Cecie Starr

Christine Evers
Lisa Starr
www.cengage.com/biology/starr

Chapter 3
Molecules of Life
(Sections 3.4 - 3.6)

Albia Dugger Miami Dade College

3.4 Lipids
Cells use lipids as major sources of energy and as structural
materials
lipid
Fatty, oily, or waxy organic compound
All are hydrophobic (nonpolar )

Types of Lipids
Fats and some other lipids have fatty acid tails;
triglycerides have three
Phospholipids are the main structural component of cell
membranes
Waxes are lipids that are part of water-repellent and
lubricating secretions
Steroids occur in cell membranes, and some are remodeled
into other molecules

Key Terms
fat
Lipid that consists of a glycerol molecule with one, two, or
three fatty acid tails
triglyceride
A fat with three fatty acid tails
fatty acid
Organic compound that consists of a chain of carbon
atoms with an acidic carboxyl group at one end
Carbon chain of saturated types has single bonds only;
that of unsaturated types has one or more double bonds

Fats and Fatty Acids

Unsaturated fatty acids have one or more double bonds that
limit their flexibility
These bonds are termed cis or trans, depending on the way
the hydrogens are arranged around them
A cis bond kinks the tail, and a trans bond keeps it straight

Saturated and Unsaturated Fats

Animal fats are saturated
Tend to remain solid at room temperature because their
saturated tails pack tightly together
Most vegetable oils are unsaturated
Kinked tails do not pack tightly, so unsaturated fats are
typically liquid at room temperature
Partially hydrogenated vegetable oils have a trans double
bond that allows them to pack tightly, like saturated fats
Solid at room temperature

Fatty Acids

carboxyl group
(head)

hydro carbon
tail

A stearic acid

B linoleic acid

C linolenic acid
Fig. 3.8, p. 42

Trans and Cis

Phospholipids
phospholipid
Lipid with a highly polar phosphate group in its hydrophilic
head, and two nonpolar, hydrophobic fatty-acid tails
Main constituent of eukaryotic cell membranes
Opposing properties of a phospholipid molecule give rise to
cell membrane structure
Two layers of lipids (lipid bilayer)
Hydrophobic tails sandwiched between hydrophilic heads

Phospholipids and Cell Membranes

Head is hydrophilic
tails are hydrophobic
Lipid bilayer the
structural foundation of
all cell membranes

hydrophilic
head

one layer
of lipids
one layer
of lipids

two hydrophobic
tails

Fig. 3.10, p. 42

Waxes
wax
Water-repellent mixture
with long fatty-acid tails
bonded to long-chain
alcohols or carbon rings

Functions:
Covers exposed surfaces
of plants
Protects and lubricates
skin and hair
Honeycomb

Steroids
steroid
Lipid with four carbon rings and no fatty acid tails
Found in all eukaryotic cell membranes
Cholesterol, the most common steroid in animal tissue, is
remodeled into many molecules:
Bile salts (which help digest fats) and vitamin D
Steroid hormones (estrogens and testosterone)

Estrogen and Testosterone

Estrogen and
testosterone
Steroid hormones
derived from
cholesterol

Steroid Functions

Steroid hormones
cause different traits to
arise in males and
females of many
species, such as wood
ducks (Aix sponsa)

Key Concepts
Lipids
Lipids function as energy reservoirs and as waterproofing
or lubricating substances
Some are remodeled into other compounds such as
vitamins
Lipids are the main structural component of all cell
membranes

Animation: Fatty acids

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Animation 2.2: Triglyceride formation

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3.5 Proteins
Diversity in Structure and Function
Structurally and functionally, proteins are the most diverse
molecules of life
The shape of a protein is the source of its function
protein
Organic compound that consists of one or more chains of
amino acids (polypeptides)

Amino Acids
Cells make thousands of different kinds of proteins from only
twenty kinds of monomers (amino acids)
amino acid
Small organic compound that is a subunit of proteins
Consists of a carboxyl group, an amine group, and a
characteristic side group (R), all typically bonded to the
same carbon atom

Amino Acids

Generalized structure of amino acids: Twenty amino acids

are used in eukaryotic proteins

Amino Acids

Stepped Art
Fig. 3.12, p. 44

Building Proteins
Protein synthesis involves covalently bonding amino acids
into a chain polypeptide linked by peptide bonds
polypeptide
Chain of amino acids linked by peptide bonds
Primary structure of a protein
peptide bond
Bond that joins the amine group of one amino acid and the
carboxyl group of another in a protein

Polypeptide Formation

Condensation: A peptide bond forms between the carboxyl

group of the methionine and the amine group of the serine
Additional amino acids are added to the carboxyl end

Polypeptide Formation

methionineserine

arginineglutamine

serine

methionine

methionine

serine

Stepped Art
Fig. 3.13, p. 44

Animation: Peptide bond formation

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Protein Structure
Polypeptides (primary structure) twist into loops, sheets, and
coils (secondary structure) that can pack further into
functional domains (tertiary structure)
Many proteins, including most enzymes, consist of two or
more polypeptides (quaternary structure)
Fibrous proteins aggregate into much larger structures

