Chapter 1

Macromolecules
SITI SABRINA KASRI
1
Learning Objective
1. Discuss some biologically important chemical groups.
2. Explain the structure of water and describe the properties of water and
its importance.
3. Formation of macromolecules from monomers.
4. Describe the synthesis of disaccharides and polysaccharides.
5. Describe the structure and function of starch, glycogen and cellulose.
6. Structures and functions nucleic acids.
7. State the types and functions of DNA and RNA.
8. Describe the general. structure of amino acids and group them based on
their side chains.
9. Discuss the classification of protein in term of levels of organisation,
structure, composition and functions.
10. State the of lipid.
11. Describe the synthesis and structure of fat/tricylglycerol.
12. Functions of lipid.
2
Macromolecules
are the main
structural
components of
cells and tissues.
Participate in and
regulate metabolic
reactions ,transmit
information,
provide energy for
the process.
3
5. The Molecules of Life
4
To be discussed
5. Molecules of Life Synthesize and breakdown of polymers.
6. Carbohydrates Four group of carbohydrates, Synthesis of
disaccharides and polysaccharides, Structures and
functions of starch, glycogen and cellulose
7.Nucleic acid Structure and components of nucleic acids,
State the types and functions of DNA and RNA.
8. Protein Monomers of protein, Polypeptides from amino
acids, Protein structure and function, Denaturation
of protein.
9. Lipid Type of lipid, Synthesis and structure of
fat/tricylglycerol, Function of lipids.
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5. The Molecules of Life
All living things are made up of four classes of large biological
molecules:
carbohydrates
lipids
proteins
nucleic acids
Within cells, small organic molecules are joined together to form
larger molecules known as macromolecules.
Molecular structure and function are inseparable.
6
Macromolecules are polymers, built from
monomers
A polymer is a long molecule consisting of many similar building
blocks linked by covalent bonds.
- These small building-block molecules are called monomers.
Three of the four classes of lifes organic molecules are polymers:
Carbohydrates
Proteins
Nucleic acids
Lipid is not true polymers.
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8
Macromolecules
The Diversity of Polymers
Each cell has thousands of different kinds of
macromolecules.
An immense variety of polymers can be built from a small
set of monomers.
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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.
10
Fig. 5-2a
Dehydration removes a water
molecule, forming a new bond
Short polymer Unlinked monomer
Longer polymer
Dehydration reaction in the synthesis of a polymer
HO
HO
HO
H
2
O
H
H H
4 3 2 1
1 2 3
(a)
11
Fig. 5-2b
Hydrolysis adds a water
molecule, breaking a bond
Hydrolysis of a polymer
HO
HO HO
H
2
O
H
H
H
3 2 1
1 2 3 4
(b)
12
6. CARBOHYDRATES
13
Four groups of carbohydrates are:
Monosaccharides
- The simplest carbohydrates, (a.k.a simple sugars)
Disaccharides
- Are double sugars
- Consisting of 2 monosaccharides joined by a covalent bond.
Oligosaccharides
- Small chains of monosaccharides (3 14 monosaccharides)
Polysaccharides
- Complex sugars
- Polymers composed of many sugar building blocks.
Sugars
Monosaccharides
Have molecular formulas that are multiples of (CH
2
O)
n
.
Serve as a major fuel for cells and as raw material for
building molecules.
Glucose (C
6
H
12
O
6
) is the most common monosaccharide,
is of central importance in the chemistry of life.
In the structure of glucose, there are few trademarks of
sugar such as:
- The molecule has a carbonyl group
and multiple hydroxyl group.
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Monosaccharides are classified by:
1. The location of the carbonyl group (as
aldose or ketose).
2. The number of carbons in the carbon
skeleton (as trioses, pentoses or
hexoses).
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1. Location of carbonyl group
Glucose and fructose has the same molecular formula,
C
6
H
12
O
6
but differ molecular structure (in the arrangements of
their atoms). Both are isomers.
As a result, both has different properties. Eg, fructose taste
sweeter than glucose.
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2. Number of carbons in the carbon skeleton
An initial breakdown
product of glucose
Component of RNA
Energy source
An initial breakdown
product of glucose
An intermediate in photosynthesis
18
Linear and Ring Form
Though often drawn as linear skeletons, in aqueous solutions, many
sugars form rings.
