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Chapter 5
The Structure and Function of
Large Biological Molecules
PowerPoint® Lecture Presentations for
Biology
Eighth Edition
Neil Campbell and Jane Reece
Lectures by Chris Romero, updated by Erin Barley with contributions from Joan Sharp
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Overview: The Molecules of Life
• All living things are made up of four classes
of large biological molecules:
carbohydrates, lipids, proteins, and nucleic
acids
• Within cells, small organic molecules are joined
together to form larger molecules
• Macromolecules are large molecules
composed of thousands of covalently
connected atoms
• Molecular structure and function are
inseparable
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Macromolecules are polymers, built from monomers
• A polymer is a long molecule consisting of
many similar building blocks
• These small building-block molecules are
called monomers
• Three of the four classes of life’s organic
molecules are polymers:
– Carbohydrates
– Proteins
– Nucleic acids
The Synthesis and Breakdown of Polymers
• A condensation reaction or more
specifically a dehydration reaction occurs
when two monomers bond together
through the loss of a water molecule
• Polymers are disassembled to monomers
by hydrolysis, a reaction that is essentially
the reverse of the dehydration reaction
Fig. 5-2a
HO
1
2
3
H
Short polymer
HO
Unlinked monomer
Dehydration removes a water
molecule, forming a new bond
HO
1
2
H
3
H2O
4
H
Longer polymer
(a) Dehydration reaction in the synthesis of a polymer
Fig. 5-2b
HO
1
2
3
4
Hydrolysis adds a water
molecule, breaking a bond
HO
1
2
3
(b) Hydrolysis of a polymer
H
H
H2O
HO
H
Dehydration Synthesis-Hydrolysis
Carbohydrates
Carbohydrates serve as fuel and building material
• Carbohydrates include sugars and the
polymers of sugars
• The term means “hydrated carbon” due to
the ratio of H to O as in water. The general
formula is (CH2O)n where n can vary.
• The simplest carbohydrates are
monosaccharides, or single sugars
• The number of carbons varies from 3 to 7.
The most common are trioses, pentoses, and
hexoses.
• Glucose (C6H12O6) is the most common
monosaccharide
• Carbohydrates are classified by many
hydroxyl OH groups and one carbonyl group
– The location of the carbonyl group
determines if they are a aldose (aldehyde
form) or ketose (ketone form)
Fig. 5-3
Trioses (C3H6O3)
Pentoses (C5H10O5)
Hexoses (C6H12O6)
Aldosescarbonyls
at end
Glyceraldehyde
Ribose
Glucose
Galactose
Ketosescarbonyls
in middle
Dihydroxyacetone
Ribulose
Fructose
Carbohydrates can form enantiomers.
• Though often drawn as linear skeletons, in
aqueous solutions many sugars form rings.
• When glucose forms a ring, the OH group
attached to the number 1 Carbon is locked
into one of two alternative positions: either
below the ring (alpha) or above the ring
(beta).
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Fig. 5-4
#1 Carbon
(a) Linear and ring forms
(b) Abbreviated ring structure
Fig. 5-7a
beta
alpha
Glucose
(a)
and
Glucose
glucose ring structures
Look at the OH group on the #1 Carbon.
• A disaccharide is formed when a dehydration
reaction joins two monosaccharides
• This covalent bond is called a glycosidic
linkage
• Examples of disaccharides are sucrose
(table sugar) and maltose
Fig. 5-5
1–4
glycosidic
linkage
Glucose
Glucose
Maltose
(a) Dehydration reaction in the synthesis of maltose
1–2
glycosidic
linkage
Glucose
Fructose
(b) Dehydration reaction in the synthesis of sucrose
Sucrose
How to calculate the formula for a disaccharide:
You have to subtract the water molecule
resulting from dehydration synthesis!
Ex: Maltose is made of two glucose units,
what is its molecular formula?
C6H12O6 times two = C12H24O12 MINUS H2O
= C12H22O11
Polysaccharides
• Polysaccharides, the polymers of sugars,
have storage and structural roles
• The structure and function of a
polysaccharide are determined by its sugar
monomers and the positions of glycosidic
linkages
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Storage Polysaccharides
• Starch, a storage polysaccharide of plants,
consists entirely of alpha glucose
monomers in helical patterns.
