Professional Documents
Culture Documents
Biology
Eighth Edition
Neil Campbell and Jane Reece
Lectures by Chris Romero, updated by Erin Barley with contributions from Joan Sharp
Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Overview: The Molecules of Life
HO 1 2 3 H HO H
HO 1 2 3 4 H
Longer polymer
(a) Dehydration reaction in the synthesis of a polymer
HO 1 2 3 4 H
HO 1 2 3 H HO H
HO 1 2 3 H HO H
HO 1 2 3 4 H
Longer polymer
(a) Dehydration reaction in the synthesis of a polymer
Fig. 5-2b
HO 1 2 3 4 H
HO 1 2 3 H HO H
Aldoses
Glyceraldehyde
Ribose
Glucose Galactose
Ketoses
Dihydroxyacetone
Ribulose
Fructose
Fig. 5-3a
Glyceraldehyde
Ribose
Glucose Galactose
Fig. 5-3b
Dihydroxyacetone
Ribulose
Fructose
Though often drawn as linear skeletons, in
aqueous solutions many sugars form rings
Monosaccharides serve as a major fuel for
cells and as raw material for building molecules
Animation: Disaccharides
14
glycosidic
linkage
0.5 m
1 m
Amylose Glycogen
Amylopectin
Animation: Polysaccharides
Glucose Glucose
(b) Starch: 14 linkage of glucose monomers (b) Cellulose: 14 linkage of glucose monomers
Fig. 5-7a
Glucose Glucose
10 m
0.5 m
Cellulose
molecules
b Glucose
monomer
Enzymes that digest starch by hydrolyzing
linkages cant hydrolyze linkages in cellulose
Cellulose in human food passes through the
digestive tract as insoluble fiber
Some microbes use enzymes to digest
cellulose
Many herbivores, from cows to termites, have
symbiotic relationships with these microbes
(a) The structure (b) Chitin forms the (c) Chitin is used to make
of the chitin exoskeleton of a strong and flexible
monomer. arthropods. surgical thread.
Concept 5.3: Lipids are a diverse group of
hydrophobic molecules
Lipids are the one class of large biological
molecules that do not form polymers
The unifying feature of lipids is having little or
no affinity for water
Lipids are hydrophobic becausethey consist
mostly of hydrocarbons, which form nonpolar
covalent bonds
The most biologically important lipids are fats,
phospholipids, and steroids
Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fats
Fatty acid
(palmitic acid)
Glycerol
(a) Dehydration reaction in the synthesis of a fat
Ester linkage
Fatty acid
(palmitic acid)
Glycerol
(a) Dehydration reaction in the synthesis of a fat
Fig. 5-11b
Ester linkage
Animation: Fats
Structural
formula of a
saturated fat
molecule
Stearic acid, a
saturated fatty
acid
(a) Saturated fat
Structural formula
of an unsaturated
fat molecule
Oleic acid, an
unsaturated
fatty acid
cis double
bond causes
(b) Unsaturated fat bending
Fig. 5-12a
Structural
formula of a
saturated fat
molecule
Stearic acid, a
saturated fatty
acid
(a) Saturated fat
Fig. 5-12b
Structural formula
of an unsaturated
fat molecule
Oleic acid, an
unsaturated
fatty acid
cis double
bond causes
(b) Unsaturated fat bending
Fats made from saturated fatty acids are called
saturated fats, and are solid at room
temperature
Most animal fats are saturated
Hydrophilic head
Choline
Phosphate
Glycerol
Hydrophobic tails
Fatty acids
Hydrophilic
head
Hydrophobic
tails
Hydrophilic head
Choline
Phosphate
Glycerol
Hydrophobic tails
Fatty acids
Hydrophilic WATER
head
Hydrophobic
WATER
tail
Steroids
Animation: Enzymes
Substrate
(sucrose)
Glucose
Enzyme
(sucrase)
OH
H2O
Fructose
HO
Polypeptides
carbon
Amino Carboxyl
group group
Fig. 5-17
Nonpolar
Polar
Electrically
charged
Acidic Basic
Nonpolar
Polar
Electrically
charged
Acidic Basic
Peptide
bond
(a)
Side chains
Peptide
bond
Backbone
Groove
Groove
Groove
Groove
pleated sheet
H3N
+
Amino end
Examples of
amino acid
subunits
helix
Fig. 5-21a
Primary Structure
1
5
+
H3N
Amino end
10
15 Amino acid
subunits
20
25
Fig. 5-21b 1
5
H3N
+
Amino end
10
15 Amino acid
subunits
20
25
75
80
90
85
95
105
100
110
115
120
125
Carboxyl end
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
Secondary Structure
pleated sheet
Examples of
amino acid
subunits
helix
Fig. 5-21d
Polypeptide
backbone
Hydrogen
bond
Disulfide bridge
Ionic bond
Fig. 5-21g
Polypeptide Chains
chain
Iron
Heme
Chains
Hemoglobin
Collagen
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
Exposed
Secondary Secondary hydrophobic
and tertiary subunit and tertiary region subunit
structures structures
Quaternary Normal Quaternary Sickle-cell
structure hemoglobin structure hemoglobin
(top view)
10 m 10 m
Secondary
and tertiary subunit
structures
Quaternary Normal
structure hemoglobin
(top view)
Function Molecules do
not associate
with one
another; each
carries oxygen.
