Topic 1 Biological Molecules Part 2 S

TENTH EDITION
Global Edition
Campbell Reece Urry Cain Wasserman Minorsky Jackson
Topic 1 Biological
Topic 1 Biological Molecules
(Part 2)
Molecules
(part 2)
Biological Macromolecules
Lecture Presentation by
Nicole Tunbridge and
Kathleen Fitzpatrick
2015 Pearson Education, Inc.
LIPIDS
Water beading on the oily coating of

feathers
2015 Pearson Education Ltd
ydrocarbons
a) Hydrocarbons = organic molecules consisting of only carbon

and hydrogen
b) Many organic molecules, such as fats, have hydrocarbon
components
c) Hydrocarbons can undergo reactions that release a large amount
of energy
Nucleus
Fat droplets
10 m
(a) Part of a human adipose cell
2011 Pearson Eduation, Inc.
(b) A fat molecule
Black = carbon
Gray = hydrogen
oncept 5.3: Lipids are a diverse group of hydrophobic

molecules
a) Lipids are the one class of large biological molecules
that does not include true polymers
b) The unifying feature of lipids is that they mix poorly, if
at all, with water
c) Lipids are hydrophobic because they consist mostly
of hydrocarbons, which form nonpolar covalent bonds
d) The most biologically important lipids are fats,
phospholipids, and steroids
ats
a) Fats are constructed from two types of smaller
molecules: glycerol and fatty acids
b) Glycerol is a three-carbon alcohol with a hydroxyl
group attached to each carbon
c) A fatty acid consists of a carboxyl group attached to
a long carbon skeleton
Figure 5.9a
aCOOHgroupattachedtoalongcarbonskeleton
H2O
Fatty acid
(in this case, palmitic acid)
threecarbonalcoholwithaOHgroupattachedtoeachcarbon
Glycerol
(a) One of three __________reactions in the synthesis of a fat
a)Fats separate from water because water molecules

hydrogen-bond to each other and exclude the fats
b)In a fat, three fatty acids are joined to glycerol
by an ester linkage, creating a triacylglycerol,
or triglyceride
c)The fatty acids in a fat can be all the same or of
two or three different kinds
Figure 5.9b
Whatlinkageisthis?
Whatisthenameofthisfatmolecule?
a) Fatty acids vary in length (number of carbons) and in

the number and locations of double bonds
b) Saturated fatty acids have the maximum number of
hydrogen atoms possible and no double bonds
c) Unsaturated fatty acids have one or more double
bonds
Figure 5.10a
Structural
formula
of a saturated
fat molecule
Space-filling
model of
stearic acid,
a saturated
fatty acid
(a) Isthisfatsaturatedorunsaturated?
Figure 5.10b
(b) Isthisfatsaturatedorunsaturated?
Structural
formula of an
unsaturated
fat molecule
Space-filling
model of oleic
acid, an
unsaturated
Cis double
fatty acid
bond causes
bending.

Fatsmadefromsaturatedfattyacidsarecalled
saturatedfatsandaresolidatroomtemperature
Mostanimalfatsaresaturated
Fatsmadefromunsaturatedfattyacidsare
calledunsaturatedfatsoroilsandareliquidat
roomtemperature
Plantfatsandfishfatsareusuallyunsaturated
1. Why is glycerol, on its own, hydrophilic?

2. If glycerol is hydrophilic, what causes fat to be
hydrophobic?
a) A diet rich in saturated fats may contribute

to cardiovascular disease through plaque
deposits
b) Hydrogenation is the process of
converting unsaturated fats to saturated
fats by adding hydrogen
c) Hydrogenating vegetable oils also creates
unsaturated fats with trans double bonds
d) These trans fats may contribute more
than saturated fats to cardiovascular
disease
a) Certain unsaturated fatty acids are not synthesized in

the human body
b) These must be supplied in the diet
c) These essential fatty acids include the omega-3 fatty
acids, which are required for normal growth and are
thought to provide protection against cardiovascular
disease
a) The major function of fats is energy storage