To form the glucose ring, carbon atom number 1 bonds to the oxygen
attached to carbon atom number 5.
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20
-glucose= -OH at C1 projects below
the plane of the ring.
-glucose= -OH at C1 projects above
the plane of the ring
To form fructose ring, carbon atom number 2 bonds to the oxygen
attached to carbon number 5.
Fructose in linear form
Fructose in ring form
fructose fructose
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Monosaccharide properties;
-have a sweet taste.
-can be crystallized.
-are polar due to hydroxyl group attached to C atoms &
form H bonds with water.
-dissolve easily in water.
-have reducing properties.
Disaccharide
A disaccharide is formed when a dehydration reaction
joined two monosaccharides and removed 1 molecule of
water.
This covalent bond is called a glycosidic linkage.
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Characteristic: water soluble, sweet tasting and
can be crystallised.
Three type of disaccharides: maltose, sucrose
and lactose.
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In the synthesis of maltose via dehydration, 2
molecules of glucose are joined by a glycosidic linkage
forming 1-4 glycosidic linkage or -1,4-glycosidic
linkage.
Water molecule is removed in this reaction.
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1-2 glycosidic linkage or -1,2-glycosidic
linkage in sucrose.
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27
Oligosaccharides
Monosaccharides can be linked together to form small
chains(typically two to ten units of monosaccharides)
termed oligosaccharides.
It can be found attached to proteins and lipids forming
glycoproteins and glycolipids of the plasma membrane.
Oligosaccharides provide energy and serve as markers
for cellular recognition.
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Fig. 7-7
Glyco-
protein
Glycolipid
EXTRACELLULAR
SIDE OF
MEMBRANE
Carbohydrate
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Polysaccharides
It is the polymers of sugars, have storage and structural roles.
Made up of the condensation of hundreds of monosaccharides
monomers in the process called polymerisation.
The structure and function of a polysaccharide are determined by its
sugar monomers and the positions of glycosidic linkages.
The chains maybe branched or unbranched.
Generally not soluble in water and not sweet to taste.
Examples of polysaccharides: starch, glycogen, cellulose, chitin,
peptidoglycan.
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Storage polysaccharides:
- Starch
- Glycogen
Structural polysaccharides:
- Cellulose
- Chitin
- Peptidoglycan
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Starch
A storage polysaccharide of plants, consists entirely of glucose
monomers. It represents stored energy.
Plants store surplus starch as granules within chloroplasts and other
plastids.
Synthesizing starch enables the plant to stockpile surplus glucose.
Potato tubers and grains (wheat, maize, rice) are the major sources of
starch.
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Starch consists entirely of glucose monomers.
The glucose monomers in starch are joined by 1-4 linkages or -1,4-
glycosidic (number 1 carbon to number 4 carbon).
It is made up of two components; amylose and amylopectin.
Amylose
- Linear unbranched polymer of 200 to 1500 -glucose units in repeating
sequence of a -1,4-glycosidic linkages.
- The amylose chain coils into a helix held by hydrogen bonds formed
between hydroxyl group.
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Amylose
Hydrogen bond
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Amylopectin
It is a more complex starch with 2 glycosidic bonds (-1,4 and
-1,6 glycosidic linkages).
Each branch of amylopectin is a short chain that is made of
many glucose subunits linked together through -1,4-
glycosidic linkages. Then, these branches are linked together
through -1,6-glycosidic linkages.
Branches -1,6-glycosidic linkage occur at intervals of 1 for
every 30 monomers.
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Amylopectin
36
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Glycogen
Storage polysaccharide in animals.
Humans and other vertebrates store glycogen mainly in liver and
muscle cells.
It is a polymer of glucose (-glucose) and is nearly identical with the
branched form of starch.
The molecule is made up of shorter chains but highly branched.
Instead of an -1,6-glycosidic linkage occuring in about 1 out of 30
monomers (in amylopectin), a branch occurs in about 1 of every 10
glucose subunits in glycogen.
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40
Cellulose
The polysaccharide cellulose is a major component of the tough wall
of plant cells.
Like starch, cellulose is a polymer of glucose, but the glycosidic
linkages differ. Therefore, both has its own distinct three-dimensional
shapes.
If starch molecules is helical, a cellulose molecule is straight.
Cellulose is a long unbranched chain of up to 10,000 of -glucose
monomers that are joined by -1,4-glycosidic linkages.
41
The difference is based on two ring forms for
glucose: alpha () and beta ().
Polymers with glucose are helical
Polymers with glucose are straight
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If you look at the figure of starch, all monomers of
glucose are in the same orientation. If you compare with
glucose monomers in cellulose, each of the glucose
monomer is upside down (flipped) with respect to its
neighbors.
The flipped orientations is important because:
1. Generates a linear molecule
2. Permits multiple hydrogen bonds to form between
adjacent, parallel strands of cellulose.
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In straight structures, H atoms on one strand bond with
OH groups on other strands.
Parallel cellulose molecules held together this way are
grouped into microfibrils, which form strong building
materials for plants.
Three-dimensional structure
44
The fibrils give the plant high tensile strength and rigidity.
The layers of fibrils are freely permeable to water and solutes.
Commercially-cellulose is used to make cotton goods and paper for
various uses.
45
Enzymes that digest starch by hydrolyzing its linkages are unable to
hydrolyze the linkages of cellulose (because of different shapes of
molecules).
But, animals that obtain nutrition from cellulose (eg, cows and termites)
have cellulose-hydrolysing prokaryotes inhabiting their digestive tracts.
Some fungi can also digest cellulose, thereby helping recycle chemical
elements within Earths ecosystem.
46
Chitin
Another structural polysaccharide, is found in the exoskeleton of
arthropods.
Chitin also provides structural support for the cell walls of many fungi.
47
Chitin is similar to cellulose except that the glucose
monomer of chitin has a nitrogen containing
appendages.
The hydroxyl group (-OH) at carbon atom number 2 is
replaced by NH.COCH
3
(amino sugar combined with
*acetyl group).
* Acetyl group: a methyl group single-bonded to a carbonyl
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Murein (Peptidoglycan)
A polysaccharide.
Component of bacterial
cell wall.
Consist of polysaccharides
cross linked with amino
acids.
7. NUCLEIC ACIDS
50
Nucleic acids
Introduction
Still remember protein?
A KIND OF POLYPEPTIDE MADE FROM LINKING MONOMERS OF
AMINO ACID VIA PEPTIDE BOND.
What determines primary structure? AMINO ACID
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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Nucleic acids are polymers, just as proteins.
Nucleic acids are made up of monomers called nucleotides.
Polymers of nucleotidespolynucleotide.
Nucleic acids - complex molecules containing elements of Carbon,
Hydrogen, Oxygen, Phosphorus and Nitrogen.
Building blocks
of nucleic acid
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Structures and Components of Nucleic Acid
A nucleotide = nucleoside (a pentose sugar + nitrogenous base) +
phosphate group
Each nucleotide consists of a
1. Pentose sugar-5 carbon sugar
2. Nitrogenous base
3. Phosphate group
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1. Pentose sugar
Pentose refers to the group of five carbon sugars.
RNA-ribose sugar
DNA-deoxyribose sugar
Compare Ribose and Deoxyribose. Look at C atom number 2.
Components of Nucleotide
1. Pentose sugar-5 carbon sugar
2. Nitrogenous base
3. Phosphate group
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2. Nitrogenous base
A base is a ring structure containing nitrogen.
The base is bonded to 1carbon of pentose sugar.
There are two families of nitrogenous bases:
Pyrimidines = cytosine (C), thymine (T), and uracil (U).
= have a single six-membered ring.
Purines = adenine (A) and guanine (G)
= have a six-membered ring fused to a five-membered ring
DNA= contain A, G, C, T
RNA= contain A, G, C, U
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Fig. 5-27c-1
(c) Nucleoside components: nitrogenous bases
Purines
Guanine (G) Adenine (A)
Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA)
Nitrogenous bases
Pyrimidines
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3. Phosphate group
The phosphate group (which derived from
phosphoric acid) is joined by condensation to the
pentose sugar.
It gives nucleic acid their acidic property.
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Fig. 5-27
5 end
Nucleoside
Nitrogenous
base
Phosphate
group
Sugar
(pentose)
(b) Nucleotide
(a) Polynucleotide, or nucleic acid
3 end
3C
3C
5C
5C
Nitrogenous bases
Pyrimidines
Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA)
Purines
Adenine (A) Guanine (G)
Sugars
Deoxyribose (in DNA) Ribose (in RNA)
(c) Nucleoside components: sugars
Summary of Structures and Components
of Nucleic Acid
58
Nucleotide Polymers
Nucleotides are linked together to build a polynucleotide.
Adjacent nucleotides are joined by covalent bonds that form between
the OH group on the 3 carbon of one nucleotide and the phosphate on
the 5 carbon on the next nucleotide.
The result of this condensation reaction is called a phosphodiester
linkage or phosphodiester bond.
There are two types of nucleic acids:
1. Deoxyribonucleic acid (DNA)
if the nucleotide involved contain the sugar deoxyribose, the resulting
polymer is called deoxyribonucleic acid, DNA.
2. Ribonucleic acid (RNA)
if the nucleotide involved contain the sugar ribose, the resulting polymer is
called ribonucleic acid, RNA.
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These links create a backbone of sugar-phosphate units with
nitrogenous bases as appendages.
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1. DNA
store genetic information.
provides directions for its own replication.
directs synthesis of messenger RNA (mRNA) and, through mRNA,
controls protein synthesis.
2. RNA
protein synthesis
Types & Roles of Nucleic Acids
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1. Deoxyribonucleic acid (DNA)- The DNA Double Helix
A DNA molecule has two polynucleotides strand that are coiled together forming a
LONG double helix.
Found in nucleus.
In the DNA double helix, the two backbones run in opposite 5 3 directions
from each other, an arrangement referred to as antiparallel.
DNA= a phosphate group + a deoxyribose sugar + nitrogenous bases
The nitrogenous bases in DNA pair up and form hydrogen bonds:
- the base pairing is precise (base purine always pair with base pyrimidine)
- adenine (A) always with thymine (T), and guanine (G) always with cytosine (C)
A-T
G-C
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Fig. 5-28
Sugar-phosphate
backbones
3' end
3' end
3' end
3' end
5' end
5' end
5' end
5' end
Base pair (joined by
hydrogen bonding)
Old strands
New
strands
Nucleotide
about to be
added to a
new strand
- Hydrogen bonding is weaker than
covalent bonding (phosphodiester
bond).
- So it is much easier to separate two
DNA strands longitudinally than
separating them in the horizontal
manner.
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2. Ribonucleic acid (RNA)
Consists of single short polynucleotide strand.
Found in cytoplasm.
Each RNA= a phosphate + a ribose sugar + nitrogenous bases (A, U, C,G)
The pyrimidine base thymine in DNA is replaced by uracil in RNA.
Three types of RNA:-
1.ribosomal RNA (rRNA)
2.messenger RNA (mRNA)
3.transfer RNA (tRNA)
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Synthesis of Protein
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Chapter 1
8. PROTEINS
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Proteins
Proteins account for more than 50% of the dry mass of most
cells.
They are polymers formed from the condensation of amino acids
joined by peptide linkage.
Proteins contain the element of Carbon, Hydrogen, Oxygen and
Nitrogen. Many proteins also contain Sulphur and Phosphorus.
Humans has ten of thousand of different protein each with
specific structure and functions.
Protein functions include structural support, storage, transport,
cellular communications, movement, and defense against foreign
substances.
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Monomers of Protein: Amino Acid
Amino acids are organic molecules with an acidic carboxyl
group, a basic amino groups, a hydrogen atom and an R
group.
Amino acids differ in their properties due to different side chains,
R groups.
At the center of the amino acid is an assymetric carbon called
the alpha () carbon
Based on the R groups attached to the carbon, there are 20
amino acids that cells use to build thousands of proteins.
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Common structure of amino acid:
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20 amino acids are group
based on:
Amino acids that have hydrocarbon
as side chain
= known Non-polar group
= Hydrophobic
Amino acids with a polar R group as
side chains
= known Polar group
= Hydrophilic
Amino acids with polar R group with
partial charges
= known Electrically-charged
group
- Amino acids with acidic R group
- Amino acid with basic R group
= Hydrophilic
1.
