Lecture Series 2
Macromolecules: Their
Structure and Function
Reading Assignments
• Read Chapter 4
(Protein structure & Function)
Biological Substances found in Living Tissues
The big four in terms of macromolecules
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A. Lipids: Water-
Water-Insoluble
Molecules
• Lipids can form large biological molecules,
molecules
but these aggregations are NOT
chemically polymers because individual
units are not linked by covalent bonds.
• Share the common trait of being
hydrophobic.
The role of hydrocarbons in fats
A. Lipids: Water-
Water-Insoluble
Molecules
• Fats and oils are composed of three fatty
acids covalently bonded to a glycerol
molecule by ester linkages.
• Fats and oils function to efficiently store
energy.
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Synthesis of a Triglyceride
A. Lipids: Water-
Water-Insoluble
Molecules
• Saturated fatty acids have a hydrocarbon
chain with no double bonds. The
hydrocarbon chains of unsaturated fatty
acids have one or more double bonds that
bend the chain, making close packing less
possible.
Saturated and Unsaturated Fatty Acids
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Examples of saturated and unsaturated fats and fatty acids
A. Lipids: Water-
Water-Insoluble
Molecules
• Phospholipids have a hydrophobic
hydrocarbon “tail” and a hydrophilic
phosphate “head.”
• Phospholipids form the core of biological
membranes.
Phospholipid Structure
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A. Lipids: Water-
Water-Insoluble
Molecules
• In water, the interactions of the
hydrophobic tails and hydrophilic heads
generate a phospholipid bilayer two
molecules thick. The head groups are
directed outward, interacting with
surrounding water. Tails are packed in the
interior.
Phospholipids form a Bilayer
Phospholipid
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A. Lipids: Water-
Water-Insoluble
Molecules
• Carotenoids trap light energy in green
plants. β-Carotene can be split to form
vitamin A, a lipid vitamin.
Example of an Important Lipid
A. Lipids: Water-
Water-Insoluble
Molecules
• Some lipids are steroids and function as
hormones. Cholesterol is synthesized by
the liver and has a role in some cell
membranes, as well as in the digestion of
other fats.
• Some lipids function as vitamins, required
for normal functioning, must be acquired
from the diet.
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Examples of an Important Lipids that are also Steroids
B. Macromolecules: Giant
Polymers
• Macromolecules have specific three-
dimensional shapes. Different functional
groups give local sites on macromolecules
specific properties.
• Monomers are joined by condensation
reactions. Hydrolysis reactions break
polymers into monomers.
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The synthesis and breakdown of polymers
Condensation or
Dehydration reactions
Hydrolysis reactions
The synthesis and structure of a fat, or triacylglycerol
C. Carbohydrates: Sugars and
Sugar Polymers
• All carbohydrates contain carbon bonded
to H and OH groups. [CH2O]N
• Hexoses are monosaccharides that
contain six carbon atoms.
• Monosaccharides are simple sugars.
Can be used for fuel.
Can be converted into other organic
molecules.
Can be combined into polymers.
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Various forms of Glucose
May be linear, but can form rings.
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Hexose sugars
Glucose Galactose
Alpha or Beta???
C. Carbohydrates: Sugars and
Sugar Polymers
• Glycosidic linkages may have either α or β
orientation in space. They covalently link
monosaccharides into larger units.
Examples of disaccharide synthesis
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Glucose monomer and disaccharides
Glucose monomer
Sucrose
Maltose
C. Carbohydrates: Sugars and
Sugar Polymers
• Cellulose, a polymer, is formed by glucose
units linked by β-glycosidic linkages
between carbons 1 and 4.
Glycosidic Linkages
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The arrangement of cellulose in plant cell walls
• Cellulose is difficult to digest
Cows have microbes in their stomachs to
facilitate this process
C. Carbohydrates: Sugars and
Sugar Polymers
• Starches are formed by α-glycosidic linkages
between carbons 1 and 4 and are distinguished
by amount of branching through glycosidic
bond formation at carbon 6.
• Glycogen contains α-1,4 glycosidic linkages and
is highly branched.
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Glycosidic Linkages
Storage polysaccharides
Starch and cellulose molecular models
α Glucose β Glucose
Cellulose
Starch
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C. Carbohydrates: Sugars and
Sugar Polymers
• Chemically modified monosaccharides
include the sugar phosphates and amino
sugars. A derivative of the amino sugar
glucosamine polymerizes to form the
polysaccharide chitin.
