Overview: The Molecules of
Life
• All living things are made up of
four classes of large biological
molecules:
– Carbohydrates
– Lipids
– Proteins
– nucleic acids
1
Proteins
• Proteins are macromolecules
(polymers) of monomers called
amino acids
• Proteins account for more than 50%
of the dry mass of most cells
2
Polypeptides
• A polypeptide
– Is an unbranched polymer (chain) of
amino acids
– Range in length from a few to more
than a thousand monomers
– Has a unique linear sequence of
amino acids, with a carboxyl end
(C-terminus) and an amino end (N-
terminus)
3
Proteins
• A protein is
– A functional biological macromolecule
consisting of one or more polypeptides
folded into specific conformations.
4
Proteins
• Proteins have many structures,
resulting in a wide range of
functions.
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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
Enzyme Virus Bacterium
Storage proteins Transport proteins
Function: Storage of amino acids Function: Transport of substances
Examples: Casein, the protein of milk, is Examples: Hemoglobin, the iron-containing
the major source of amino acids for baby protein of vertebrate blood, transports
mammals. Plants have storage proteins in oxygen from the lungs to other parts of the
their seeds. Ovalbumin is the protein of body. Other proteins transport molecules
egg white, used as an amino acid source across membranes, as shown here.
for the developing embryo.
Transport
protein
Ovalbumin Amino acids
for embryo Cell membrane
Hormonal proteins Receptor proteins
Function: Coordination of an organism’s Function: Responses of cells to chemical
activities stimuli
Example: Insulin, a hormone secreted by Example: Receptors built into the
the pancreas, causes other tissues to take membrane of a nerve cell detect signaling
up glucose, thus regulating blood sugar molecules released by other nerve cells.
concentration.
Receptor
protein
High Insulin Normal Signaling
blood sugar secreted blood sugar molecules
Contractile and motor proteins Structural proteins
Function: Movement Function: Support
Examples: Motor proteins are responsible Examples: Keratin is the protein of hair,
for the undulations of cilia and flagella. horns, feathers, and other skin appendages.
Actin and myosin proteins are responsible Insects and spiders use silk fibers to make
for the contraction of muscles. their cocoons and webs, respectively.
Collagen and elastin proteins provide a
fibrous framework in animal connective
Actin Myosin tissues.
Collagen
Muscle
30 µm
tissue Connective
60 µm
tissue
• Amino acids
– Are organic molecules possessing both
carboxyl and amino groups
– Differ in their properties due to differing side
chains, called R groups
Side chain (R group)
α carbon
Amino Carboxyl
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group group
Figure 5.14a
Nonpolar side chains; hydrophobic
Side chain (R group)
Glycine Alanine Valine Leucine Isoleucine
(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)
Methionine Phenylalanine Tryptophan Proline
(Met or M) (Phe or F) (Trp or W) (Pro or P)
Figure 5.14b
Polar side chains; hydrophilic
Serine Threonine Cysteine
(Ser or S) (Thr or T) (Cys or C)
Tyrosine Asparagine Glutamine
(Tyr or Y) (Asn or N) (Gln or Q)
Figure 5.14c
Electrically charged side chains; hydrophilic
Basic (positively charged)
Acidic (negatively charged)
Aspartic acid Glutamic acid Lysine Arginine Histidine
(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)
The Synthesis &
Breakdown of
Proteins
Polypeptides (Amino Acid
Polymers)
• Amino acids are linked by covalent
bonds called peptide bonds
© 2017 Pearson Education, Inc.
Figure 5.15
Peptide bond
H2O
New peptide
bond forming
Side
chains
Back-
bone
Amino end Peptide Carboxyl end
(N-terminus) bond (C-terminus)
Four Levels of Protein Structure
(1) Primary structure
(2) Secondary structure
(3) Tertiary structure
(4) Quaternary structure
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(1) Primary structure
• Is the protein’s linear sequence of
amino acids
• It is like the order of letters in a long
word
• Determined by inherited genetic
information
© 2017 Pearson Education, Inc.
Primary Structure
Amino
acids
1 5 10
Amino end
30 25 20 15
35 40 45 50
Primary structure of transthyretin
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70 65 60
75
80 85 90
95
115 110 105 100
120 125
Carboxyl end
(2) Secondary structure
– Is the coiling or folding of the polypeptide into a
repeating configuration (coils and folds)
– Includes the helix and the pleated sheet
(example: Keratin, a structural protein of hair)
– Results from hydrogen bonds between repeating
constituents of the polypeptide
pleated sheet
O H H O H H O H H O H H
R
Amino acid C C N R C C N R C C N C C N
C N C C N C C N C C N C C
subunits R R R R
H O H H OH H OH H O
R R R R
O C O O C O H
C H H H C
H H
C N HC N H C N H C N C NH C N C N HC N
H H C H C H
C O C O O O C
R R R
R H R H
C C
N H O C N H O C
N H N H
O C O C helix
H C R H C H C R H C R
R
N H O C N H
OH C
H
O C N H O C N H
C C
R
R 18
Secondary Structure
α helix
Hydrogen bond
β strand
Hydrogen
bond
β pleated sheet
(3) Tertiary structure
– Is the three-dimensional shape of a
polypeptide
– Results from interactions between the side
chains (R groups) of the various amino acids,
rather than interactions between backbone
constituents.
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Tertiary Structure
α helix
β pleated sheet
Transthyretin
polypeptide
How can the tertiary structure be stabilized?
A. Hydrophobic and van der Waals interactions
formed between hydrophobic (non-polar) side
chains
B. H-bonds: formed between polar side chains
C. Ionic bonds: formed between charged side
Hydrophobic
chains interactions and
van der Waals
A + B + C are relatively CH
CH
H C
CH
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CH interactions
3
O 3
weak bonds Hyrdogen H H C CH 3 Polypeptide
3
bond O CH backbone
HO C
CH2 CH2 S S CH2
Disulfide bridge
O
CH2 NH3+-O C CH2
Ionic bond
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How can the tertiary structure be stabilized?
D. Disulfide bridges: Covalent bonding formed
where 2 cysteine monomers (amino acids with
sulfhydryl groups) gets close to each other by
folding of the protein.
Hydrophobic
interactions and
van der Waals
CH2 CH
CH 2
H 3C
interactions
CH3
O
Hyrdogen H H 3C CH3 Polypeptide
bond O CH backbone
HO C
CH2 CH2 S S CH2
Disulfide bridge
O
CH2 NH3+ -O C CH2
Ionic bond
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Hydrogen
bond
Hydrophobic
interactions and
van der Waals
interactions
Disulfide
bridge Ionic bond
Polypeptide
backbone
(4) Quaternary structure
– Results when two or more polypeptide
chains form one functional macromolecule.
- The polypeptide chains may be identical as
in Collagen (a fibrous protein) or different as
in Hemoglobin (a globular protein).
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Fig. 5-21g
Polypeptide Chains
chain
Iron
Heme
Chains
Hemoglobin
Collagen
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Heme
Iron
β subunit
α subunit
α subunit
β subunit
Hemoglobin
Primary Secondary Tertiary Quaternary
Structure Structure Structure Structure
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• What will happen if a single
amino acid in a protein is
either omitted or substituted?
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