34 1 Cell Structure and Functions

Skills: Analyzing, Interpreting and Communication

 Compare and contrast the structure and function of mitochondria with those of chloroplasts.
 Compare in tabular form, the functions of organelles with the processes occurring in animals and
plants.
 List the structure and molecules, which can cross the nuclear envelope.

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Exercise

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MCQs

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1. Select the correct answer
(i) Which of the following is the major advantage of using a light microscope instead of
an electron microscope? .o
(A) superior resolving power
(B) constant depth of focus
(C) observation of living matter
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(D) use of very thin sections
(ii) Some cellular organelles are bound by a single membrane, while other organelles
.n

have two membranes (envelopes) around them. Which one of the following is
correct?
Single membrane Double membranes
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(A) peroxysomes, lysosome nucleus, chloroplast

(B) chloroplast, lysosome nucleus, peroxysomes
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(C) nucleus, chloroplast lysosome, peroxysomes

(D) nucleus, lysosome chloroplast, peroxysomes
(iii) Which of the following cell structures contains the highest concentration of RNA?
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(A) centriole (B) lysosome

(C) chromosome (D) nucleolus
(iv) A tadpole’s tail is gradually broken down during metamorphosis into an adult frog.
Which organelle increases in number in the cells of the tail at this time?
(A) centriole (B) endoplasmic reticulum
(C) Golgi complex (D) lysosomes
(v) Which of the following organelles always contains DNA?
(A) centriole (B) Golgi complex
(C) lysosome (D) mitochondria
 1 Cell Structure and Functions 35
(vi) Which distinguishes a prokaryotic cell from a eukaryotic cell?
(A) prokaryotic cell have a cell wall and a nucleus
(B) prokaryotic cells have no membrane bound organelles
(C) prokaryotic cells have a centriole
(D) prokaryotic cells have no ribosomes
(vii) The elasticity of the plasma membrane demonstrates that it is made up in part of
(A) lipids (B) nucleic acids (C) carbohydrates (D) proteins
(viii) Filaments present in flagella and cilia are
(A) microfibrils (B) microtubules

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(C) microfilaments (D) microvilli
(ix) Which of the following structure is found in all living organisms:

.p
(A) cell membrane (B) nucleus
(C) lysosome (D) vacuole
(x) The cell wall of plant cell is different from that of prokaryotes in:

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(A) both structure and chemical composition
(B) structure only
(C) chemical composition only
.o
(D) number of layers only
(xi) Which of the following are present in prokaryotic cells:
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(A) chloroplast, DNA, nuclear envelope
(B) chromosomes, mitochondria, nuclear envelope
(C) cytoplasm, DNA, mitochondria
.n

(A) cytoplasm, DNA, ribosome

(xii) Which of the following is present in all eukaryotic cells:
(A) cell wall (B) diploid nucleus
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(A) flagellum (A) membrane bounded organelles

(xiii) Which of the following would be more prominent in a secretory cell than non-
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secretory cell:
(A) lysosome (B) Golgi complex
(C) mitochondrion (D) ribosome
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(xiv) When a glycoprotein is being synthesized for secretion from a cell, which rout e is
it most likely to take?
(A) Golgi complex  RER SER
(B) RER Golgi complex  SER
(C) RER SER Golgi complex
(D) SER Golgi complex  RER
(xv) Which one of the following is responsible for cyclosis?
(A) microtubule (B) microfilament
(C) intermediate filament (D) none of them
36 1 Cell Structure and Functions

Short Questions
2. What are the applications of chromatography and electrophoresis?
3. Write the difference between:
(a) resolution and magnification
(b) plant cell wall and bacterial cell wall
(c) cytoplasm of eukaryotic and prokaryotic cell
(d) flagella of eukaryotic and prokaryotic cell
(e) rough ER and smooth ER.

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(f) chromatin and chromosome.

.p
4. Name three organelles revealed by an electron microscope.
5. What holds the ribosomes together in a polysome?
6. Why lysosomes are called suicide bags?

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7. How and where lysosomes are formed in the cell?
8. Name the structures and organelles which are common in plant cell, animal cell and a
prokarytic cell. .o
9. How is a chloroplast similar to a bacterium?
10. What would happen if there are no lysosomes in human cells?
11. Draw a labelled diagram of a section through:
bf
(a) mitochondrion (b) bacterium
(c) chloroplast
12. What are lysosomal storage diseases? Give example.
.n

13. Name the organelles of cells that are highly specialized to do

(a) protein synthesis (b) actively transport substances into the cell
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(c) synthesis of lipids (d) phagocytize foreign substances

14. Why cell wall is not present in animal cells?
15. List the structure and molecules, which can cross the nuclear envelope.
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16. Why do eukaryotic cells need both membranous organelles and cytoskeleton?
17. List the structures missing in prokaryotic cells.
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18. Differentiate between the patterns of cell division in prokaryotic and eukaryotic cells.
19. Compare microfilaments and microtubules.
20. Why ER is present in all eukaryotic cells but not in prokaryotic cells?
21. Write a very brief notes on: (a) mesosomes (b) plasmids (c) nucleoid (d) cell surface
makers (e) vacuole (f) plastids
22. What organelles are single and double layer membranes?

Extensive Questions
23. List the principles and identify the apparatus used in the techniques of:
 1 Cell Structure and Functions 37
(a) Fractionation
(b) Microdissection
(c) Tissue culture
(d) Differential staining
(e) Centrifugation
(f) Chromatography
(g) Electrophoresis
(h) Spectrophotometry
24. Describe the locations, chemical compositions and significance of the primary and
secondary cell wall and of middle lamella in a plant cell.