Modified Sugars
• Chitin, another important structural
polysaccharide
Is found in the exoskeleton of arthropods
Can be used as surgical thread
Chitin forms the exoskeleton Chitin is used to make a
of arthropods. This cicada strong and flexible surgical
is molting, shedding its old thread that decomposes after
exoskeleton and emerging the wound or incision heals.
in adult form.
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D. Nucleic Acids: Informational
Macromolecules
• In cells, DNA is the hereditary material.
DNA and RNA play roles in protein
formation.
D. Nucleic Acids: Informational
Macromolecules
• Nucleic acids are polymers of nucleotides
consisting of a phosphate group, a sugar,
and a nitrogen-containing base. The DNA
bases are adenine, guanine, cytosine, and
thymine. In RNA uracil substitutes for
thymine and ribose substitutes for
deoxyribose.
Nucleotides have three parts
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D. Nucleic Acids: Informational
Macromolecules
• In the nucleic acids, bases extend from a
sugar–phosphate backbone using the
phosphodiester linkage.
• DNA and RNA information resides in
their base sequences.
D. Nucleic Acids: Informational
Macromolecules
• RNA is single-stranded.
• DNA is a double-stranded helix with
complementary, hydrogen-bonded base
pairing between adenine and thymine and
guanine and cytosine. The two strands run
in opposite 5’ to 3’ directions.
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DNA structure: The double helix
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D. Nucleic Acids: Informational
Macromolecules
• Comparing the DNA base sequences of
different living species provides
information on evolutionary relatedness.
• This is called molecular phylogeny.
E. Proteins: Amazing Polymers of
Amino Acids
• Functions of proteins include support,
protection, catalysis, transport, defense,
regulation, and movement. They sometimes
require an attached prosthetic group.
• Twenty amino acids are found in proteins.
Each consists of an amino group, a carboxyl
group, a hydrogen, and a side chain bonded
to the α carbon atom.
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E. Proteins: Amazing Polymers of
Amino Acids
• Side chains of amino acids may be
charged, polar, or hydrophobic. SH groups
can form disulfide bridges.
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Cysteine residues can
form a covalently
linked disulfide bridge
E. Proteins: Amazing Polymers of
Amino Acids
• Amino acids are covalently bonded
together by peptide linkages.
α carbon
R
H O
N C C
H OH
H
Amino Carboxyl
group group
Making a polypeptide chain
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E. Proteins: Amazing Polymers of
Amino Acids
• Polypeptide chains of proteins are folded
into specific three-dimensional shapes.
Primary, secondary, tertiary, and
quaternary structures are possible.
E. Proteins: Amazing Polymers of
Amino Acids
• The primary structure of a protein is the
sequence of amino acids bonded by
peptide linkages.
• Secondary structures are maintained by
hydrogen bonds between atoms of the
amino acid residues.
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Abdominal glands of the
spider secrete silk fibers
that form the web
The radiating strands, made
of dry silk fibers maintained
the shape of the web
The spiral strands (capture
strands) are elastic, stretching
in response to wind, rain,
and the touch of insects
Spider silk: a structural protein
containing β pleated sheets
E. Proteins: Amazing Polymers of
Amino Acids
• The tertiary structure is generated by
bending and folding of the polypeptide
chain. This results
esults from interactions
between amino acids and R groups.
• The quaternary structure is the
arrangement of polypeptides in a single
functional unit consisting of more than
one polypeptide subunit.
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Quaternary Structure
Domains
Catabolite
Activator
Protein
E. Proteins: Amazing Polymers of
Amino Acids
• Weak chemical interactions are important
in the binding of proteins to other
molecules.
• Any molecule that binds to a protein is
called a ligand (e.g., antibodies to
antigens).
• Proteins denatured by heat, acid, or
chemicals lose tertiary and possibly
secondary structure and lose biological
function.
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Noncovalent interactions
can occur between proteins
and other molecules
Extreme Diversity
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Antibodies
Denaturation is the loss of Tertiary Structure and Function
E. Proteins: Amazing Polymers of
Amino Acids
• Chaperonins assist protein folding by
preventing binding to inappropriate
ligands.
• They also help to shape proteins with
special needs regarding hydrophobic and
hydrophilic interactions.
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Chaperonins aid in Folding through Protection
Binding to specific ligands
Prion diseases
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F. The Interactions with other
Macromolecules
• Glycoproteins contain an oligosaccharide
“label” that directs the protein to the
proper cell destination. The carbohydrate
groups of glycolipids are on the cell’s
outer surface, serving as recognition
signals.
• An example of emergent properties
where greater complexity is exhibited.
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