Fig. 5-22b
Sickle-cell hemoglobin
Primary
Val His Leu Thr Pro Val Glu
structure
1 2 3 4 5 6 7
Exposed
Secondary hydrophobic
and tertiary region subunit
structures
Quaternary Sickle-cell
structure hemoglobin
Function Molecules
interact with
one another and
crystallize into
a fiber; capacity
to carry oxygen
is greatly reduced.
Fig. 5-22c
10 m 10 m
Denaturation
Correctly
folded
protein
Polypeptide
Cap
Hollow
cylinder
Chaperonin Steps of Chaperonin 2 The cap attaches, causing the 3 The cap comes
(fully assembled) Action: cylinder to change shape in off, and the properly
1 An unfolded poly- such a way that it creates a folded protein is
peptide enters the hydrophilic environment for released.
cylinder from one end. the folding of the polypeptide.
Fig. 5-24a
Cap
Hollow
cylinder
Chaperonin
(fully assembled)
Fig. 5-24b
Correctly
folded
protein
Polypeptide
Steps of Chaperonin 2 The cap attaches, causing the 3 The cap comes
Action: cylinder to change shape in off, and the properly
1 An unfolded poly- such a way that it creates a folded protein is
peptide enters the hydrophilic environment for released.
cylinder from one end. the folding of the polypeptide.
Scientists use X-ray crystallography to
determine a proteins structure
Another method is nuclear magnetic resonance
(NMR) spectroscopy, which does not require
protein crystallization
Bioinformatics uses computer programs to
predict protein structure from amino acid
sequences
Diffracted
X-rays
X-ray
source X-ray
beam
RESULTS
RNA
polymerase
DNA
RNA
Fig. 5-25a
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
RESULTS
RNA
polymerase
DNA
RNA
Concept 5.5: Nucleic acids store and transmit
hereditary information
The amino acid sequence of a polypeptide is
programmed by a unit of inheritance called a
gene
Genes are made of DNA, a nucleic acid
DNA
1 Synthesis of
mRNA in the
nucleus mRNA
NUCLEUS
CYTOPLASM
Fig. 5-26-2
DNA
1 Synthesis of
mRNA in the
nucleus mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm
via nuclear pore
Fig. 5-26-3
DNA
1 Synthesis of
mRNA in the
nucleus mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm Ribosome
via nuclear pore
3 Synthesis
of protein
Amino
Polypeptide acids
The Structure of Nucleic Acids
5 end
Nitrogenous bases
Pyrimidines
5C
3C
Nucleoside
Nitrogenous
base Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA)
Purines
Phosphate
group Sugar
5C (pentose)
Adenine (A) Guanine (G)
3C (b) Nucleotide
Sugars
3 end
(a) Polynucleotide, or nucleic acid
5'C
3'C
Nucleoside
Nitrogenous
base
5'C
Phosphate 3'C
group Sugar
5'C (pentose)
3' end
(a) Polynucleotide, or nucleic acid
Fig. 5-27c-1
Nitrogenous bases
Pyrimidines
Purines
Sugars
Sugar-phosphate
backbones
Old strands
Nucleotide
about to be
added to a
new strand
3' end
5' end
New
strands
% of glycosidic
linkages broken
50
0
100
Time
Fig. 5-UN4
Fig. 5-UN5
Fig. 5-UN6
Fig. 5-UN7
Fig. 5-UN8
Fig. 5-UN9
Fig. 5-UN10
You should now be able to: