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of Life
Longer polymer
Dehydration reaction in the synthesis of a polymer
Hydrolysis of a polymer
The Diversity of Polymers
1 2 3 H HO
Glyceraldehyde
Ribose
Glucose Galactose
Dihydroxyacetone
Ribulose
Fructose
Monosaccharides serve as a major fuel for cells and as raw
material for building molecules
Though often drawn as a linear skeleton, in aqueous solutions
they form rings
Linear and Abbreviated ring
ring forms structure
A disaccharide is formed when a dehydration reaction joins
two monosaccharides
This covalent bond is called a glycosidic bond
Lactose = Glu + Gal
Maltose = Glu + Glu
Sucrose = Glu + Fru
Dehydration
14
reaction in the glycosidic
synthesis of maltose linkage
Dehydration
12
reaction in the glycosidic
synthesis of sucrose linkage
Glucose
monomer
Glycogen granules
in muscle
tissue Glycogen
Cellulose microfibrils
in a plant cell wall Cellulose
Cellulose
Hydrogen bonds
molecules
between OH groups
(not shown) attached to
carbons 3 and 6
Storage Polysaccharides
1 m
Amylose Amylopectin
0.5 m
Glycogen
0.5 m
Plant cells
Cellulose
molecules
Glucose
monomer
Enzymes that digest starch by hydrolyzing alpha linkages cant
hydrolyze beta 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
Chitin, another structural polysaccharide, is found in the
exoskeleton of arthropods
Chitin also provides structural support for the cell walls of
many fungi
Chitin can be used as surgical thread
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 because they consist mostly of
hydrocarbons, which form nonpolar covalent bonds
The most biologically important lipids are fats, phospholipids
and steroids
Fats
Glycerol
Dehydration reaction in the synthesis of a fat
Fats separate from water because water
molecules form hydrogen bonds with each other
and exclude the fats
In a fat, three fatty acids are joined to glycerol by
an ester linkage, creating a triacylglycerol, or
triglyceride
Ester linkage
Structural
formula of a
saturated fat
molecule
Structural
formula
of an
unsaturated
Space-filling fat molecule
model of
stearic acid,
a saturated
fatty acid
Space-filling
model of oleic
acid, an
unsaturated
fatty acid Double bond
causes bending.
Fats made from saturated fatty acids are called saturated fats
Most animal fats are saturated
Saturated fats are solid at room temperature
A diet rich in saturated fats may contribute to cardiovascular
disease through plaque deposits
Stearic acid
Choline
Phosphate
Glycerol
Hydrophobic tails
Fatty acids
Hydrophilic
head
Hydrophobic
tails
(a) Structural formula (b) Space-filling model (c) Phospholipid (d) Phospholipid
symbol bilayer
When phospholipids are added to water, they self-assemble
into a bilayer, with the hydrophobic tails pointing toward the
interior
The structure of phospholipids results in a bilayer
arrangement found in cell membranes
Phospholipids are the major component of all cell membranes
WATER
Hydrophilic
head
Hydrophobic
WATER
tails
Steroids
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
Enzymatic proteins Defensive proteins
Function: Selective acceleration of Function: Protection against disease
chemical reactions Example: Antibodies inactivate and help
Example: Digestive enzymes catalyze the destroy viruses and bacteria.
hydrolysis of bonds in food molecules.
Antibodies
Glucose
Enzyme
(sucrose)
Fructose
Defensive proteins
Function: Protection against disease
Example: Antibodies inactivate and help
destroy viruses and bacteria.
Antibodies
Virus Bacterium
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.
Transport
protein
Cell membrane
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.
Insulin
High secreted Normal
blood sugar blood sugar
Receptor proteins
Function: Response of cell to chemical
stimuli
Example: Receptors built into the
membrane of a nerve cell detect signaling
molecules released by other nerve cells.
Receptor
protein
Signaling molecules
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.