2.
3.
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Amino acids are amphoteric molecules
- have both basic group (amino group) and acidic group (carboxyl group).
- function as buffer maintain the environment of the bodys internal fluid by
resist any change in pH and try to maintain the pH.
When dissolved in water :
-It dissociate to form zwitterion.
- A zwitterion
carries both positively and negatively charged poles.
its amino group is ionised into NH
3
+
,
its acidic group is ionised into COO
-
.
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All these amino acids contain a basic
amine group, which can act as a
proton acceptor, and an acidic
carboxylic acid group, which an act as
a proton donor.
The COOH donates a proton to the
NH
2
group, forming a zwitterion, in an
internal acid-base reaction.
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Amino acids
Two kinds of proteins:
1. Essential amino acids
- cannot be synthesized by the body.
- must be included in the diet.
2. Non-essential amino acids
- can be synthesized from other amino acids in the body.
Two class of proteins:
1. First class proteins
- found in milk, eggs, meats and fish.
- are rich with essential amino acids.
2. Second class proteins
- found in plants
- contain less of the essential amino acids.
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Polypeptides from Amino Acids
A protein consists of one or more polypeptides each
folded and coiled into a specific three dimensional
structure.
Polypeptides
polymer of amino acids.
range in length from a few to more than a thousand
monomers.
Each polypeptide has a unique linear sequence of amino
acids
How to link amino acids to form proteins?
DEHYDRATION/CONDENSATION PROCESS
76
How to link amino acids to form proteins?
Amino acid monomers are linked by peptide bonds to
form proteins.
Accomplished by an dehydration/condensation reaction.
This links the carboxyl group of one amino acid to the amino group
of the next amino acid.
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At one end of polypeptide chain is a free amino group and free
carboxyl group.
Repeating sequence of amino acid= Backbone.
Appendages extending from backbone= Side chains.
The polypeptide chain has a backbone of atoms in the regular
pattern: -N-C-C-N-C-C-etc.
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Protein Structure and Function
The model shows how single polypeptide
chain folds and coils to form functional
protein.
The model shows specific three-
dimensional structure unique to lysozyme.
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Classification of Proteins
What determine protein structure and function?
1. Levels of organizations
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure
2. Structures
- Globular proteins
- Structural proteins
Classification of Proteins
3. Composition
- Simple proteins
- Conjugated proteins
4. Functions
- Structure
- Catalysts
- Signals
- Movement
- Defense
- Storage
1. Levels of Protein Structure
There are four levels of protein structure: i. Primary Structure
ii. Secondary Structure
iii. Tertiary Structure
iv. Quartenary Structure
i. Primary structure
Refers to the linear sequence of amino acids in a polypeptide chain.
Sequence of amino acids is determined by the genetic information
carried in the DNA molecule in the nucleus.
This sequence is unique for a particular protein.
A substitution or deletion of even 1 amino acid in the primary structure
can affect the structure & function of the protein.
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PRIMARY STRUCTURE
OF PROTEIN
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ii. Secondary structure
Secondary structure, found in most proteins, consists of coils and
folds in the polypeptide chain.
2 types of proteins with secondary structure:
- helix coiled form
- pleated sheet folded form
The coils and folds of secondary structure result from hydrogen
bonds between repeating constituents of the polypeptide backbone.
Both the oxygen and the nitrogen atoms of the backbone are
electronegative, with partial charges.
The weakly positive hydrogen atom (attached to the nitrogen atom) has
an affinity for the oxygen atom of a nearby peptide bond.
This result to hydrogen bonds formed between C=O and NH-groups from the
peptide bond regions.
Individually, hydrogen bonds are weak, but because they are repeated many
times over a long region of the polypeptide chain, they can support a
particular shape for that part of the protein.
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helix
delicate coil held by hydrogen bonding forming helical structure.
shape of the helix is maintained by hydrogen bonds between every 4th
amino acid.
examples of helix protein:
i. Globular proteins
- may have single helix structure or multiple stretches of helix
separated by non helical regions.
ii. Some fibrous proteins
- fibrous protein keratin found in hair, nails, horn and feathers.
- fibrous protein collagen found in tendons, ligaments and cartilage.
