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The Molecules of Life
Macromolecules/Biomolecules
• Within cells, small organic molecules are joined
together to form larger molecules
• Macromolecules are large molecules composed
of thousands of covalently connected atoms
Most macromolecules are polymers, built from
monomers
• A polymer is a long molecule consisting of many
similar building blocks called monomers
• Three of the four classes of life’s organic
molecules are polymers:
– Carbohydrates
– Proteins
– Nucleic acids
– Fats – are large molecules but not
polymers
The Synthesis and Breakdown of Polymers
• Monomers form larger molecules by condensation
reactions called dehydration reactions
• Polymers are broken down to monomers by
hydrolysis, a reaction that is essentially the
reverse of the dehydration reaction
Short polymer
Unlinked monomer
Dehydration removes a water
molecule, forming a new bond
Longer polymer
Dehydration reaction in the synthesis of a polymer
Hydrolysis adds a water
molecule, breaking a bond
Hydrolysis of a polymer
Carbohydrates serve as fuel and building material
• Carbohydrates are sugars and the polymers of
sugars
• The simplest carbohydrates are
monosaccharides, or single sugars
• Carbohydrate macromolecules are
polysaccharides, polymers composed of many
(> 10 monomers) sugar building blocks
Sugars
• Monosaccharides have molecular formulas that
are usually multiples of CH2O.
• Monosacharides are the basic units within
carbohydrates.
• Glucose is the most common monosaccharide
• 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
The bonds that join monosaccharides to form large
polysaccharides are called glycosidic bonds/linkages
Dehydration
reaction in the
synthesis of maltose
1–4
glycosidic
linkage
Glucose
Glucose
Dehydration
reaction in the
synthesis of sucrose
Maltose
1–2
glycosidic
linkage
Glucose
Fructose
Sucrose
FUNCTION OF CARBOHYDRATES
• Polysaccharides, the polymers of sugars, have
storage and structural functions. (when an
organism wants to store carbs, it stores them in
the form of polysaccharides)
Starch granules
in a potato tuber cell
Starch (amylose)
Glucose
monomer
Glycogen granules
in muscle
tissue
Cellulose microfibrils
in a plant cell wall
Cellulose
molecules
Glycogen
Cellulose
Hydrogen bonds
between —OH groups
(not shown) attached to
carbons 3 and 6
Storage Polysaccharides
• Starch, a storage polysaccharide of plants,
consists entirely of glucose monomers
• Plants store surplus starch as granules within
chloroplasts and other plastids
Chloroplast
Starch
1 µm
Amylose
Amylopectin
Starch: a plant polysaccharide
• Glycogen is a storage polysaccharide in animals
• Humans and other vertebrates store glycogen
mainly in liver and muscle cells
Mitochondria Glycogen granules
0.5 µm
Glycogen
Glycogen: an animal polysaccharide
Structural Polysaccharides
• Cellulose is a major component of the tough wall
of plant cells
• Like starch, cellulose is a polymer of glucose, but
the glycosidic linkages differ
• The difference is based on two ring forms for
glucose: alpha () and beta ()
a Glucose
b Glucose
a and b glucose ring structures
Starch: 1–4 linkage of a glucose monomers.
Cellulose: 1–4 linkage of b glucose monomers.
• Polymers with alpha glucose are helical
• Polymers with beta glucose are straight
• In straight structures, H atoms on one strand
can bond with OH groups on other strands
• Parallel cellulose molecules held together
this way are grouped into microfibrils, which
form strong building materials for plants
Cellulose microfibrils
in a plant cell wall
Cell walls
Microfibril
0.5 µm
Plant cells
Cellulose
molecules
 Glucose
monomer
• Enzymes that digest starch by hydrolyzing alpha
linkages can’t 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
END OF CARBOHYDRATES
• NEXT>…… LIPIDS
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 3 main classes of lipids are fats,
phospholipids and steroids
Fats
• Fats are constructed from two types of smaller
molecules: glycerol and fatty acids
• Glycerol is a three-carbon alcohol with a hydroxyl
group attached to each carbon
• A fatty acid consists of a carboxyl group
attached to a long carbon skeleton
Fatty acid
(palmitic acid)
Glycerol
Dehydration reaction in the synthesis of a fat
• In a fat, three fatty acids are each joined to
glycerol by an ester linkage
Ester linkage
Fat molecule (triacylglycerol)
• Fatty acids vary in length (number of carbons) and
in the number and locations of double bonds
• Saturated fatty acids have the maximum number
of hydrogen atoms possible and no double bonds
• Unsaturated fatty acids have one or more
double bonds
(a) Saturated fat
Structural
formula of a
saturated fat
molecule
Space-filling
model of
stearic acid,
a saturated
fatty acid
(b) Unsaturated fat
Structural
formula
of an
unsaturated
fat molecule
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
Saturated fat and fatty acid.
• Fats made from unsaturated fatty acids are called
unsaturated fats
• Plant fats and fish fats are usually unsaturated
• Plant fats and fish fats are liquid at room
temperature and are called oils
Oleic acid
cis double bond
causes bending
Unsaturated fat and fatty acid.
FUNCTION OF FATS
• The major function of fats is energy
storage
Phospholipids
• In a phospholipid, two fatty acids and a
phosphate group (PO43-) are attached to glycerol
• The two fatty acid tails are hydrophobic(waterfearing), but the phosphate group and its
attachments form a hydrophilic (water-loving)
head
Hydrophilic head
Hydrophobic tails
Choline
Phosphate