b) Humans and other mammals store their long-term
food reserves in adipose cells
c) Adipose tissue also cushions vital organs and
insulates the body
Fat
droplets
Adipose tissue
ritical Thinking Time
a)Hydrogenated vegetable oils are more like

animal fats than other plant oils. Because
they ______________________ than other
plant oils, they can contribute to
cardiovascular disease.
hospholipids
a) In a phospholipid, two fatty acids and a phosphate
group are attached to glycerol
b) The two fatty acid tails are hydrophobic, but the
phosphate group and its attachments form a
hydrophilic head
Hydrophobic tails
Hydrophilic head
Figure 5.11
Hydrophilic
head
Phosphate
Hydrophobic
tails
Glycerol
(c) Phospholipid symbol
Fatty acids
Kink due to cis
double bond
(a) Structural formula
Choline
(b) Space-filling model
(d) Phospholipid bilayer
What is X?
Interstitialfluid
WhyareX&Ypositionedasshown?
X:abletointeractwithwater/polar
environment//orientatetowards
water/polarenvironment
Y:repelswater//orientateawayfrom
water//excludesitselffromwater
WhatisY?
Cytoplasm
a) When phospholipids are added to water, they

self-assemble into double-layered structures
called bilayers
b) At the surface of a cell, phospholipids are also
arranged in a bilayer, with the hydrophobic tails
pointing toward the interior
c) The structure of phospholipids results in a bilayer
arrangement found in cell membranes
d) The existence of cells depends on phospholipids
a)Because water and oil don't mix, water is

ineffective at washing away oily dirt. The
ability of soap to mix with both water and
oily dirt allows dirt to be washed away.
Provide the most logical chemical
explanation for this phenomenon?
teroids
a) Steroids are lipids characterized by a carbon
skeleton consisting of four fused rings
b) Cholesterol, a type of steroid, is a component in
animal cell membranes
c) A high level of cholesterol in the blood may contribute
to cardiovascular disease
Cholesterol, a steroid
Differences in the chemical groups of sex

hormones
Testosterone
Estradiol
Anabolic steroids pose health risks
synthetic variants of
testosterone
cause a buildup of
muscle and bone
mass
a) prescribed to treat general anemia and some

diseases that destroy body muscle
b) abused by some athletes with serious
consequences, including violent mood swings,
depression ,liver damage or cancer, high cholesterol,
and high blood pressure.
Concept 5.4:
Proteins include a diversity of structures, resulting in a
wide range of functions
a) Proteins account for more than 50% of the dry mass
of most cells
b) Protein functions
1. Enzymes
6. Contractile / Movement
2. Storage
7. Receptor
3. Defensive
4. Transport
5. Signal
8. Structural support
9. Cellular communications
igure 5.13a
Enzymatic proteins
Defensive proteins
Function: Selective acceleration of

chemical reactions
Example: Digestive enzymes catalyze the
hydrolysis of bonds in food molecules.
Function: Protection against disease

Example: Antibodies inactivate and help
destroy 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 membranes, as shown here.
Ovalbumin
Amino acids
for embryo
Transport
protein
Cell membrane
igure 5.13b
Hormonal proteins
Receptor proteins
Function: Coordination of an organisms

activities
Example: Insulin, a hormone secreted by the
pancreas, causes other tissues to take up
glucose, thus regulating blood sugar,
concentration.
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.
High
blood sugar
Insulin
secreted
Normal
blood sugar
Signaling
molecules
Receptor
protein
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
30 m
Connective
60 m
tissue
a) Enzymes are proteins that act as catalysts to speed

up chemical reactions
b) Enzymes can perform their functions repeatedly,
functioning as workhorses that carry out the
processes of life
Defensive proteins are manufactured by the

__________ system.
mino Acid Monomers

a) Amino acids are organic molecules with amino and
carboxyl groups
b) Amino acids differ in their properties due to differing
side chains, called R groups
igure 5.UN01
Side chain (R group)

carbon
What is this molecule called?

