Lipids

• Lipids are the one class of large biological

molecules that do not form polymers
• Lipids are hydrophobic because they consist
mostly of hydrocarbons, which form nonpolar
covalent bonds - The unifying feature of lipids is having little or no affinity for water
• The most biologically important lipids are fats,
phospholipids, and steroids

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Fats
• Fats are constructed Fatty acid
from two types of (in this case, palmitic acid)

smaller molecules:
glycerol and fatty Glycerol
acids (a) One of three dehydration reactions in the synthesis of a fat
• Glycerol is a three-
Ester linkage
carbon alcohol with a
hydroxyl group
attached to each
carbon
• A fatty acid consists
of a carboxyl group
attached to a long
carbon skeleton

• Storage at adipose (b) Fat molecule (triacylglycerol) / triglyceride

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 (a) Saturated fat
• Fatty acids vary in
length (number of
carbons) and in the
number and locations of
double bonds

Structural
• Saturated fatty acids formula of a
have the maximum saturated fat
molecule
number of hydrogen
atoms possible and no
double bonds

• Unsaturated fatty
acids have one or more
double bonds Space-filling
model of stearic
acid, a saturated
fatty acid
 (b) Unsaturated fat

• Fats made from

saturated fatty acids are
called saturated fats, and
are solid at room
temperature
• Most animal fats are
saturated
• Fats made from Structural
formula of an
unsaturated fatty acids
unsaturated fat
are called unsaturated molecule
fats or oils, and are liquid
at room temperature
• Plant fats and fish fats
are usually unsaturated Space-filling model
of oleic acid, an
unsaturated fatty
acid
Cis double bond
causes bending.
Phospholipids • In a phospholipid, two
fatty acids and a
phosphate group are
attached to glycerol
Choline
Hydrophilic head

Phosphate • The two fatty acid tails are

hydrophobic, but the
Glycerol phosphate group and its
attachments form a
hydrophilic head
Hydrophobic tails

Fatty acids

Hydrophilic
head

Hydrophobic
tails

(a) Structural formula (b) Space-filling model (c) Phospholipid symbol

• 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

Hydrophilic WATER
head

Hydrophobic
tail WATER
Steroids
• Steroids are lipids characterized by a carbon skeleton consisting of
four fused rings
• Cholesterol, an important steroid, is a component in animal cell
membranes
• Although cholesterol is essential in animals, high levels in the blood
may contribute to cardiovascular disease

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Proteins
• 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 Example: Antibodies inactivate and help destroy
of bonds in food molecules. viruses and bacteria.

Antibodies

Enzyme Virus Bacterium

Storage proteins Transport 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.
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

Ovalbumin Amino acids

for embryo Cell membrane
Figure 5.15-b

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 Example: Receptors built into the membrane of a
pancreas, causes other tissues to take up glucose, nerve cell detect signaling molecules released by
thus regulating blood sugar concentration other nerve cells.

Receptor
Signaling protein
Insulin
High secreted Normal molecules
blood sugar blood sugar

Contractile and motor proteins Structural 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.
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.

Actin Myosin
Collagen

Muscle tissue Connective

100 m tissue 60 m
 Animation: Structural Proteins
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 Animation: Storage Proteins
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 Animation: Transport Proteins
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 Animation: Receptor Proteins
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 Animation: Contractile Proteins
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 Animation: Defensive Proteins
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 Animation: Hormonal Proteins
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 Animation: Sensory Proteins
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 Animation: Gene Regulatory Proteins
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• Enzymes are a type of protein that acts as a catalyst to speed up
chemical reactions
• Enzymes can perform their functions repeatedly, functioning as
workhorses that carry out the processes of life

Animation: Enzymes
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Polypeptides

• Polypeptides are unbranched polymers built from the same set of

20 amino acids
• A protein is a biologically functional molecule that consists of one or
more polypeptides
Side chain (R group)
Amino Acid Monomers

• Amino acids are organic

 carbon
molecules with carboxyl and
amino groups
• Amino acids differ in their
properties due to differing side
chains, called R groups
Amino Carboxyl
group group
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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)

Polar side chains; hydrophilic

Serine Threonine Cysteine Tyrosine Asparagine Glutamine

(Ser or S) (Thr or T) (Cys or C) (Tyr or Y) (Asn or N) (Gln or Q)

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)
Amino Acid Polymers
• Amino acids are linked
by peptide bonds
• A polypeptide is a
polymer of amino acids
Peptide bond
• Polypeptides range in
length from a few to
New peptide
more than a thousand bond forming
monomers
Side
• Each polypeptide has a chains
unique linear sequence
of amino acids, with a
carboxyl end (C- Back-
terminus) and an amino bone
end (N-terminus)
Amino end Peptide Carboxyl end
(N-terminus) bond (C-terminus)
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Protein Structure and Function
• A functional protein consists of one or more polypeptides
precisely twisted, folded, and coiled into a unique shape