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25. Explain the (a) chemical composition of plasma membrane (b) role of plasma membrane
in regulating cell’s interactions with environment.

.p
26. (a) Relate the lipid foundation and variety of proteins of the plasma membrane.
(b) Identify the role of glycolipids and glycoproteins as the cell surface markers.

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27. What are the functions of the plasma membrane proteins?
28. What is the chemical nature of cytoplasm? Explain the metabolic roles of cytoplasm.
29. Distinguish between smooth and rough endoplasmic reticulum in terms of their structures
and functions.
30.
.o
Explain the structure, chemical composition and function of ribosomes.
31. Explain the structure, and functions of Golgi complex.
bf
32. Explain the structure, and functions of the peroxysomes and glyoxisomes in animal and
plant cells.
33. (a) Describe the formation, structure and functions of the lysosomes.
.n

(b) Interpret the storage diseases with reference to the malfunctioning of lysosomes.
34. Explain the external and internal structure of mitochondrion and interlink it with its function.
35. Explain the external and internal structure of chloroplast and interlink it with its function.
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36. Compare and contrast the structure and functions of mitochondria and chloroplasts.
37. Describe the structure, composition and functions of centriole.
38. Describe the types, structure, composition and functions of cytoskeleton.
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39. How cytoskeletons are important to eukaryotic cells?

40. Explain the structure of cilia and flagella and the mechanism of their movement.
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41. Describe the chemical composition and structure of nuclear envelope.

42. Compare the chemical composition of nucleoplasm with that of cytoplasm.
43. Explain that nucleoli are the areas where ribosomes are assembled.
44. Describe the structure, chemical composition and function of chromosome.
45. Describe the composition of cell wall in a prokaryotic cell.
46. Describe the structure of bacteria as a model prokaryotic cell.
47. What is the relationship of endoplasmic reticulum with Golgi complex, lysosome and
plasma membrane?
 2
BIOLOGICAL MOLECULES
This is a 21 days unit

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2.1 Biological Molecules in Protoplasm (2 Periods)

.p
2.2 Importance of Water (1 Period)
2.3 Carbohydrates (4 Periods)
2.4 Proteins (4 Periods)

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2.5 Lipids (4 Periods)
2.6 Nucleic Acids (5 periods)
2.7 Conjugated Molecules (1 Period)
.o
Reading
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You have got a very brief introduction about biological molecules in IX-X biology course.
This chapter caters the detailed study of carbohydrates, proteins, lipids and nucleic acid as well
.n

as the importance of water and the role of conjugated molecules.

2.1 BIOLOGICAL MOLECULES IN PROTOPLASM

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Biological molecules or biomolecules are different chemical compounds of living

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beings. Biochemistry is the branch of biology that deals with such molecules. It also deals with
various chemical reactions (metabolism) of living beings. Biochemistry helps biologists to
understand anatomy, physiology, pharmacology, biotechnology, bioinformatics etc.
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2.1.1 Chemical Composition of Protoplasm

Approximately 25 elements out of 92 naturally occurring elements of earth are found in
living beings. These are called biogenic or bioelements. However, human body is composed
of only 16 of these bioelements. These elements can be classified on the basis of their
proportions in organisms. The six commonest bioelements that constitute 99% of protoplasm
are called major bioelements. Minor bioelements are those that are found as less than 1%
whereas those that are found as less than 0.01% of the protoplasm are called trace elements.
The proportions of these elements are given in the fig: 2.1. Some trace elements such as iron
are needed by all forms of life. Others are required only by certain species.
 2 Biological Molecules 39
The bioelements are combined with each other and can form thousands of different
biomolecules which may be inorganic (water and minerals) and organic (carbohydrates, lipids,
proteins and nucleic acids). The proportions of these biomolecules are given in the table 2.1.

k
.p
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.o
Minor elements include: potassium (0.35%), sulphur (0.25%), chlorine (0.15%), sodium
bf
(0.15%) and magnesium (0.05%).
Trace elements include iron, copper, manganese, zinc and iodine.

Fig. 2.1: Proportions of various bioelements in human body

.n

Table 2.1: Proportions of various biomolecules in bacterial and

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mammalian cells

Biomolecules Bacterial cell Mammalian cell

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Water 70% 70%

Protein 15% 18%
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Carbohydrates 3% 4%
Lipids 2% 3%
DNA 1% 0.25%
RNA 6% 1.1%
Other organic molecules (enzymes, 2% 2%
hormones, metabilites)
Inorganic ions (Na+, K+, Ca++, 1% 1%
Mg++, Cl-, SO4--)
40 2 Biological Molecules
The four fundamental kinds of biological molecules are carbohydrates, proteins, lipids
and nucleic acids. Carbohydrates are present in the inclusions of the cells and provide fuel for
the metabolic activities of the cell. Proteins are present in the membranes, ribosomes,
cytoskeleton and enzymes of the cell. Lipids are present on the membranes of Golgi complex
and inclusion of the cell. Lipids provide a reserved energy source, shape, protect and insulate
the cells. The nucleic acid DNA is present in the chromosome. It controls the cell activity. The
nucleic acid RNA is present in the nucleoplasm and cytoplasm. It transmits genetic information
and takes part in protein synthesis.

2.1.2 Condensation and Hydrolysis

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A macromolecule is high molecular
weight compound which is made from many

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repeating units. Molecules built like this are also
known as polymers. The individual units of

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polymers are micromolecules which are also
known as monomers. The interconversions of
Fig: 2.2: Monomer and polymer
these molecules are carried out by condensation
and hydrolysis.
.o During condensation, when two monomers
join, a hydroxyl (–OH) group is removed from one
bf
Science Titbits monomer and a hydrogen (–H) is removed from the
Do not confuse involvement of water in
other to make water and as a result a bond is
hydrolysis with making a solution, in which the
role of water is to act as a solvent, rather than synthesized between the monomers. The product
.n

taking part in a chemical reaction. Hydration is of such reaction is called a dimer. If the same
yet another completely different process, reaction is repeated several times the resulting
involving the addition of water, but not breaking molecule will be a polymer. Condensation is also
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of bonds. Also do not assume that this

called dehydration synthesis because water is
breakdown releases energy, which is usually
produced when the simpler substances are removed (dehydration) and bond is made
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oxidized in respiration. (synthesis). Condensation does not take place

unless the proper enzyme is present and the
monomers are in an activated energy- rich form.
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The hydrolysis is essentially the reverse of

condensation i.e., the breakdown of a polymer into
its monomers by the addition of water. During
hydrolysis, an (–OH) group from water is attached
to one monomer and (–H) is attached to the other
monomer. Actually all (food) digestion reactions are
examples of hydrolysis, which are controlled by
enzymes such as carbohydrases, proteases,
Fig. 2.3: Condensation and Hydrolysis lipases, nucleases.
 2 Biological Molecules 41

2.2 IMPORTANCE OF WATER

Water is one of the main constituents on earth. More than two thirds of the earth is
covered by water. Approximately 70 percent of the any organism is formed of water. Water is
the most abundant component in any organism, the Critical Thinking
lowest is 20% in seeds and bones and highest is When hydrogen gas combines with oxygen
85-90% in brain cells. Jellyfish has exceptionally gas to form water, is the hydrogen reduced or
large amount of water i.e., 99% (hence the body oxidized?
shows transparency).
2.2.1. Properties of water

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The properties of water that make it the cradle of life

.p
are :
1. High polarity

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The bonds which are formed by the mutual sharing
of electrons between two atoms are called covalent
bonds. Normally the sharing of electrons between two
Fig: 2.4: Polarity of water molecule
atoms is fairly equal and the covalent bond is nonpolar.
.o
In the case of water, however the sharing of electrons between oxygen and hydrogen is
not completely equal so the covalent bond is polar. A polar covalent bond is a chemical
bf
bond in which shared electrons are pulled closer to the more electronegative atom, making
it partially negative and the other atom partially positive. Thus, in H 2O, the O atom actually
has a slight negative charge and each H atom has a slight positive charge, even though
.n

H2O as a whole is neutral. Because of its polar covalent bonds, water is a polar molecule
i.e., it has a slightly negative pole and two slightly positive ones.
This is polarity of water molecules that makes it an excellent or universal solvent for
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polar substances. Ionic compound or electrolytes can be easily dissolved in water, non-polar
substances having charged groups in their molecules can also be dissolved in water. Such
compounds when dissolved in water, dissociates into positive
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and negative ions and are in more favourable state to react

with other molecules and ions. This is the reason why all
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chemical reactions in living beings occur in aqueous medium.

2. Hydrogen bonding
The polarity of water molecules makes them interact
with each other. The charged regions on each molecule are
attracted to oppositely charged regions on neighbouring
molecules, forming weak bonds. Since the positively charged
region in this special type of bond is always an H atom, the bond
is called a hydrogen bond. This bond is often represented by
a dotted line because a hydrogen bond is easily broken. Fig: 2.5 Hydrogen bonds between
water molecules
42 2 Biological Molecules
Because of hydrogen bonding, water is a liquid at temperatures suitable for life. The high
cohesion and adhesion force of water is due to the presence of hydrogen bonds in water, which
in turns makes water as transport medium.
3. Cohesion and adhesion
Cohesion is the attraction among the water molecules which enables the water
molecules to stick together. Water flows freely due to cohesion. Water molecules also have
attraction to polar surfaces. This attraction is called adhesion. Both cohesion and adhesion are
due to hydrogen bonds among water molecules. These properties of water enable it to circulate
in living bodies and to act as transport medium.

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4. High specific heat
Heat capacity can be defined as the amount of heat required for minimum increase (1 oC

.p
or 1oK) in temperature of a substance. The specific heat capacity of water can be represented
as number of calories required to raise the temperature of 1g of water up to 1 oC i.e., 1 Calorie

rg
(4.18 Joules). Water has relatively a very high heat capacity than any other substance due to
its hydrogen bonding, because much of the heat absorbed by water is utilized in the breakdown
of hydrogen bonding therefore it does not manifest itself to raise the temperature of water.
Hence, very large amount of heat can increase very little in temperature in water. Due to its high
.o
heat capacity water works as temperature stabilizer or regulator for organisms in the hot
environment and hence protects the living material against sudden thermal changes.
bf
5. High heat of vapourization
Heat of vapourization is the amount of heat required to convert a unit mass of a liquid
into gaseous form. Heat of vapourization of water is represented as number of calories
.n

absorbed per gram vapourized. Water has high heat of vapourization i.e., 574 calories per
gram. The high heat of vapourization means that a large amount of heat can be lost with
minimal loss of water from the body. This is high heat of vapourization of water that gives
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animals an efficient way to release excess body heat in a hot environment. When an anima l
sweats, body heat is used to vapourize the sweat thus cooling the animal. Due to this property
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of water, evaporation of only 2 ml out of one litter of water lowers the temperature of the
remaining 998 ml water by 1oC.
6. Hydrophobic exclusion
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Hydrophobic exclusion can be defined as

reduction of the contact area between water and
hydrophobic substances which are placed in
water. For example, if you place few drops of oil
on the surface of a water solution, the oil drops will
tend to coalesce (to unite into one whole) into a
single drop. Biologically, hydrophobic exclusion
plays key roles in maintaining the integrity of lipid
Fig: 2.6: Hydrophobic exclusion
bilayer membranes.
 2 Biological Molecules 43