What groups are X & Y?
igure 5.14a
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
(Ile or I)
Proline
(Pro or P)
igure 5.14b
Polar side chains; hydrophilic
Serine
(Ser or S)
Threonine
(Thr or T)
Cysteine
(Cys or C)
Tyrosine Asparagine Glutamine

(Tyr or Y) (Asn or N) (Gln or Q)
igure 5.14c
Electrically charged side chains; hydrophilic

Basic (positively charged)
Acidic (negatively charged)
Aspartic acid Glutamic acid

(Asp or D)
(Glu or E)
Lysine
Arginine
(Lys or K) (Arg or R)
Histidine
(His or H)
olypeptides (Amino Acid Polymers)

a) Amino acids are linked by covalent bonds called
peptide bonds
b) A polypeptide is a polymer of amino acids
c) Polypeptides range in length from a few to more than
a thousand monomers
d) Each polypeptide has a unique linear sequence of
amino acids, with a carboxyl end (C-terminus) and an
amino end (N-terminus)
a) Proteins are all constructed from the same set of 20

amino acids
b) Polypeptides are unbranched polymers built from
these amino acids
c) A protein is a biologically functional molecule that
consists of one or more polypeptides
(b)
(a)
What type of
reaction is this?
What is the name of
bond W?
Peptide bond
(c)
New peptide
bond forming
Side
chains
Backbone
Amino end
(N-terminus)
Carboxyl end
(C-terminus)
Which is an example
of a dipeptide &
tripeptide?
Is this functional group soluble in water or lipids?

Carbox
yl
STRUCTURE
Carboxylic acids, or
organic acids
EXAMPLE
NAME OF
COMPOUND
FUNCTIONAL
Has acidic properties
PROPERTIES
because the covalent
bond between oxygen and
hydrogen is so polar; for
example,
Acetic acid, which gives
vinegar its sour taste
Acetic
Acetate
acid
ion
Found in cells in the
ionized form with a
charge of 1 and called a
carboxylate ion (here,
specifically, the acetate
ion).

Amino
STRUCTURE
Amines
EXAMPLE
Glycine
Because it also has
a carboxyl group,
glycine is both an
amine and
a carboxylic acid;
compounds with
both groups are
called amino acids.
Acts as a base;
can pick up an H+
from the
surrounding
solution (water,
in living
organisms).
(nonionize (ionized)
d)
Ionized, with a
charge of 1+,
under cellular
conditions.
NAME OF
COMPOUND
FUNCTIONA
L
PROPERTIES

Sulfhydryl
STRUCTURE
Thiols
NAME OF
COMPOUND
(may be
written HS
)
EXAMPLE
Cysteine
Cysteine is an
important sulfurcontaining amino
acid.
FUNCTIONAL
Two sulfhydryl
PROPERTIES
groups can react,
forming a covalent
bond. This crosslinking helps
stabilize protein
structure.
Cross-linking of
cysteines in hair
proteins maintains the
curliness or
straightness of hair.
Straight hair can be
permanently curled
by shaping it around
curlers, then breaking
and re-forming the
cross-linking bonds.
rotein Structure and Function

a) The specific activities of proteins result from their
intricate three-dimensional architecture
b) A functional protein consists of one or more
polypeptides precisely twisted, folded, and coiled into
a unique shape
igure 5.16
Target
molecule
Groove
(a) A ribbon model
Groove
(b) A space-filling model
(c) A wireframe model
a) The sequence of amino acids determines a proteins

three-dimensional structure
b) A proteins structure determines how it works
c) The function of a protein usually depends on
its ability to recognize and bind to some other
molecule
igure 5.17
Antibody protein
Protein from flu virus
Q
1. What shape are most proteins?
2. What is the name given to a protein polymer?
3. What is a protein monomer called?
our Levels of Protein Structure

a) The primary structure of a protein is its unique
sequence of amino acids
b) Secondary structure, found in most proteins, consists
of coils and folds in the polypeptide chain
c) Tertiary structure is determined by interactions among
various side chains (R groups)
d) Quaternary structure results when a protein consists
of multiple polypeptide chains
a) The primary structure of a protein is its sequence of

amino acids
b) Primary structure is like the order of letters in a long
word
c) Primary structure is determined by inherited genetic
information
Primary Structure
Amino
acids
1
10
20
15
Amino end
30
25
igure 5.18a
Primary structure
of transthyretin
Primary Structure
Amino
acids
1
Function:
Transport vitamin A
& one of the thyroid
hormones in blood
10
20
15
Amino end
30
25
35
45
40
50
Primary structure of transthyretin