Glycerol
Fatty acids
(a) Structural formula
Hydrophilic
head
Hydrophobic
tails
(b) Space-filling model
(c) Phospholipid
symbol
(d) Phospholipid
bilayer
• When phospholipids are added to water, they selfassemble into a bilayer, with the hydrophobic tails
pointing toward the interior
• The structure of phospholipids results in a bilayer
(double layer, recall Bio 10th grade)
arrangement found in cell membranes
• Phospholipids are the major component of all cell
membranes
Hydrophilic
head
Hydrophobic
tails
WATER
WATER
Main Function of Phospholipids (2 group of
lipids)
• Phospholipids are the major component of
all cell membranes (used to make cell
membranes)
Steroids (3rd class of lipids)
• Steroids are lipids characterized by a carbon
skeleton consisting of four fused rings
• Cholesterol, an important steroid, is also a
component in animal cell membranes
• Although cholesterol is essential in animals, high
levels in the blood may contribute to
cardiovascular disease
FUNCTIONS OF STEROIDS
-Used in cell membranes too (just like
phospholipids)
-Several hormones are made from steroids.
eg. Testosterone and estrogen sex hormones.
• END OF LIPIDS
• NEXT PROTEINS --- proteins have a ton of
function make sure you know at least 3
functions and be able to give examples of each
function…. The next 2 slides summarize
these… the following 15 or so slides expand on
these functions more.
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
Enzymatic proteins
Defensive proteins
Function: Selective acceleration of
chemical reactions
Function: Protection against disease
Example: Digestive enzymes catalyze the
hydrolysis of bonds in food molecules.
Example: Antibodies inactivate and help
destroy viruses and bacteria.
Antibodies
Enzyme
Virus
Bacterium
Storage proteins
Transport proteins
Function: Storage of amino acids
Function: Transport of substances
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.
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
Ovalbumin
Amino acids
for embryo
Cell membrane
Hormonal proteins
Receptor proteins
Function: Coordination of an organism’s
activities
Function: Response of cell to chemical
stimuli
Example: Insulin, a hormone secreted by
the pancreas, causes other tissues to
take up glucose, thus regulating blood
sugar concentration.
Example: Receptors built into the
membrane of a nerve cell detect signaling
molecules released by other nerve cells.
Receptor
protein
High
blood sugar
Insulin
secreted
Signaling molecules
Normal
blood sugar
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
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.
Myosin
Collagen
Muscle tissue
30 m
Connective tissue 60 m
• 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
(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.
Ovalbumin
Amino acids
for embryo
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
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
Insulin
secreted
Normal
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
Muscle tissue
30 m
Myosin
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(proteins) are polymers of amino
acids
Amino Acid Monomers
• Amino acids are organic molecules with carboxyl
and amino groups (see next slide picture)
• Amino acids differ in their properties due to
differing side chains, called R groups
• Cells use 20 amino acids to make thousands of
proteins (YOU DON’T NEED TO KNOW THE
NAMES OF THESE)
 carbon
Amino
group
Carboxyl
group
Nonpolar side chains; hydrophobic
Side chain
(R group)
Glycine
(Gly or G)
Methionine
(Met or M)
Alanine
(Ala or A)
Valine
(Val or V)
Phenylalanine
(Phe or F)
Leucine
(Leu or L)
Tryptophan
(Trp or W)
Isoleucine
(le or )
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
Basic (positively charged)
Acidic (negatively charged)
Aspartic acid Glutamic acid
(Asp or D)
(Glu or E)
Lysine
(Lys or K)
Arginine
(Arg or R)
Histidine
(His or H)
Amino Acid Polymers
• Amino acids are linked by peptide bonds
• A polypeptide is a polymer of amino acids
• Each polypeptide has a unique linear sequence of
amino acids
Peptide bond
New peptide
bond forming
Side
chains
Backbone
Amino end
(N-terminus)
Peptide
bond
Carboxyl end
(C-terminus)
Protein Conformation and Function
• A functional protein consists of one or more
polypeptides twisted, folded, and coiled into a
unique shape
• The sequence of amino acids determines a
protein’s three-dimensional conformation/shape
• A protein’s conformation/shape determines its
function
• Ribbon models and space-filling models can
depict a protein’s conformation/shape
Antibody protein
Protein from flu virus
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
Secondary
structure
Tertiary
structure
Quaternary
structure
Transthyretin
polypeptide
Transthyretin
protein
 helix
 pleated sheet
• 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
10
5
Amino end
30
35
15
20
25
45
40
50
Primary structure of transthyretin
65
70
55
60
75
80
90
85
95
115
120
110
105
100
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
 pleated sheet
Hydrogen bond
 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
Polypeptide chain
Collagen
 Chains
Hemoglobin
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
Red blood Normal cells are
cell shape full of individual
hemoglobin
molecules, each
carrying oxygen.
10 µm
Red blood
cell shape
Fibers of abnormal
hemoglobin deform
cell into sickle
shape.
Figure 3.22
Sickle-cell
Normal
Primary
Structure
1
2
3
4
5
6
7
1
2
3
4
5
6
7
Secondary
and Tertiary
Structures
Quaternary
Structure
Function
Normal
hemoglobin
 subunit