7. Ionization
The dissociation of a molecule
into ions is called ionization. When
water molecule ionizes, it releases an
equal number of positive hydrogen and
negative hydroxyl ions.
This reaction is reversible but
Fig: 2.7: Ionization of water
equilibrium is maintained at 25oC. The
H+ and OH- ions affect and take part in many of the

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reactions that occur in cells, e.g., it helps to maintain
or change the pH of the medium.

.p
8 Lower density of ice
Ice floats on water. This is because ice is less

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dense than water. The reason is that ice has a giant
structure and show maximum number of hydrogen
bonding among water molecules; hence, they are
.o
arranged like a lattice. In freezing weather, ice forms
on the surface of ponds and lakes forming an
insulating layer above the water below. This Fig: 2.8: Lattice likes arrangement of water
bf
provides a living environment for some organisms molecules in ice
until the ice melts. Organisms can also live under the ice.
.n

Skills: Analyzing, Interpreting and Communication

 Draw model diagrams to describe the hydrogen bonding.
 Develop a table to align the properties of water with the benefits to life.
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2.3 CARBOHYDRATES
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Carbohydrates are the compounds of carbon, hydrogen and oxygen. Literally word
carbohydrate means “hydrates of carbon” i.e., a carbon associated with water or any compound
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composed of carbon, hydrogen and oxygen and in which

hydrogen and oxygen are found in the same ratio as they
are found in water (2:1), can be called carbohydrate.
Although this definition is applied on many carbohydrates
like glucose (C6H12O6), sucrose (C12H22O11), and the
starches and cellulose (C6H10O5)n but some compounds
containing hydrogen and oxygen in the same ratio as they
are found in water (2:1), are actually not carbohydrates
e.g., acetic acid (C2H4O2) and lactic acid (C3H6O3).
Moreover, there are also some carbohydrates, such as Fig: 2.9: Chemical nature of carbohydrates
44 2 Biological Molecules
rhamnose (C6H12O5)n which do not contain hydrogen and oxygen in the ratio of water. Hence
the classical concept of carbohydrates as hydrates of carbon is now supposed to be incorrect
and a more valid definition of these compounds is suggested as:
“Polyhydroxy aldehyde or polyhydroxy ketone or those compounds which upon hydrolysis
yield such compounds (derivatives) are called carbohydrates”.

2.3.1 Classification of Carbohydrates

Carbohydrates are commonly known as sugars because more familiar carbohydrates
have sweet taste. In Greek, “sakcharon” word is used for sugars, so the term saccharide is
derived from this word. Therefore carbohydrates are also called saccharides. A polyhydroxy

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aldehyde or polyhydroxy ketone is supposed to be single saccharide units, whereas, the

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derivative carbohydrates are composed of more than one saccharide units.
Classification of carbohydrates is based upon number of saccharide units. Carbohydrates
are generally classified into three group i.e., monosaccharides, oligosaccharides and

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polysaccharides.
Table: 2.2: Comparison of characteristics of carbohydrates
Monosaccharides
.o Oligosaccharides Polysaccharides
They consist of single saccharide They are composed of 2 to 10 They are composed of more than
unit. saccharide units. 10 saccharide units.
bf
They are simplest carbohydrates; They have less complex structure, so They have highly complex
therefore, they cannot be further upon hydrolysis they yield at least 2 structure, so upon hydrolysis they
hydrolyzed. and maximum 10 monosaccharides. yield at least 11 monosaccharides.
.n

They are highly soluble in water. They are less soluble in water. They are generally insoluble in
water.
They are sweetest among all They are less sweet in taste. They are tasteless.
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carbohydrates.

2.3.1.1 Monosaccharides
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Monosaccharides are true carbohydrates which are either polyhydroxy aldehydes or

polyhydroxy ketones. The range of number of carbons in monosaccharide is 3 to 7. All the
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carbon atoms in a monosaccharide except one, have a hydroxyl group (-OH) while the
remaining carbon atom is either the part of aldehyde or ketone. The general formula for
the representation of monosaccharides is C nH2nO n, where, n is the number of carbon atoms
in monosaccharides.
Classification of monosaccharides
Classification of monosaccharides is based upon functional group and number of carbon
atoms. On the basis of functional group, the monosaccharides containing aldehyde are called
aldoses while those containing ketone are called ketoses. On the other hand monosaccharides
are classified into five groups based upon number of carbon atoms i.e., trioses (3C), tetroses
(4C), pentoses (5C), hexoses (6C) and heptoses (7C).
 2 Biological Molecules 45
Table: 2.3: Examples and functions of monosaccharide
Class Formula Aldoses Ketoses Function
Trioses C3H6O3 Glyceraldehyde Dihydroxy Intermediates in photosynthesis and cellular
(3C) acetone respiration.
Tetroses C4H8O4 Erythrose Erythrulose Intermediates in bacterial photosynthesis.
(4C)
Pentoses C5H10O5 Ribose, Ribulose Ribose and deoxyribose are components of
(5C) Deoxyribose RNA and DNA respectively.
(C5H10O4)
Ribulose is an intermediates in photosynthesis.