70
65
60
55
75
80
85
90
95
115
120
110
125
105
100
Carboxyl end
roteins
What bonds are involved in primary structure?
Which parts of two amino acids are involved per bond?
a) The coils and folds of secondary structure result

from hydrogen bonds between repeating constituents
of the polypeptide backbone
b) Typical secondary structures are a coil called an
helix and a folded structure called a pleated sheet
Secondary
Structure
helix
Hydrogen bond
strand
Hydrogen
bond
pleated sheet
Abdominal glands of the

spider secrete silk fibers
made of a structural protein
containing pleated sheets.
The radiating strands, made
of dry silk fibers, maintain
the shape of the web.
The spiral strands (capture
strands) are elastic, stretching
in response to wind, rain,
and the touch of insects.
Q
What shapes can you see in secondary structure?
What bonds are responsible for producing such

shapes?
Which atoms are involved in such bonds?
a) Tertiary structure, the overall shape of a

polypeptide, results from interactions between
R groups, rather than interactions between backbone
constituents
b) These interactions include hydrogen bonds,
ionic bonds, hydrophobic interactions, and
van der Waals interactions
c) Strong covalent bonds called disulfide bridges may
reinforce the proteins structure
igure 5.18d
Hydrogen
bond
Hydrophobic
interactions and
Van der Waals
interactions
Disulfide
bridge
Ionic bond
Polypeptide
backbone
a) Quaternary structure results when two or more

polypeptide chains form one macromolecule
b) Collagen is a fibrous protein consisting of three
polypeptides coiled like a rope
Collagen
c) Hemoglobin is a globular protein consisting of

four polypeptides: two alpha and two beta chains
Hemoglobin
Heme
Iron
subunit
subunit
subunit
subunit
Whats the difference between the 2 structures below?

one comprises a polypeptide; the other, more than one
Tertiary Structure Quaternary Structure
Which levels of protein structure are represented

below?
Polypeptide
chain
Chains
Quaternary
Iron
Heme
Chains
Collagen
Hemoglobin
Q
a) How many poly peptides are involved?
a) What type of bonds give rise to Quaternary

Structure?
a) Are these intra- or inter-polypeptide bonds?
ickle-Cell Disease: A Change in Primary Structure

a) A slight change in primary structure can affect a
proteins structure and ability to function
b) Sickle-cell disease, an inherited blood disorder,
results from a single amino acid substitution in the
protein hemoglobin
igure 5.19
Normal
Primary
Structure
1
2
3
4
5
6
7
Secondary
and Tertiary
Structures
Normal
subunit
Quaternary
Structure
Function
Normal
hemoglobin
Proteins do not associate

with one another; each
carries oxygen.
5 m
Sickle-cell
1
2
3
4
5
6
7
Sickle-cell
subunit
Sickle-cell
hemoglobin
Proteins aggregate into a

fiber; capacity to
carry oxygen
is reduced.
Red Blood Cell

Shape
5 m
10 m
Normal red blood

cells are full of
individual
hemoglobin
molecules, each
carrying oxygen.
10 m
Fibers of abnormal
hemoglobin deform
red blood cell into
sickle shape.
hat Determines Protein Structure?