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pleated sheet
Structure of two or more regions of the polypeptide chain lying side by side
connected by hydrogen bonds between parts of the two parallel
polypeptide backbones.
Make up the core of many globular proteins & also some fibrous proteins.
Has high resistance to stretching, strong but flexible.
an example of pleated sheet
- silk protein (fibrous protein) of a spider web.
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iii. Tertiary structure
Tertiary structure is determined by interactions between R groups,
rather than interactions between backbone constituents.
- it is the overall three dimensional shape of polypeptide.
- the structure is formed by the folding and coiling of the secondary structure of
polypeptide chains to form a precise, compact globular protein which
determines its functions.
These interactions between R groups (to maintain three dimensional
shape) include:
- hydrogen bonds
- ionic bonds
- hydrophobic interactions
- van der Waals interactions
Strong covalent bonds called disulfide bridges reinforce the proteins
structure.
- form where two cysteine monomers (amino acid with sulfhydryl groups, -SH)
are brought close together by the folding of the protein.
Hydrophobic interaction is the clustering of hydrophobic
non-polar side chains away from water. Once non-polar
side chains are close together, van der Waals interactions
hold them together.
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Globular proteins such as enzymes, hormones, antibodies, plasma
proteins and myoglobin are examples proteins with tertiary
structure.
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iv. Quartenary structure
Quaternary structure results when a protein consists of multiple
polypeptide chains.
Examples:
- the protein hemoglobin that carries oxygen contains four globular
polypeptide chains, two - and two -polypeptide chains each
containing an iron-containing heme group.
- collagen, that has helical subunits intertwined into a larger triple
helix, giving the long fibers great strength.
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2. Types of structure protein
Two types on how protein classified according to their structure
i. Fibrous proteins
long parallel polypeptide chains.
most of it have the secondary structure (helical structure of pleated
sheets held by hydrogen bonds).
stable structures and are insoluble in water- important in carrying out its
structural and supporting function (formation of body structures of animals).
examples: keratin, collagen, elastin.
ii. Globular proteins
coiled and folded into globular shape (form a sphere).
have tertiary structures (that determines its metabolic functions) and
some also have quaternary structures.
unstable structure.
soluble in water, but being a very large molecule, it cannot dissolve
completely in water - form colloidal suspension.
examples: haemoglobin, myoglobin, enzymes, antibodies and some
hormones.
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3. Composition of protein
Proteins are classified according to their composition.
i. Simple protein
pure proteins that do not contain any other substance.
examples: fibrous proteins and globular proteins.
consists only of amino acids
do not contain any other substance
Examples:
- Albumins : egg albumin, serum albumin
- Globulins : antibodies, fibrinogen
- Histones : protein associated with DNA
- Scleroprotein : keratin, collagen
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ii. Conjugated protein
contain protein and non protein material (prosthetic
group).
prosthetic group-plays an important role in the
functioning of the protein.
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Table 5-1
4. Function of protein
97
Denaturation of Proteins
Three dimensional structure of a protein is relatively unstable structure
due to the presence of weak hydrogen, ionic bonds and hydrophobic
interactions.
Alterations in pH, salt concentration, temperature, or other
environmental factors can cause a protein to unravel.
1. pH= breaking ionic bonds
2. salt concentration= disruption of the ionic bonds
3. temperature= breaking the hydrogen and ionic bonds
4. organic solvents & detergents= disruption of hydrophobic interactions
5. mechanical force= break the weak hydrogen bonds
This loss of a proteins native structure is called denaturation.
A denatured protein is biologically inactive.
98
Fig. 5-23
Normal protein Denatured protein
Denaturation
Renaturation
High temperatures or various chemical treatments will denature a protein, causing
it to lose its shape and hence its ability to function. But often renatured when the
chemical and physical aspects of its environment are restored to normal in
certain situation.
Denaturation and Renaturation of A Protein.
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9. LIPID
100
Lipids
One class of large biological molecules.
Do not form true polymers.
Contain carbon, hydrogen and oxygen.
Lipids are characterized by physical property:
their solubility not chemical structure.
trait: they mix poorly in water.
101
Lipids
= hydrophobic because they consist mostly of hydrocarbons.