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Hexoses C6H12O6 Glucose, Fructose Glucose is respiratory fuel (initial substrate)

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(6C) Galactose
Fructose is an intermediate in respiration.
Galactose is the component of milk sugar.
Heptoses C7H14O7 Glucoheptose Sedoheptulose Intermediates in photosynthesis.

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(7C)

Chemical structures of monosaccharides.o

Monosaccharides are usually found in open chain
structure in crystalline form but when they are dissolved in water
most of them (pentoses and hexoses) are converted into ring
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chain structure. Two types of ring structures are found in Fig: 2.10: Types of rings in
monosaccharides i.e., furanose and pyranose. monosaccharides
.n

Furanose is a five membered ring in which one oxygen atom and four carbon atoms are
found, oxygen atom is linked with C1 and C4. All pentoses and ketohexoses are converted into
furanose ring.
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Pyranose is a six membered ring in which one oxygen atom and five carbon atoms are
found, oxygen atom is linked with C1 and C5. Only aldohexoses are converted into pyranose
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ring.
Let us understand it by taking ribose as an
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example. Ribose is an aldopentose, with the molecular

formula C5H10O5. It can exist in open chain structure in
dried form but it exists in furanose ring in aqueous
medium. When it is dissolved in water, the oxygen atom
from aldehyde group reacts with penultimate carbon
(second last carbon i.e., C4 in case of ribose) in this way
oxygen atom forms a link between C1 and C4 while the
OH group of C4 is shifted to C1. After this modification
ring structure of ribose is formed. The ring structure
demonstrated by Emil Fischer is called Fischer Fig: 2.11: Conversion of open chain into
ring chain
46 2 Biological Molecules
projection (a two dimensional representation of ring structure) while that represented by an
English chemist Norman Haworth is called as Haworth projection (a three dimensional
representation of ring structure).
Each pentose or hexose molecule in ring structure exists in either α or β form depending
upon the position of –H and –OH group on C-1. If –OH group is found downward on C-1 then it
is called α sugar and if –OH is present upward on C-1 then it is known as β sugar as shown
in the fig: 2.12.
Stereoisomerism in monosaccharides (Glucose)
Those isomers in which –H and –OH groups are arranged in different pattern to the

k
asymmetric carbon atoms are called stereoisomers. An asymmetric carbon atom is that

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which makes bonds with four different atoms around it. For example, in glucose, the C-2, C-3,
C-4 and C-5 are asymmetric carbon atoms. In
monosaccharide the number of stereoisomers;

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actually depends upon the number of asymmetric
carbons in its structure and can be calculated by
.o the formula 2n, where n is the number of
asymmetric carbon atoms so glucose has 16
stereoisomers. Stereoisomers can be classified
Fig: 2.12: α and β isomers of glucose in three groups:
bf
(i) Enantiomers: Those stereoisomers which are non-superimposable mirror images of one
another are called enantiomers. An example of an enantiomer is the D and L isomers of
glucose, as shown in figure 2.14. In D isomers (also called right handed form) the asymmetric
.n

carbon atom farthest from aldehyde group (second last carbon or C-5 in case of glucose also
called penultimate carbon) has –OH group on right side whereas in L isomers (also called left
handed form), the –OH group is projected on left side at penultimate carbon atom. Out of 16
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stereoisomers of glucose, 8 are enantiomers of other 8.

(ii) Diastereoisomers: Those stereoisomers
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which have different arrangement of –H and –

OH groups at more than one asymmetrical
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carbon atoms are called diastereoisomers.

Unlike an enantiomer, diastereoisomers are
not mirror images. For example, the two
carbohydrates that are diastereoisomers are
D-Glucose and D-Altrose.
(iii) Epimers: Those stereoisomers which
have different arrangement of –H and –OH
groups at only one asymmetrical carbon atom
Fig: 2.13: Asymmetric Fig: 2.14: An example of are called epimers. D-Glucose and D-
carbons enantiomers
Mannose are an example of an epimer.
 2 Biological Molecules 47

Laboratory Manufactured (Artificial) Sweeteners

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Fig: 2.15: Stereoisomers of D-glucose
Laboratory manufactured sugars such as tagatose, sucralose etc., are left-handed forms

.p
(L sugars). On the other hand the naturally occurring sugars in bodies are D sugars. Proteins
and cell receptors are designed to react only with particular enantiomers. For example the

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enzymes in your stomach can digest only right-handed sugars. Likewise left-handed sugars
cannot be metabolized by right-handed enzymes. Just as the glove fits only on the proper hand,
a right-handed enzyme cannot fit on or react with a left-handed substrate. The substrate must
fit on the proper active site of the enzyme. So for the left handed substrate (sweetener) the
enzyme must be left-handed.
.o
2.3.1.2 Oligosaccharides
bf
This group consists of derivatives of monosaccharides. Those carbohydrates which upon
hydrolysis yield 2 to 10 saccharide units are called oligosaccharides. On the basis of number of
saccharide units, the oligosaccharides are classified into disaccharides, trisaccharides,
.n

tetrasaccharides and so on. The most common among these are disaccharides.
Disaccharides
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Two monosaccharides combine to form a disaccharide. It is a kind of oligosaccharides.