a) In addition to primary structure, physical and chemical
conditions can affect structure
b) Alterations in pH, salt concentration,
temperature, or other environmental factors
can cause a protein to unravel
c) This loss of a proteins native structure is
called denaturation
d) A denatured protein is biologically inactive
igure 5.20-1
Normal protein
igure 5.20-2
Normal protein
Denatured protein
igure 5.20-3
Normal protein
Denatured protein
Although polypeptide and protein are

often used interchangeably
Terms
Match terms (left) with

definitions (below)
(Protein
1. two or more amino
acids joined
Polypeptid
e
2. linear polymer
composed of multiple
Peptide)
amino acids
3. not-yet functional
product
4. large polypeptides.
5. a functional product
after undergoing
subsequent chemical
Although polypeptide and protein are

often used interchangeably
Terms
Match terms (left) with

definitions (below)
Peptide
bond
1. Joining of two or more

amino acids
Polypeptid 2. linear polymer composed

e
of multiple amino acids
3. not-yet functional
product
Protein
4. large polypeptides
5. a functional product
after undergoing
subsequent chemical
modification (discussed
oncept 5.5: Nucleic acids store, transmit, and help

express hereditary information
a) The amino acid sequence of a polypeptide is
programmed by a unit of inheritance called
a gene
b) Genes consist of DNA, a nucleic acid made of
monomers called nucleotides
he Roles of Nucleic Acids

a) There are two types of nucleic acids
a)Deoxyribonucleic acid (DNA)
b)Ribonucleic acid (RNA)
b) DNA provides directions for its own replication

c) DNA directs synthesis of messenger RNA (mRNA)
and, through mRNA, controls protein synthesis
d) This process is called gene expression
igure 5.23-1
DNA
1 Synthesis of
mRNA
mRNA
NUCLEUS
CYTOPLASM
igure 5.23-2
DNA
1 Synthesis of
mRNA
mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into
cytoplasm
igure 5.23-3
DNA
1 Synthesis of
mRNA
mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into
cytoplasm
Ribosome
3 Synthesis
of protein
Polypeptide
Amino
acids
a) Each gene along a DNA molecule directs synthesis of

a messenger RNA (mRNA)
b) The mRNA molecule interacts with the cells proteinsynthesizing machinery to direct production of a
polypeptide
c) The flow of genetic information can be summarized
as DNA RNA protein
he Components of Nucleic Acids

a) Nucleic acids are polymers called polynucleotides
b) Each polynucleotide is made of monomers called
nucleotides
c) Each nucleotide consists of a nitrogenous base, a
pentose sugar, and one or more phosphate groups
d) The portion of a nucleotide without the phosphate
group is called a nucleoside
a) Nucleoside nitrogenous base sugar

b) There are two families of nitrogenous bases
a) Pyrimidines (cytosine, thymine, and uracil)
have a single six-membered ring
b)Purines (adenine and guanine) have a six-membered
ring fused to a five-membered ring
c) In DNA, the sugar is deoxyribose; in RNA, the sugar is

ribose
d) Nucleotide nucleoside phosphate group
igure 5.24
NITROGENOUS BASES
Pyrimidines
5 end
Sugar-phosphate backbone
(on blue background)
Cytosine
(C)
5C
3C
Thymine
(T, in DNA)
Purines
Uracil
(U, in RNA)
Nucleoside
Nitrogenous
base
Adenine (A)
5C
1C
5C
3C
Phosphate
group
SUGARS
3C
Sugar
(pentose)
(b) Nucleotide
3 end
(a) Polynucleotide, or nucleic acid
Guanine (G)
Deoxyribose
(in DNA)
Ribose (in DNA)
(c) Nucleoside components
Sugar-phosphate backbone
(on blue background)
Why is the sugar called pentose?
5 end
igure 5.24a
5 carbon sugar
5C
Whats the diff between nucleoside & nucleotide?

Nucleoside is the portion of nucleotide without
the phosphate group
3C
Nucleoside
Nitrogenous
base
5C
1C
Phosphate
group
5C
3C
Sugar
(pentose)
(b) Nucleotide
3 end
(a) Polynucleotide, or nucleic acid
3C
At which sugar C no. is:

i. phosphate attached? 5 carbon
ii. A base attached? 1 carbon
igure 5.24b
NITROGENOUS BASES
Pyrimidines
Cytosine
(C)
Thymine
(T, in DNA)
Purines
Adenine (A)
Guanine (G)