= have some polar bonds associated with oxygen though they are
hydrophobic.
= having little or no affinity for water, thus soluble in organic solvent
such as alcohols, ether and chloroform.
Three most biologically important lipids:
1. Triglycerides (fats and oil)
2. Phospholipids
3. Steroids
Other group of lipid waxes (water proof)
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103
1.Triglycerides (Fats)
Usually known as fats or oils.
The most common lipids.
Fats separate from water because water molecules form hydrogen
bonds with each other and exclude the fats.
Fats are constructed from two types of smaller molecules:
- Glycerol = three-carbon alcohol with a hydroxyl group
(-OH) attached to each carbon.
- A fatty acid = has carboxyl group (-COOH) attached to a
long carbon skeleton.
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How to make Triglyceride?
1 Glycerol + 3 Fatty acids = Triacylglycerol/ triglyceride + 3 Water
(removed)
- Three molecules of fatty acids are joined to one molecule of glycerol by
an ester linkage to become an ester compound- triglyceride.
- In glycerol, 3 hydroxyl group form ester bonds with 3 carboxyl groups
of fatty acids via esterification process.
- three molecule of water is removed.
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106
Fatty Acids
Fatty acids vary :
1. length (number of carbons).
2. in the number and locations of double bonds.
Two types of fatty acid
- Saturated fatty acid.
- Unsaturated fatty acid.
107
Saturated fatty acids
Saturated fatty acids have the maximum number of
hydrogen atoms possible and no double bonds.
Saturated fatty acids are straight molecules.
They have flexibility to pack together tightly and are solid in
room temperature.
Fats made from saturated fatty acids are called saturated
fats.
Most animal fats are saturated. Example: stearic acid
(C
17
H
35
COOH).
108
A diet rich in saturated fats may
contribute to cardiovascular disease
(atherosclerosis) through plaque
deposits within the walls of blood vessels.
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Unsaturated fatty acids
Unsaturated fatty acids have one or more double
bonds.
Unsaturated fatty acids are bent molecules. The number
of bends is dependent on the number of unsaturated
bonds in the molecule.
The kinks where the cis double bonds are located
prevented the molecules from packing together closely
enough to solidify at room temperature.
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111
Fats made from unsaturated fatty acids are called
unsaturated fats or oils, and are liquid at room
temperature.
Plant fats and fish fats are usually unsaturated.
Example:
oleic acid (C
17
H
33
COOH)-one double bond, linolenic acid
(C
17
H
29
COOH)- 3 double bonds.
linolenic acid
112
How to convert unsaturated fats to saturated fats?
Answer: Hydrogenation
Hydrogenation is the process of converting unsaturated fats
to saturated fats by adding hydrogen.
This is to improve the texture and keep the quality of oil-
based fats.
Hydrogenating vegetable oils also creates unsaturated fats
with trans double bonds.
These trans fats may contribute more than saturated fats to
cardiovascular disease.
113
2. Phospholipids
Cells could not exist without another type of lipid-phospholipids.
Phospholipids are the major component of all cell membranes
Two fatty acids and a phosphate group are attached to glycerol.
The two fatty acid tails are hydrophobic, but the phosphate group and
its attachments form a hydrophilic head.
114
Fig. 5-13
(b) Space-filling model (a) (c) Structural formula Phospholipid symbol
Fatty acids
Hydrophilic
head
Hydrophobic
tails
Choline
Phosphate
Glycerol
H
y
d
r
o
p
h
o
b
i
c

t
a
i
l
s
H
y
d
r
o
p
h
i
l
i
c

h
e
a
d
115
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.
116
Bilayer structure formed by self-assembly of phospholipids in an aqueous
environment.
117
3.Steroids
Steroids are lipids characterized by a carbon skeleton consisting of four
fused rings.
- Do not contain fatty acids.
Classified as lipids- insolubility in water
The various steroid groups differ from one another by the functional
groups or side groups attached to that ring.
Cholesterol, an important steroid,
1. is a component in animal cell membranes- maintain fluidity.
2. starting material for making other steroids, eg sex hormones.