• Plants store surplus starch as granules
within chloroplasts and other plastids
• The simplest form is amylose and is
unbranched. A more complex branched
from is amylopectin.
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• Glycogen is a storage polysaccharide in
animals
• Humans and other vertebrates store
glycogen mainly in liver and muscle cells.
It is similar to amylopectin but more highly
branched.
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Fig. 5-6
Chloroplast
Mitochondria Glycogen granules
Starch
0.5 µm
1 µm
Glycogen
Amylose
Amylopectin
(a) Starch: a plant polysaccharide
(b) Glycogen: an animal polysaccharide
Structural Polysaccharides
• The polysaccharide cellulose is a major
component of the tough wall of plant cells
• Cellulose is a polymer of beta glucose
units. The glycosidic linkages differ and
make the glucose units appear right side up
and upside down.
• Cellulose is the most abundant organic
compound on earth.
Fig. 5-7bc
(b) Starch: 1–4 linkage of
glucose monomers
(c) Cellulose: 1–4 linkage of
glucose monomers
We cannot digest cellulose!
• Polymers with  glucose are helical
• Polymers with  glucose are straight
• Parallel cellulose molecules held
together this way are grouped into
microfibrils, which form strong building
materials for plants
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Fig. 5-8
Cell walls
Cellulose
microfibrils
in a plant
cell wall
Microfibril
10 µm
0.5 µm
Cellulose
molecules
b Glucose
monomer
• Enzymes that digest starch by hydrolyzing
 linkages can’t hydrolyze  linkages in
cellulose
• Cellulose in human food passes through
the digestive tract as insoluble fiber
• Some microbes use enzymes to digest
cellulose
• Many herbivores, from cows to termites,
have symbiotic relationships with these
microbes
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Fig. 5-9
• Chitin, another structural polysaccharide, is
found in the exoskeleton of arthropods
• Chitin also provides structural support for
the cell walls of many fungi
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Fig. 5-10
(a) The structure
of the chitin
monomer.
(b) Chitin forms the
exoskeleton of
arthropods.
Has N containing
appendage
(c) Chitin is used to make
a strong and flexible
surgical thread.
Lipids are a diverse group of hydrophobic
molecules
• Lipids are the one class of large biological
molecules that do not form polymers
• The unifying feature of lipids is basically
insolubility in water.
• Lipids are hydrophobic because they
consist mostly of hydrocarbons, which
form nonpolar covalent bonds
• The most biologically important lipids are
fats, phospholipids, and steroids
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Fats
• Fats (triglycerides or triacyglycerols) are
constructed from two types of smaller
molecules: glycerol and fatty acids
• Glycerol is a three-carbon alcohol with a
hydroxyl group attached to each carbon
• A fatty acid consists of a carboxyl group
attached to a long carbon skeleton
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-11
Fatty acid
(palmitic acid)
Glycerol
(a) Dehydration reaction in the synthesis of a fat
Ester linkage
(b) Fat molecule (triacylglycerol)
Fig. 5-11a
Fatty acid
(palmitic acid)
Glycerol
(a) Dehydration reaction in the synthesis of a fat
Fig. 5-11b
Ester linkage
(b) Fat molecule (triacylglycerol)
• In a fat, three fatty acids are joined
to glycerol by an ester linkage,
creating a triacylglycerol, or
triglyceride
• The source of variation among fat
molecules is the fatty acid
composition.
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• Fatty acids vary in length (number of
carbons) and in the number and locations of
double bonds
• Saturated fatty acids have the maximum
number of hydrogen atoms possible and no
double bonds. They tend to be solid at room
temperature. Most animal fats are
saturated.
• Unsaturated fatty acids have one or more
double bonds and are liquid at room temp.
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-12
Structural
formula of a
saturated fat
molecule
Stearic acid, a
saturated fatty
acid
(a) Saturated fat
Structural formula
of an unsaturated
fat molecule
Oleic acid, an
unsaturated
fatty acid
(b) Unsaturated fat
cis double
bond causes
bending
Fig. 5-12a
Structural
formula of a
saturated fat
molecule
Stearic acid, a
saturated fatty
acid
(a) Saturated fat
Fig. 5-12b
Structural formula
of an unsaturated
fat molecule
Oleic acid, an
unsaturated
fatty acid
(b) Unsaturated fat
cis double
bond causes
bending
• A diet rich in saturated fats may contribute to
cardiovascular disease through plaque
deposits
• Hydrogenation is the process of converting
unsaturated fats to saturated fats by adding
hydrogen
• Hydrogenating vegetable oils also creates
unsaturated fats with trans double bonds
• These trans fats may contribute more than
saturated fats to cardiovascular disease
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Trans Fats
What’s so bad about trans fats?