Uracil
(U, in RNA)
1. What are the elements

present in ALL these bases?
carbon, hydrogen, oxygen,
nitrogen
2. What bases are found in
a. RNA?
A, C, U, G
b. DNA?
A, C, T, G
igure 5.24c
Structural Similarity & Difference between

Sugars in DNA & RNA
SUGARS
Deoxyribose
(in DNA)
Ribose (in RNA)
ucleotide Polymers
a) Nucleotides are linked together to build a
polynucleotide
b) Adjacent nucleotides are joined by a phosphodiester
linkage, which consists of a phosphate group that
links the sugars of two nucleotides (OH group on 3
carbon of one nucleotide and phosphate on 5 carbon
on the next)
c) These links create a backbone of sugar-phosphate
units with nitrogenous bases as appendages
d) The sequence of bases along a DNA or mRNA
polymer is unique for each gene
he Structures of DNA and RNA Molecules

a) DNA molecules have two
polynucleotides spiraling
around an imaginary axis,
forming a double helix
b) The backbones run in
opposite 5 3 directions
from each other, an
arrangement referred to as
antiparallel
c) One DNA molecule includes
many genes
a) Only certain bases in DNA pair up and form hydrogen

bonds: adenine (A) always with thymine (T), and
guanine (G) always with cytosine (C)
adenine (A) = thymine (T)
guanine (G) = cytosine (C)
b) This is called complementary base pairing

c) This feature of DNA structure makes it possible
to generate two identical copies of each DNA
molecule in a cell preparing to divide
a) RNA, in contrast to DNA, is single

stranded.
b) Complementary pairing can also
occur within an RNA molecule allows
it to take on particular 3D shape.
c) tRNA shape result from base pairing
between nucleotides where
complementary stretches of molecule
run antiparallel to each other.
d) While DNA always exists as a double
helix, RNA molecules are more
variable in form.
igure 5.UN03
igure 5.UN05

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TENTH EDITION

2015 Pearson Education, Inc.

Water beading on the oily coating of

a) Hydrocarbons = organic molecules consisting of only carbon

2011 Pearson Eduation, Inc.

(b) A fat molecule

oncept 5.3: Lipids are a diverse group of hydrophobic

2015 Pearson Education Ltd

2015 Pearson Education Ltd

2015 Pearson Education Ltd

a)Fats separate from water because water molecules

2015 Pearson Education Ltd

a) Fatty acids vary in length (number of carbons) and in

2015 Pearson Education Ltd

2015 Pearson Education Ltd

2015 Pearson Education Ltd

1. Why is glycerol, on its own, hydrophilic?

2015 Pearson Education Ltd

a) A diet rich in saturated fats may contribute

2015 Pearson Education Ltd

2015 Pearson Education Ltd

a) Certain unsaturated fatty acids are not synthesized in

2015 Pearson Education Ltd

a) The major function of fats is energy storage

2015 Pearson Education Ltd

ritical Thinking Time

a)Hydrogenated vegetable oils are more like

2015 Pearson Education Ltd

2015 Pearson Education Ltd

2015 Pearson Education Ltd

(a) Structural formula

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(b) Space-filling model

(d) Phospholipid bilayer

2015 Pearson Education Ltd

a) When phospholipids are added to water, they

ritical Thinking Time

a)Because water and oil don't mix, water is

2015 Pearson Education Ltd

Differences in the chemical groups of sex

2015 Pearson Education Ltd

Anabolic steroids pose health risks

a) prescribed to treat general anemia and some

Function: Selective acceleration of

Function: Protection against disease

Function: Storage of amino acids

Function: Transport of substances

2015 Pearson Education Ltd

Function: Coordination of an organisms

Function: Response of cell to chemical

Contractile and motor proteins

2015 Pearson Education Ltd

a) Enzymes are proteins that act as catalysts to speed

2015 Pearson Education Ltd

ritical Thinking Time

Defensive proteins are manufactured by the

2015 Pearson Education Ltd

mino Acid Monomers

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Side chain (R group)

What is this molecule called?

Nonpolar side chains; hydrophobic

2015 Pearson Education Ltd

Polar side chains; hydrophilic