Disaccharides are less sweet in taste and less soluble in water. These can be hydrolyzed to
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give monosaccharides. Examples are: maltose, lactose, sucrose. The general formula of
disaccharide is: C12 H22 O11. Some common disaccharides are as follows:
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Sucrose: It is commonly known as cane sugar because it occurs abundantly in sugarcane

beside it many other plants also have sucrose in considerable amount like sugar beet, pine
apple, sorghum and all sweet fruits. It is widely used as sweetener at homes for making sweet
dishes. In plants sucrose is also called transport disaccharide as prepared food in plants is
transported in the form of sucrose. Upon hydrolysis sucrose yields a molecule of α-glucose and
a molecule of β-fructose. Therefore, the sucrose is formed by the condensation of glucose and
fructose. In this reaction, the –OH group at C-1 of glucose reacts with the –OH group at C-2 of
fructose, liberating a water molecule and a linkage is formed between C-1 of glucose and C-2
of fructose known as α-1,2-glycosidic linkage.
48 2 Biological Molecules

Fig: 2.16: Formation of sucrose

k
Maltose: It is commonly known as malt sugar. It is an intermediate disaccharide produced

.p
during the breakdown of starch and glycogen. Maltose is generally found in germinating seeds.
In brewing industry the maltose is produced from the breakdown of barley starch by the help of
amylase enzyme. This process is known as malting. Upon hydrolysis it yields two molecules of

rg
α-glucoses. Therefore, the maltose is formed by the condensation of α-glucoses. In this reaction,
the –OH group at C-1 of one glucose reacts with the –OH group at C-4 of other glucose,
liberating a water molecule and a linkage is formed between C-1 of one glucose and C-4 of other
.o
glucose, known as α-1, 4-glycosidic linkage.
bf
.n
w
w

Fig: 2.17: Formation of maltose

Lactose: It is commonly known as milk sugar as it is found in milk of mammals i.e., 4-6% in
w

cow's milk and 5-8% in human milk. It is also a byproduct in the manufacture of cheese. Upon
hydrolysis it yields a molecule of β-galactose and a molecule of α-glucose. Therefore, the lactose
is formed by the condensation of β-galactose and β-glucose. In this reaction, the –OH group at
C-1 of galactose reacts with the –OH group at C-4 of glucose, liberating a water molecule and
a linkage is formed between C-1 of galactose and C-4 of glucose, known as β-1, 4-glycosidic
linkage.
 2 Biological Molecules 49

Fig: 2.18: Formation of lactose

k
Science Titbits

.p
Any carbohydrate which is capable being oxidized and causes the reduction of other substances without
having to be hydrolyzed first is known as reducing sugar, but those which are unable to be oxidized and do not
reduce the other substances are known as non-reducing sugars. All monosaccharides and two of three types

rg
of disaccharides (maltose and lactose) have the open chemical structure needed to act as reducing agents. The
third type of disaccharides, sucrose, and polysaccharides are non-reducing sugars.

2.3.1.3 Polysaccharides
.o
Those carbohydrates which upon hydrolysis yield more than ten monosaccharide units
bf
are called polysaccharides. This is largest group of carbohydrates. The polysaccharides which
are composed by the condensation of only one kind of monosaccharides are called
homopolysaccharides e.g., starch, glycogen, cellulose, chitin; whereas the polysaccharide
.n

which are composed by the condensation of different kind of monosaccharides are called
heteropolysaccharides e.g., agar, pectin, peptidoglycan. Polysaccharides function chiefly as
food and energy stores, e.g., starch, glycogen, and structural material, e.g., cellulose and chitin.
w

They are convenient storage molecule for several reasons. Their large size makes them more
or less insoluble in water, so they exert no osmotic or chemical influence in the cell; they fold
into compact shapes and they are easily converted to sugars by hydrolysis when required. Some
w

common polysaccharides e.g., starch, cellulose, and chitin are being discussed here.
Starch
w

Starch is a homopolysaccharides which is formed by the condensation of hundreds of

α-glucoses. It is storage carbohydrate of plants. It is mainly stored in root, stem and seeds.
Cereal grains and potato tubers are rich sources of starch in human diet. Starch is digested in
oral cavity and in small intestine by the enzyme amylase. Upon hydrolysis it yields maltose first
and then maltose is further digested by maltase enzyme and yields glucoses. The presence of
starch in a given sample can be confirmed by iodine test as it gives blue colour with iodine
solution. There are two types of starches i.e., amylose and amylopectin.
50 2 Biological Molecules

k
.p
rg
Fig: 2.19: Structure of starches
Amylose is un-branched i.e., a linear chain of glucoses in which glucoses are attached
.o
together by α-1, 4-glycosidic linkages. It is soluble in hot water only. On the other hand,
amylopectin has branched structure i.e., a linear chain of glucoses but more chains of glucoses
in the form of branches are also attached by α-1, 6-glycosidic linkages. It is completely
bf
insoluble in water.
Glycogen
.n

Like starch, glycogen is

also a homopolysaccharides
composed of α-glucoses. It is
w

storage carbohydrate of animals.