• The health implications of trans fats were
recognized as early as 1958, when Dr Ancel
Keys reported that he believed that
hydrogenated vegetable oils with their trans
fats components were responsible for the
sudden and significant increase in heart
disease over the previous decade.
• The Harvard School of Public Health has
issued a warning regarding the comsumption of
margarines, snack foods and other foods
containing hydrogenated oils (and their trans
fats), in favor of butter.
• The major function of fats is energy storage
• Humans and other mammals store their fat
in adipose cells
• Adipose tissue also cushions vital organs
and insulates the body
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Phospholipids
• In a phospholipid, two fatty acids and a
phosphate group, which replaces one of the
fatty acids, are attached to glycerol
• The two fatty acid tails are hydrophobic, but
the phosphate group and its attachments
form a hydrophilic head
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Hydrophobic tails
Hydrophilic head
Fig. 5-13
(a) Structural formula
Choline
Phosphate
Glycerol
Fatty acids
Hydrophilic
head
Hydrophobic
tails
(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
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Fig. 5-14
Hydrophilic
head
Hydrophobic
tail
WATER
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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Fig. 5-15
Wow – Super hydrophobic!
• Waxes – alcohol (long chain hydrocarbon
with OH at end) bonded with a long chain
fatty acid.
Proteins have many structures, resulting in a wide
range of functions
• 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
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Types of Proteins and their functions:
1. Structural - collagen
2. Storage – amino acids in egg albumin
3. Transport – hemoglobin
4. Hormonal – insulin
5. Receptors – G proteins
6. Contractile – actin in muscles
7. Defensive – antibodies
8. Enzymes – pepsin in stomach
A protein consists of one or more polypeptides.
• Polypeptides are polymers built from the
same set of 20 amino acids that are
arranged in a specific linear sequence and
linked by peptide bonds through
condensation (dehydration) reactions.
• Proteins have a unique 3-D shape
(conformation) that determines their
function
• This is an aspirin-binding
protein.
Fig. 5-16
Enzymes have specific
shapes to fit their
substrates.
Substrate
(sucrose)
Glucose
OH
Fructose
HO
Enzyme
(sucrase)
H2O
Amino Acids are the Monomers of Proteins
• Amino acids are organic molecules with
carboxyl COOH and amino groups NH2
• Amino acids differ in their properties due to
differing side chains, called R groups –
makes each amino acid unique.
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-UN1
carbon
Amino
group
Carboxyl
group
What is a zwitterion?
• At normal pH’s in the cell, both the carboxyl
and amino groups are ionized zwitterion.
• The pH of the solution determines which
ionic state predominates.
• The side chains (R groups) confer degrees of
polarity to the amino acid.
• Amino acids may be polar, nonpolar, or
electrically charged.
Fig. 5-17a
Nonpolar
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)
Fig. 5-17b
Polar
Serine
(Ser or S)
Threonine
(Thr or T)
Cysteine
(Cys or C)
Tyrosine
(Tyr or Y)
Asparagine Glutamine
(Asn or N) (Gln or Q)
Fig. 5-17c
Electrically
charged
Acidic
Aspartic acid Glutamic acid
(Glu or E)
(Asp or D)
Basic
Lysine
(Lys or K)
Arginine
(Arg or R)
Histidine
(His or H)
Amino Acid Polymers
• Amino acids are linked by peptide bonds
• A polypeptide is a polymer of amino acids
• Polypeptides range in length from a few to
more than a thousand monomers
• Each polypeptide has a unique linear
sequence of amino acids
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Fig. 5-UN5
Fig. 5-18
Notice the
peptide bond
separates the
NCC of each
amino acid.
Peptide
bond
(a)
Side chains
Peptide
bond
Backbone
(b)
Amino end
(N-terminus)
Carboxyl end
(C-terminus)
Remember!
NCC NCC NCC NCC NCC NCC….
Like a cheer!
