Figure 5.5
(a) Dehydration reaction in the synthesis of maltose
(b) Dehydration reaction in the synthesis of sucrose
Glucose Glucose
Glucose
Maltose
Fructose Sucrose
1–4
glycosidic
linkage
1–2
glycosidic
linkage
1 4
1 2
19
31. Figure 5.9
Chitin forms the exoskeleton
of arthropods.
The structure
of the chitin
monomer
Chitin is used to make a strong and flexible
surgical thread that decomposes after the
wound or incision heals. 31
38. Figure 5.10
(a) One of three dehydration reactions in the synthesis of a fat
(b) Fat molecule (triacylglycerol)
Fatty acid
(in this case, palmitic acid)
Glycerol
Ester linkage
38
39. Figure 5.10a
(a) One of three dehydration reactions in the synthesis of a fat
Fatty acid
(in this case, palmitic acid)
Glycerol
39
42. Figure 5.11
(a) Saturated fat
(b) Unsaturated fat
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.
42
43. Saturated fats
• Are made from saturated fatty acids
• are solid at room temperature
• Most animal fats are saturated
• A diet rich in saturated fats may
contribute to cardiovascular disease
43
44. Unsaturated fats or oils
• Are made from unsaturated fatty acids
• Are liquid at room temperature
• Plant fats and fish fats are usually
unsaturated
44
56. Figure 5.15b
Storage proteins
Ovalbumin Amino acids
for embryo
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.
56
57. Figure 5.15c
Hormonal proteins
Function: Coordination of an organism’s activities
Example: Insulin, a hormone secreted by the
pancreas, causes other tissues to take up glucose,
thus regulating blood sugar concentration
High
blood sugar
Normal
blood sugar
Insulin
secreted
57
58. Figure 5.15d
Muscle tissue
Actin Myosin
100 m
Contractile and motor proteins
Function: Movement
Examples: Motor proteins are responsible for the
undulations of cilia and flagella. Actin and myosin
proteins are responsible for the contraction of
muscles.
58
60. Figure 5.15f
Transport proteins
Transport
protein
Cell membrane
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.
60
62. Figure 5.15h
60 m
Collagen
Connective
tissue
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.
62
66. Figure 5.16
Nonpolar side chains; hydrophobic
Side chain
(R group)
Glycine
(Gly or G)
Alanine
(Ala or A)
Valine
(Val or V)
Leucine
(Leu or L)
Isoleucine
(Ile or I)
Methionine
(Met or M)
Phenylalanine
(Phe or F)
Tryptophan
(Trp or W)
Proline
(Pro or P)
Polar side chains; hydrophilic
Serine
(Ser or S)
Threonine
(Thr or T)
Cysteine
(Cys or C)
Tyrosine
(Tyr or Y)
Asparagine
(Asn or N)
Glutamine
(Gln or Q)
Electrically charged side chains; hydrophilic
Acidic (negatively charged)
Basic (positively charged)
Aspartic acid
(Asp or D)
Glutamic acid
(Glu or E)
Lysine
(Lys or K)
Arginine
(Arg or R)
Histidine
(His or H) 66
67. Figure 5.16a
Nonpolar side chains; hydrophobic
Side chain
Glycine
(Gly or G)
Alanine
(Ala or A)
Valine
(Val or V)
Leucine
(Leu or L)
Isoleucine
(Ile or I)
Methionine
(Met or M)
Phenylalanine
(Phe or F)
Tryptophan
(Trp or W)
Proline
(Pro or P)
67
68. Figure 5.16b
Polar side chains; hydrophilic
Serine
(Ser or S)
Threonine
(Thr or T)
Cysteine
(Cys or C)
Tyrosine
(Tyr or Y)
Asparagine
(Asn or N)
Glutamine
(Gln or Q) 68
69. Figure 5.16c
Electrically charged side chains; hydrophilic
Acidic (negatively charged)
Basic (positively charged)
Aspartic acid
(Asp or D)
Glutamic acid
(Glu or E)
Lysine
(Lys or K)
Arginine
(Arg or R)
Histidine
(His or H)
69
80. secondary structure
• The coils and folds
• Typical secondary structures are
• a coil called an helix and
• a folded structure called a pleated sheet
• Stabilized by :
– H-bonding between between polypeptide
backbone constituents 80
81. Secondary structure
Hydrogen bond
helix
pleated sheet
strand, shown as a flat
arrow pointing toward
the carboxyl end
Hydrogen bond
Figure 5.20c
81
82. 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,
– disulfide bridges
– hydrophobic interactions, and
– van der Waals interactions
82
85. Quaternary structure
• results when two or more polypeptide
chains form one macromolecule
– Example:
• Hemoglobin is a protein consisting of four
polypeptides: two alpha and two beta chains
85