It is mainly stored in liver and
w

muscles. Therefore it is also

known as animal’s starch. The
digestion of glycogen is also quite
w

similar to that of starch. The

presence of glycogen in a given
sample can also be confirmed by
iodine test as it gives red colour
with iodine solution. Structure of
glycogen resembles with
Glycogen (Highly branched unlike amylopectin) amylopectin starch but glycogen
has much more branching than
Fig: 2.20: Structure of glycogen amylopectin.
 2 Biological Molecules 51

Cellulose
Cellulose is most abundant carbohydrate on earth. It is also a homopolysaccharides but
unlike starch and glycogen it is formed by the condensation of hundreds of β-glucoses. It is
structural carbohydrate of plants as it is major constituent of plant cell wall. Cotton and paper
are the pure forms of cellulose.
Cellulose shows no colour with iodine solution. Structure of cellulose resembles with
amylose starch in such a way that it has un-branched structure but it has β-1, 4-glycosidic
linkages between glucose residues. Therefore, in a cellulose chain, the β-glucoses are
alternatively arranged in upright and inverted manner.

k
.p
rg
.o
Fig: 2.21: Structure of cellulose
bf
Science Titbits
Cellulose cannot be digested by human body but it has to be taken into diet because it works as roughage or
.n

fibre so it prevents abnormal absorption of food in intestine. However, herbivore animals have some symbiotic
bacteria that secrete cellulase enzyme for its digestion. Upon hydrolysis it first yields a disaccharide, the
cellubiose and then cellubiose is further digested into glucoses.
w

Chitin
Chitin is the second most abundant organic molecule on earth. It is also a
w

homopolysaccharides. It is a structural carbohydrate found in the cell walls of fungi and in the
exoskeleton of arthropods. Due to the occurrence of chitin in fungal cell wall, it is also known as
w

fungal cellulose. Chitin is the derivative of N-acetyl glucosamine which is a modified form of

Fig: 2.22: Structure of chitin

52 2 Biological Molecules
glucose. It has an un-branched structure like cellulose in which alternative upright and inverted
N-acetyl glucosamine residues are linked together by β-1, 4-glycosidic linkages.
Skills: Analyzing, Interpreting and Communication
• Draw the ring forms of alpha and beta glucose.
• Illustrate the formation and breakage of maltose, sucrose and lactose.

2.4. PROTEINS
Proteins are the main structural components of the cell. All proteins contain C, H, O and
N, while some contains P, S. Few proteins have Fe, I and Mg incorporated into the molecule.

k
2.4.1 Structure of Proteins

.p
Chemically proteins can be defined as polymers of amino acids or polypeptide chains.
A protein may consist of a single polypeptide or more than one polypeptide.

rg
Amino acids
Amino acids are the building blocks of proteins. There are
many amino acids known to occur, but only 20 are commonly found
.o
in proteins. The amino acids are built on a common plan. Each
contains a carbon atom. It is called α (alpha) carbon to this a
hydrogen atom, an amino group (–NH2), a carboxyl group (–OOH)
bf
and a variable group known as –R group are attached. The R group
has a different structure in each of the 20 biologically important
amino acids and determines their individual chemical properties.
.n

Fig: 2.23 General structure

of an amino acid Two simplest amino acids i.e., glycine and alanine are shown in
figure 2.24.
w

Dipeptides and Polypeptides

Dipeptides and polypeptides are formed by the condensation of amino acids on the
w

ribosome under the instructions of mRNA which takes these instructions from DNA. This process
is known as translation. During this process, when an amino acid reacts with another amino
acid, the –OH from carboxylic acid group of one amino acid and –H from amino group of other
w

amino acid are liberated and form a water molecule, as a result a bond is established between

Fig: 2.24: Formation of a dipeptide and peptide bond

 2 Biological Molecules 53
C of carboxylic acid group and N of amino group of two amino acids called peptide bond.
Hence, a product of two amino acids is formed which is known as dipeptide.
A dipeptide has two ends; one is called amino or –N terminal end while other is called
carboxylic acid or –C terminal end. A new amino acid can be added in this chain from its
carboxylic acid or –C terminal end in the same way. Thus, a tripeptide (a product of three amino
acids) is formed and another water molecule is also released. Similarly, when several amino
acids are linked together by many peptide bonds, the polypeptide chain is formed.
Structural conformations in proteins
A linear polypeptide with a specific sequence and number of amino acid is called primary

k
structure. It is shown by all proteins at the time of their synthesis on ribosomal surface. After

.p
rg
.o
bf
.n
w
w
w

Fig: 2.25: Structural conformations in proteins

54 2 Biological Molecules
synthesis a protein does not remain in its primary structure but can be changed into some other
structural conformations (particular form, shape or structure). A helical (α-helix) or flattened
sheets (β-pleated sheet) like structures which are established by H-bonding between opposite
charge bearing groups of different amino acids are called secondary structures. In some
proteins the linear polypeptide is changed into α-helix, then α-helix fold again and again by ionic
bonds and disulfide bridges to form a globular shaped structure, the tertiary structure. Some
proteins exist in very complex structure in which more than one globule is attached together by
hydrophobic interaction. Such structures are called quaternary structures.
2.4.2 Significance of Amino Acid Sequence

k
Sequence of amino acid in a polypeptide is a characteristic feature of primary structure