Protein Structure and Function
• A functional protein consists of one or
more polypeptides twisted, folded, and
coiled into a unique shape
• A protein’s structure determines its
function
• The sequence of amino acids determines a
protein’s three-dimensional structure
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-19
Groove
Groove
(a) A ribbon model of lysozyme
(b) A space-filling model of lysozyme
Fig. 5-20
Antibody protein
Protein from flu virus
The levels of protein structure
• 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
• Amino acids are bonded by peptide bonds.
Fig. 5-21a
Primary Structure
1
+H
5
3N
Amino end
10
Amino acid
subunits
15
20
25
Fig. 5-21b
1
5
+H
3N
Amino end
10
Amino acid
subunits
15
20
25
75
80
90
85
95
105
100
110
115
120
125
Carboxyl end
• 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
Fig. 5-21c
Secondary Structure
pleated sheet
Examples of
amino acid
subunits
helix
Fig. 5-21d
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.
• Tertiary structure is determined by
interactions between R groups, rather than
interactions between backbone
constituents
• These weak interactions between R groups
include hydrogen bonds, ionic bonds,
hydrophobic interactions, and van der
Waals interactions
• Strong covalent bonds called disulfide
bridges may reinforce the protein’s
structure
Fig. 5-21e
Tertiary Structure
Quaternary Structure
Fig. 5-21f
Hydrophobic
interactions and
van der Waals
interactions
Polypeptide
backbone
Hydrogen
bond
Disulfide bridge
Ionic bond
• Quaternary structure results when two or
more polypeptide chains form one
macromolecule
• Collagen is a fibrous protein consisting of
three polypeptides coiled like a rope
• Hemoglobin is a globular protein consisting
of four polypeptides: two alpha and two
beta chains
Fig. 5-21g
Polypeptide
chain
Chains
Iron
Heme
Chains
Hemoglobin
Collagen
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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Fig. 5-22c
10 µm
Normal red blood
cells are full of
individual
hemoglobin
molecules, each
carrying oxygen.
10 µm
Fibers of abnormal
hemoglobin deform
red blood cell into
sickle shape.
Fig. 5-22
Normal hemoglobin
Primary
structure
Sickle-cell hemoglobin
Primary
structure
Val His Leu Thr Pro Glu Glu
1
2
3
Secondary
and tertiary
structures
4
5
6
7
subunit
Secondary
and tertiary
structures
Val His Leu Thr Pro Val Glu
1
2
3
Exposed
hydrophobic
region
Quaternary
structure
Normal
hemoglobin
(top view)
Quaternary
structure
Sickle-cell
hemoglobin
Function
Molecules do
not associate
with one
another; each
carries oxygen.
Function
Molecules
interact with
one another and
crystallize into
a fiber; capacity
to carry oxygen
is greatly reduced.
10 µm
Red blood
cell shape
Normal red blood
cells are full of
individual
hemoglobin
moledules, each
carrying oxygen.
4
5
6
7
subunit
10 µm
Red blood
cell shape
Fibers of abnormal
hemoglobin deform
red blood cell into
sickle shape.
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
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Fig. 5-23
Denaturation
Normal protein
Renaturation
Denatured protein
Protein Folding in the Cell
• It is hard to predict a protein’s structure
from its primary structure
• Most proteins probably go through several
states on their way to a stable structure
• Chaperonins are protein molecules that
assist the proper folding of other proteins
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Fig. 5-24
Polypeptide
Correctly
folded
protein
Cap
Hollow
cylinder
Chaperonin
(fully assembled)
Steps of Chaperonin 2
Action:
1 An unfolded polypeptide enters the
cylinder from one end.
The cap attaches, causing the 3 The cap comes
cylinder to change shape in
off, and the properly
such a way that it creates a
folded protein is
hydrophilic environment for
released.
the folding of the polypeptide.