Actin Myosin
Muscle tissue 30 m
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
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
carbon
Amino Carboxyl
group group
Nonpolar side chains; hydrophobic
Side chain
(R group)
New peptide
bond forming
Side
chains
Back-
bone
helix
pleated sheet
Transthyretin Transthyretin
polypeptide protein
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
Primary structure
Amino
acids
1 5 10
Amino end
30 25 20 15
35 40 45 50
75
80 85 90
95
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 alpha helix
and a folded structure called a beta pleated sheet
Secondary structure
helix
Hydrogen bond
pleated sheet
strand
Hydrogen
bond
Tertiary structure
Transthyretin
polypeptide
Hydrophobic
interactions and
van der Waals
interactions
Polypeptide
backbone
Hydrogen
bond
Disulfide bridge
Ionic bond
Quaternary structure
Transthyretin
protein
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
Polypeptide
chain Chains
Iron
Heme
Chains
Polypeptide chain Collagen Hemoglobin
Sickle-Cell Disease: A Simple Change in
Primary Structure
Secondary
Primary Quaternary Red Blood Cell
and Tertiary Function
Structure Structure Shape
Structures
Normal Molecules do not
1 hemoglobin associate with one
2 another; each carries
3 oxygen.
Normal
4
5 subunit
6
7
5 m
3
4
5
6 subunit
7
5 m
What Determines Protein
Conformation?
Renaturation
The Protein-Folding Problem
Hollow
cylinder
Chaperonin
(fully assembled)
Correctly
Polypeptide folded
protein
Diffracted X-rays
X-ray
X-ray
source
beam
Crystal
Nucleic acid Protein
X-ray
source X-ray
beam
Results
RNA DNA
RNA
polymerase
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
The Roles of Nucleic Acids
There are two types of nucleic acids:
Deoxyribonucleic acid (DNA)
Ribonucleic acid (RNA)
DNA provides directions for its own replication
DNA directs synthesis of messenger RNA (mRNA) and, through
mRNA, controls protein synthesis
Protein synthesis occurs in ribosomes
DNA
Synthesis of
mRNA in the nucleus
mRNA
NUCLEUS
CYTOPLASM
mRNA
Movement of
mRNA into cytoplasm
Ribosome
via nuclear pore
Synthesis
of protein
Amino
Polypeptide acids
The Structure of Nucleic Acids
Nucleic acids are polymers called polynucleotides
Each polynucleotide is made of monomers called nucleotides
Each nucleotide consists of a nitrogenous base, a pentose
sugar and a phosphate group
The portion of a nucleotide without the phosphate group is
called a nucleoside
Sugar-phosphate backbone
5 end (on blue background) Nitrogenous bases
Pyrimidines
5C
3C
Nucleoside
Nitrogenous
Cytosine (C) Thymine Uracil
base
(T, in DNA) (U, in RNA)
Purines
Phosphate
5C group Sugar
(pentose) Adenine (A) Guanine (G)
3C
(b) Nucleotide
Sugars
3 end
(a) Polynucleotide, or nucleic acid
Nucleoside
Nitrogenous
base
Phosphate
group Pentose
sugar
Nucleotide
3 end
Polynucleotide, or
nucleic acid
5 3 Sugar-phosphate
backbones
Hydrogen bonds
Purines
Adenine Guanine
A G
Pentose sugars
Nucleoside components
Nucleotide Polymers
Nucleotide polymers are linked together, building a polynucleotide
Adjacent nucleotides are joined by covalent bonds that form
between the OH group on the 3 carbon of one nucleotide and
the phosphate on the 5 carbon on the next
These links create a backbone of sugar-phosphate units with
nitrogenous bases as appendages
The sequence of bases along a DNA or mRNA polymer is unique for
each gene
The DNA Double Helix
A DNA molecule has two polynucleotides spiraling around an
imaginary axis, forming a double helix
In the DNA double helix, the two backbones run in opposite 5
to 3 directions from each other, an arrangement referred to as
antiparallel
One DNA molecule includes many genes
The nitrogenous bases in DNA form hydrogen bonds in a
complementary fashion: A always with T, and G always with
C
5 end 3 end
Sugar-phosphate
backbone
Old strands
Nucleotide
about to be
added to a
new strand
5 end
New
strands
3 end 5 end
5 end 3 end
DNA and Proteins as Tape
Measures of Evolution