Groove

Groove

(a) A ribbon model (b) A space-filling model

• The sequence of amino acids determines a protein’s three-dimensional

structure
• A protein’s structure determines its function
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 Primary structure

Four Levels of Protein Structure Amino

acids
• The primary structure of a protein is
its unique sequence of amino acids
• Secondary structure, found in most
Amino end
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 Primary structure of transthyretin
protein consists of multiple
polypeptide chains

• 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
Carboxyl end
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Figure 5.20b Secondary Tertiary Quaternary
structure structure structure

 helix

Hydrogen bond
 pleated sheet
 strand
Transthyretin
Hydrogen Transthyretin protein
bond polypeptide

• 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
• Tertiary structure is determined by interactions between R groups, rather than interactions
between backbone constituents
• Quaternary structure results when two or more polypeptide chains form one macromolecule
Sickle-Cell Disease: A Change in Primary
Structure
• A slight change in primary structure can affect
a protein’s structure and ability to function
• Sickle-cell disease, an inherited blood
disorder, results from a single amino acid
substitution in the protein hemoglobin

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Figure 5.21

Primary Secondary Quaternary Red Blood

and Tertiary Function
Structure Structure Cell Shape
Structures

1 Normal Molecules do not

hemoglobin associate with one
Normal hemoglobin

2 another; each carries

3 oxygen.
4
5 
 subunit  10 m
6
7



1 Exposed Sickle-cell Molecules crystallize

hydrophobic hemoglobin into a fiber; capacity
Sickle-cell hemoglobin

2 region to carry oxygen is

3 reduced.
4
5 
6  10 m
7  subunit


What Determines Protein Structure?
• In addition to primary structure, physical and chemical conditions can affect
structure
• Alterations in pH, salt concentration, temperature, or other environmental factors
can cause a protein to unravel
• This loss of a protein’s native structure is called denaturation
• A denatured protein is biologically inactive

tu

Normal protein Denatured protein

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Protein Folding in the Cell
• It is hard to predict a protein’s structure from its primary structure
• Most proteins probably go through several stages on their way to a stable structure
• Chaperonins are protein molecules that assist the proper folding of other proteins
• Diseases such as Alzheimer’s, Parkinson’s, and mad cow disease are associated with
misfolded proteins

Correctly
folded
protein
Polypeptide
Cap

Hollow
cylinder

Chaperonin Steps of Chaperonin 2 The cap attaches, causing 3 The cap comes
(fully assembled) Action: the cylinder to change off, and the
1 An unfolded poly- shape in such a way that properly folded
peptide enters the it creates a hydrophilic protein is
cylinder from environment for the released.
one end. folding of the polypeptide.
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 EXPERIMENT
Diffracted
X-rays
• Scientists use X-ray
crystallography to
X-ray
determine a protein’s source X-ray
structure beam

Crystal Digital detector X-ray diffraction

• Another method is pattern
nuclear magnetic
RESULTS
resonance (NMR)
spectroscopy, which RNA DNA
does not require
protein crystallization

• Bioinformatics uses
computer programs to
predict protein
structure from amino
acid sequences RNA
polymerase II
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Nucleic acids

• Nucleic acids store, transmit, and help

express 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
made of monomers called nucleotides

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 DNA
The Roles of
Nucleic Acids 1 Synthesis of
mRNA
• There are two types of mRNA
nucleic acids
– Deoxyribonucleic
acid (DNA) NUCLEUS
– Ribonucleic acid CYTOPLASM
(RNA)
• DNA provides directions mRNA
for its own replication 2 Movement of
• DNA directs synthesis of mRNA into Ribosome
messenger RNA (mRNA) cytoplasm
and, through mRNA,
controls protein synthesis 3 Synthesis
• Protein synthesis occurs of protein
on ribosomes
Amino
Polypeptide acids
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 Sugar-phosphate backbone
5 end
5C

3C

The Components: Nucleoside

Nucleic acids
Nitrogenous
are polymers base
called
polynucleoti
des 5C
Each
polynucleotid
e is made of 1C
monomers
called Phosphate 3C
nucleotides 5C group Sugar
(pentose)
3C (b) Nucleotide

3 end
(a) Polynucleotide, or nucleic acid
Figure 5.26c

Nitrogenous bases
Pyrimidines

Cytosine Thymine Uracil

(C) (T, in DNA) (U, in RNA)
Sugars
Purines

Deoxyribose Ribose
Adenine (A) Guanine (G) (in DNA) (in RNA)

(c) Nucleoside components

The Structures of DNA and RNA Molecules
5 3 Sugar-phosphate
backbones
Hydrogen bonds

Base pair joined

by hydrogen
bonding

3 5 Base pair joined

by hydrogen bonding
(a) DNA (b) Transfer RNA

•antiparallel
•double helix
DNA and Proteins as Tape Measures of
Evolution
• The linear sequences of nucleotides in DNA
molecules 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

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