• Scientists use X-ray crystallography to
determine a protein’s structure
• Another method is nuclear magnetic
resonance (NMR) spectroscopy, which
does not require protein crystallization
• Bioinformatics uses computer programs to
predict protein structure from amino acid
sequences
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Fig. 5-25
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
Crystal
Digital detector
X-ray diffraction
pattern
RESULTS
RNA
polymerase II
DNA
RNA
Fig. 5-25a
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
Crystal
Digital detector
X-ray diffraction
pattern
Fig. 5-25b
RESULTS
RNA
polymerase II
DNA
RNA
Concept 5.5: Nucleic acids store and transmit
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
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The Roles of Nucleic Acids
• There are two types of nucleic acids:
– Deoxyribonucleic acid (DNA)
– Ribonucleic acid (RNA)
• DNA directs synthesis of messenger RNA
(mRNA) and, through mRNA, controls
protein synthesis
Fig. 5-26-1
DNA
1 Synthesis of
mRNA in the
nucleus
mRNA
NUCLEUS
CYTOPLASM
Fig. 5-26-2
DNA
1 Synthesis of
mRNA in the
nucleus
mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm
via nuclear pore
Fig. 5-26-3
DNA
1 Synthesis of
mRNA in the
nucleus
mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm
via nuclear pore
Ribosome
3 Synthesis
of protein
Polypeptide
Amino
acids
The Structure of Nucleic Acids
• Nucleic acids are polymers made of
nucleotides
• Each nucleotide consists of a nitrogenous
base, a pentose sugar, and a phosphate
group
• The portion of a nucleotide without the
phosphate group is called a nucleoside
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Fig. 5-27ab
5' end
5'C
3'C
Nucleoside
Nitrogenous
base
5'C
Phosphate
group
5'C
3'C
(b) Nucleotide
3' end
(a) Polynucleotide, or nucleic acid
3'C
Sugar
(pentose)
Nitrogenous Bases
• There are two families of nitrogenous
bases:
– Pyrimidines (cytosine, thymine, and uracil)
have a SINGLE six-membered ring
– Purines (adenine and guanine) have a sixmembered ring fused to a five-membered
ring – DOUBLE RING
Fig. 5-27c-1
Nitrogenous bases
Pyrimidines
Cytosine (C)
Thymine (T, in DNA)
Uracil (U, in RNA)
Purines
Adenine (A)
Guanine (G)
(c) Nucleoside components: nitrogenous bases
Sugars in nucleic acids
• In DNA, the sugar is deoxyribose; in RNA,
the sugar is ribose
Deoxyribose (in DNA)
Ribose (in RNA
Adjacent nucleotides are joined by covalent
bonds called phosphodiester linkages
between the sugars and phosphates.
Phosphodiester
Linkage
These links create
a backbone of
sugar-phosphate
units with
nitrogenous bases
as appendages
• The sequence of bases along a DNA or
mRNA polymer is unique for each gene
The DNA Double Helix
• A DNA molecule has two polynucleotides
spiraling around an imaginary axis, forming a
double helix
• In the DNA double helix, the two backbones
run in opposite 5 → 3 directions from each
other, an arrangement referred to as
antiparallel
• One DNA molecule includes many genes
• The nitrogenous bases in DNA pair up and
form hydrogen bonds: adenine (A) always with
thymine (T), and guanine (G) always with
cytosine (C)
Base Pairing in DNA
Fig. 5-UN9
In Summary for all macromolecules
Carbohydrates
• Monomers – monosaccharides
• How to recognize – carbonyl group
(becomes integral oxygen in ring), many OH
groups, mostly C, H, O
• Functions – ENERGY
• Properties – polar (hydrophilic)
• Linkages - glycosidic
Fig. 5-7a
beta
alpha
Glucose
(a)
and
Glucose
glucose ring structures
Look at the OH group on the #1 Carbon.
Lipids
Components:
• Fats (triglycerides): glycerol + 3 fatty acids
• Phospholipids: one fatty acid replaced by
phosphate group
• Steroids: four fused rings
How to recognize: glycerol – 3 carbons linked to OH,
fatty acids – COOH + many C-H bonds, also see
above
Functions: stored energy
Properties: nonpolar (hydrophobic)
• Linkage: ester
PHOSPHATE GROUP
Proteins
• Monomers: amino acids
• How to recognize: amino group NH 2 and
COOH acid group bonded to a central C
with a R group; four levels of structure
• Functions: many
• Properties: generally polar (R groups may
be nonpolar)
• Linkages: peptide
Fig. 5-UN5
Nucleic Acids
• Monomer – nucleotides
• How to recognize: nitrogenous base,
sugar, phosphate
• Functions: direct synthesis of proteins
• Properties: polar
• Linkages: phosphodiester