Although cholesterol is essential in animals, high levels in the blood may
contribute to cardiovascular disease
118
Fig. 5-15
Cholesterol
119
120
Type Function Description Uses
Fats Respiratory substrate Released energy
when oxidised
Butter
For energy storage Excess energy is
stored in the form
of fat
As heat (thermal) and
electrical insulator
Fat deposited as
adipose tissue
(heat insulator)
Fat acts as an
electrical insulator
(myelin sheath of
nerve cells)
To protect internal organs Fat provides
support
(abdomen)and
protection
(kidney)
Types and Major Function of Lipid
121
Type Function Description Uses
Oils For energy
storage
Long-termenergy storage in
plants and seeds
Cooking oils
Phospholipids A component of
plasma
membrane
Providing
structural
support
Involved in formation of cells
Important component of
plasma membrane, nuclear
membrane and the myelin
sheath
Non-stick
pan spray
Steroids Precursor for
steroid hormones
All steroid hormones are
synthesized from cholesterol
Medicines
SUMMARY OF MACROMOLECULES
122
Functional Group & Water
The seven functional groups that are most important in the chemistry of life:
1. Hydroxyl group ( - OH )
2. Carbonyl group ( C = O )
3. Carboxyl group ( - COOH )
4. Amino group ( - NH
2
)
5. Phosphate group ( - OPO
3
2-
)
6. Sulfhydryl group ( - SH )
7. Methyl group ( - CH
3
)
123
Water properties due hydrogen bonding.
Waters life supporting properties:
1. Cohesive behavior
2. Ability to moderate temperature
3. Expansion upon freezing
4. Versatility as a solvent
124
CARBOHYDRATE
Monosaccharides are simple sugars. Usually found as trioses, pentoses
and hexoses AND exist either as aldose or ketose sugar.
Most monosaccharides found in organisms have 6 carbons. Eg, glucose
(because it is mostly utilised by cells for quick energy).
Dissacharides contain two monosaccharides joined by dehydration reaction
creating a glycosidic bond.
lactose, maltose and sucrose are dissacharides.
Polysaccharides are polymers of monosaccharides. They are not soluble
in water and do not pass through the plasma membrane of the cell. They
role as energy storage and structural support.
starch, glycogen, cellulose, chitin and peptidoglycan are polysaccharides
125
LIPID
Lipids are hydrocarbons that are insoluble in water because most of them
are hydrophobic.
Some has polar bond.
They include fats and oil (triglycerides), phospholipids and steroids.
Fats and oil are triglycerides used primarily for long term energy storage.
They are formed via dehydration creating an ester bond.
Saturated fatty acid- no double bonds between their carbon atoms, solid at
room temperature.
Unsaturated fatty acid- have double bonds in the carbon chain, liquid at
room temperature.
Phospholipids are important component in cell membrane.
Steroids have a skeleton of four fused carbon rings and vary according to
the attached functional groups that determine the biological functions of the
various steroid molecules
126
PROTEIN
Amino acids are building block of proteins. Amino acids contain acidic
carboxyl group, a basic amino groups, a hydrogen atom and an R
group.
Amino acid differ according to their side chains, R group.
There are 20 amino acids commonly found in cells and they can be
grouped into polar, non polar, electrical charges (acidic and basic
groups).
A peptide bond is a covalent bond formed between two amino acids.
Therefore, linking many amino acids via peptide bond= polypeptide.
Protein shape determines its function. Protein can have up to four levels of
structure (primary, secondary, tertiary, quartenary).
Based on the level of structure, there are fibrous protein and globular
protein.
Protein play important roles in support, enzymes, transport, defense,
hormones, motion etc.
127
Nucleic Acids
Nucleic acids are polymers of nucleotides with very specific functions in
cells.
Nucleotides are molecular complex comprising three types of molecules; a
phosphate group, a pentose sugar, and a nitrogen containing base.
DNA stores the genetic code for its own replication and for the amino
acid sequences in proteins that is needed by an organism.
RNA allows for translation of the DNA genetic code into amino acid
sequences of proteins. They are three types of RNA; rRNA, tRNA and
mRNA.
128
Fig. 5-UN2
129
Fig. 5-UN2a
130
Fig. 5-UN2b
131
EXERCISE
OPEN FILE
1. PROTEIN
2. CARBOHYDRATE
3. LIPID
4. NUCLEIC ACID
132