Molecules do not
associate with one
another; each carries
oxygen.


5 m

Exposed hydrophobic region
Sickle-cell
hemoglobin

 subunit

Red Blood Cell
Shape
Molecules crystallized
into a fiber; capacity to
carry oxygen is reduced.


5 m
Denaturation
Normal protein
Denatured protein
Renaturation
END OF PROTEINS
START NUCLEIC ACIDS
The Roles of Nucleic Acids
• There are two types of nucleic acids:
– Deoxyribonucleic acid (DNA)
– Ribonucleic acid (RNA)
• DNA directs synthesis of messenger RNA (mRNA)
and, through mRNA, controls protein synthesis
• Protein synthesis occurs in ribosomes
DNA
10th
Tbt
grade
Biology
Synthesis of
mRNA in the nucleus
mRNA
NUCLEUS
CYTOPLASM
mRNA
Movement of
mRNA into cytoplasm
via nuclear pore
Ribosome
Synthesis
of protein
Polypeptide
Amino
acids
The Structure of Nucleic Acids
• Nucleic acids are polymers made of monomers
called nucleotides
• Each nucleotide consists of a nitrogenous base,
a pentose sugar and a phosphate group
5 end
Sugar-phosphate backbone
(on blue background)
Nitrogenous bases
Pyrimidines
5C
3C
Nucleoside
Nitrogenous
base
Cytosine (C)
Thymine
(T, in DNA)
Uracil
(U, in RNA)
Purines
5C
Phosphate
group
3C
Sugar
(pentose)
Adenine (A)
Guanine (G)
(b) Nucleotide
3 end
Sugars
(a) Polynucleotide, or nucleic acid
Deoxyribose (in DNA)
(c) Nucleoside components
Ribose (in RNA)
5 end
Nucleoside
Nitrogenous
base
Phosphate
group
Nucleotide
3 end
Polynucleotide, or
nucleic acid
Pentose
sugar
5
3
3
5
Sugar-phosphate
backbones
Hydrogen bonds
Base pair joined
by hydrogen bonding
Nucleotide Monomers
• A Nucleotide monomer is made up of a BASE, A
SUGAR and a PHOSPHATE GROUP
• In DNA, the sugar is deoxyribose
• In RNA, the sugar is ribose
Nitrogenous bases
Pyrimidines
Cytosine
C
Thymine (in DNA) Uracil (in RNA)
U
T
Purines
Adenine
A
Guanine
G
Pentose sugars
Deoxyribose (in DNA)
Nucleoside components
Ribose (in RNA)
The DNA Double Helix
• A DNA molecule has two polynucleotides chains
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
Base pair (joined by
hydrogen bonding)
Old strands
Nucleotide
about to be
added to a
new strand
5 end
New
strands
5 end
3 end
5 end
3 end
DNA and Proteins as Tape Measures of Evolution
• The linear sequences of nucleotides in DNA
molecules (genes) are passed from parents to
offspring
• Two closely related species are more similar in
DNA than are more distantly related species
• Molecular biology can be used to assess
evolutionary kinship
SUMMARY OF BIOMOLECULES
RATES OF BIOCHEMICAL REACTIONS
1. The rate of a chemical reaction is measured by
• how fast products are being formed
• How fast reactants are being used
2. Many factors affect how quickly a chemical reaction may happen.
a. the initial concentration of reactants
b. The surface area of reactants
c. Temperature of the reaction mixure
d. Presence of a catalyst (they lower the Ea activation
energy of the reaction)
3. A catalyst is a substance that speeds up a reaction and remains
unchanged after the reaction (it is neither a reactant nor product.
You should feel confident in explaining any of the factors
affecting the rate of chemical reactions USING
COLLISION THEORY