Primary and Secondary Structure

Primary structure (polypeptide) twists into secondary structure

Tertiary and Quaternary Structure

Tertiary structure forms functional domains

Hemoglobin has quaternary structure (4 globin chains)

Aggregate Proteins

Many proteins aggregate by thousands into much larger

structures, such as keratin filaments that make up hair

Polypeptide Formation
lysine

glycine

A proteins primary
structure consists of a
linear sequence of
amino acids (a
polypeptide chain).
Each type of protein
has a unique primary
structure.
1

arginine

glycine

2 Secondary structure

arises as a polypeptide
chain twists into a coil
(helix) or sheet held in
place by hydrogen
bonds between different
parts of the molecule.
The same patterns of
secondary structure
occur in many different
proteins.

3 Tertiary structure

occurs when a chains

coils and sheets fold
up into a functional
domain such as a
barrel or pocket. In
this example, the coils
of a globin chain form
a pocket.

Many proteins aggregate

by the thousands into much
larger structures, such as the
keratin filaments that make
up hair.

4 Some proteins have

quaternary structure, in
which two or more
polypeptide chains
associate as one
molecule. Hemoglobin,
shown here, consists of
four globin chains (green
and blue). Each globin
pocket now holds a heme
group (red).

Stepped Art
Fig. 3.14.1-4, p. 45

Animation: Secondary and tertiary structure

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Combined Proteins
Enzymes often attach sugars or lipids to proteins
Glycoproteins allow a tissue or body to recognize its own cells
Lipoproteins carry fats and cholesterol through the
bloodstream
Low-density lipoprotein (LDL)
High-density lipoprotein (HDL)

3.6 Importance of Protein Structure

A proteins structure dictates its function so, if a protein
unravels (denatures), it loses its function
denature
To unravel the shape of a protein or other large biological
molecule
Caused by shifts in pH or temperature, exposure to
detergent or some salts that disrupt hydrogen bonds, and
other molecular interactions responsible for protein shape

Prions
Prion diseases, are the result of misfolded proteins
Mad cow disease (bovine spongiform encephalitis, BSE)
CreutzfeldtJakob disease (vCJD) in humans
Scrapie in sheep
prion
Infectious protein
Misfolded PrPC protein

PrPC Protein Becomes a Prion

The PrPC protein misfolds into an unknown conformation

Prions cause other PrPC proteins to misfold
Misfolded proteins aggregate into long fibers

Conformational
change
?

PrPC
protein

prion
protein

Fig. 3.16, p. 46

Variant CreutzfeldtJakob Disease

Charlene Singh:
Diagnosed in 2001
Died in 2004

Brain tissue shows

characteristic holes and
prion protein fibers
radiating from several
deposits

Key Concepts

Proteins
Structurally and functionally, proteins are the most diverse
molecules of life
They include enzymes and structural materials
A proteins function arises from and depends on its
structure

ANIMATION: Globin and hemoglobin

structure

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ANIMATION: Sickle-Cell Anemia

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3.7 Nucleic Acids

Nucleotides are small organic molecules consisting of a

sugar, a phosphate group, and a nitrogen-containing base
nucleotide
Monomer of nucleic acids; has five-carbon sugar, nitrogencontaining base, and phosphate groups

A Nucleotide Monomer

ATP, a nucleotide monomer of RNA, and also an essential

participant in many metabolic processes

Nucleic Acids

Nucleotides are monomers of DNA and RNA, which are

nucleic acids
nucleic acid
Single- or double-stranded chain of nucleotides joined by
sugarphosphate bonds; for example, DNA, RNA

A Nucleic Acid
A chain of nucleotides is
a nucleic acid
The sugar of one
nucleotide is covalently
bonded to the
phosphate group of the
next, forming a sugar
phosphate backbone

ANIMATION: Nucleotide Subunits of DNA

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DNA and RNA

DNA (Deoxyribonucleic acid)
DNA encodes heritable information that guides the
synthesis of RNA and proteins
Consists of two nucleotide chains twisted in a double helix
RNA (Ribonucleic acid)
RNAs interact with DNA and with one another to carry out
protein synthesis

DNA

DNA consists of two

chains of nucleotides,
twisted into a double
helix
Hydrogen bonding
maintains the threedimensional structure

Other Nucleotides
Some nucleotides have additional functions
Example: ATP energizes many kinds of molecules by
phosphate-group transfers
ATP Adenosine triphosphate
Nucleotide that consists of an adenine base, a five-carbon
ribose sugar, and three phosphate groups

Key Concepts

Nucleic Acids
Nucleotides are the building blocks of nucleic acids
Some have additional roles in metabolism
DNA and RNA are part of a cells system of storing and
retrieving heritable information

Fear of Frying (revisited)

Trans fatty acids are rare in unprocessed foods

Enzymes that hydrolyze cis fatty acids have difficulty breaking
down trans fatty acids, a problem that may be a factor in the ill
effects of trans fats on our health