.p
of protein which is responsible for proper functioning of protein. It is determined by the sequence
of nucleotide in DNA. Even due to point mutation (change of single or few nucleotides in DNA)
the sequence of amino acid in a particular protein (polypeptide) may be disturbed which causes

rg
severe defects in the body as it happens in sickle cell anemia, a hereditary disease.
Normal red blood cells are disc-shaped and look like doughnuts without holes in the
centre. They move easily through your blood vessels. Red blood cells contain an iron-rich
.o
protein called haemoglobin. This protein carries oxygen from the lungs to the rest of the body.
Normal haemoglobin (HbA) contains four polypeptides i.e. two α-chains which consist of 141
amino acids each and two β-chains which consist of 146 amino acids each.
bf
Sickle cell anemia is a serious disorder in which the body makes sickle or crescent
shaped red blood cells. Sickle cells contain abnormal hemoglobin called sickle haemoglobin
(HbS). Sickle haemoglobin causes the cells to develop a sickle, or crescent, shape. Sickle cells
.n

are stiff and sticky. They tend to block blood flow in the blood vessels of the limbs and organs.
Blocked blood flow can cause pain and organ damage. Sickle cell anemia is caused by a point
w

mutation in β-globin gene in which only one nucleotide is replaced by another which causes a
change in amino acid sequence of β-chain of hemoglobin. Sickle cell haemoglobin (HbS) shows
only one difference from HbA i.e., glutamic acid is replaced by valine at position number six in
w

β-chain.
w

Fig: 2.26: Difference in β-chain of HbA and HbS

 2 Biological Molecules 55

2.4.3 Classification of Proteins

Based upon structure and shape proteins can be classified into two groups i.e., fibrous
and globular.
Fibrous proteins
These proteins have fibre or filament like shape. Therefore, they exist in secondary
structure during function. These proteins are insoluble in aqueous medium, elastic in nature and
cannot be crystalized. Examples are: collagen, fibrinogen, actin, myosin and keratin.
Globular proteins

k
These proteins have spherical or globules like shape. Therefore, they exist in tertiary or
quaternary structure during function. These proteins are soluble in aqueous medium, inelastic

.p
in nature and can be crystalized. Examples are: enzymes, hormones, antibodies, channel
proteins.

rg
2.4.4 Role of Proteins
Proteins are very important molecules in our cells. They are involved in virtually all cell
functions. Each protein within the body has a specific function. Some proteins are involved in
.o
support or composition of body parts i.e., structural roles, while others are involved in various
physiological activities like bodily movement or in defence against germs i.e., functional roles. A
list of several types of proteins and their functions is given in table 2.4 and 2.5.
bf
Table: 2.4: List of structural proteins
Types Roles of proteins
.n

Collagen It establishes the matrix of bone and cartilages.

Elastin Elastin provides support for connective tissues such as tendons and
w

ligaments.
Keratin It strengthens protective coverings such as hair, nails, quills, feathers,
w

horns, and beaks.

Histone It arranges the DNA into the chromosome.
w

Table: 2.5 List of functional proteins

Types Roles of proteins
Enzymes The most of enzymes are protein which control metabolism i.e., they
speed up the biochemical reactions.
Hormones Some hormones are protein in nature which are involved in the
regulation of physiological activities such as regulation of glucose level,
calcium level, digestion, blood pressure etc.
56 2 Biological Molecules
Antibodies These proteins are produced by WBCs in response to antigen (a
foreign particle) and provide immunity.
Haemoglobin It is found in RBCs and is involved in the transport of oxygen mainly
and carbon dioxide to some extent.
Fibrinogen It is found in blood plasma and is involved in blood clotting process.
Ovalbumin and Ovalbumin is found in egg whites and casein is a milk-based protein.
Casein Both of them are involved in the storage of amino acids.

k
Skills: Analyzing, Interpreting and Communication
• Draw table to illustrate different structural and functional proteins with roles of each.

.p
• Illustrate the synthesis and breakage of peptide linkages.

rg
2.5 LIPIDS
Lipid is the collective name for variety of organic compounds such as fats, oils, waxes
.o
and fat-like molecules (steroids) found in the body. Therefore, it is defined as a heterogeneous
group of organic compounds which are insoluble in water (hydrophobic) but soluble in organic
solvent such as acetone, alcohol, and ether etc. Lipids are composed of carbon, hydrogen and
bf
oxygen as carbohydrates. However, they have relatively less oxygen in proportion to carbon
and hydrogen than do carbohydrates. For instance, tristearin is a simple lipid which shows
molecular formula as C57H110O6. Due to high contents of carbon and hydrogen, they contain
.n

double amount of energy than carbohydrates.

In general lipids are components of cell membranes (phospholipids and cholesterol), act
as energy stores (triglycerides), chemical messengers (steroid) and are also involved in
w

protection, waterproofing, insulation and buoyancy.

2.5.1 Classification of Lipids

w

Lipids are broadly classified into simple, complex and derived, which are further
w

subdivided into different groups. Simple lipids are esters of fatty acids with various alcohols
e.g., acylglycerols (fats and oils) and waxes. The compound/complex lipids contain other groups
in addition to an alcohol and a fatty acid e.g., phospholipids, glycolipids and lipoproteins. Derived
lipids are the derivatives of simple and complex lipids e.g., terpenes, steroids, prostaglandins
and cholesterols. Some examples such as acylglycerol, waxes, phospholipids, terpenes,
prostaglandin and steroids are discussed here.
Acylglycerol
The most abundant lipids in living things are acylglycerol. Chemically, acylglycerols can
be defined as esters of glycerol and fatty acids. An ester is the compound produced as the result
 2 Biological Molecules 57
of a chemical reaction of an alcohol with acid and a water molecule is released such a reaction
is called esterification.

k
Fig: 2.27: Esterification

.p
Glycerol is a trihydroxy alcohol which contains three carbons, each bears an OH group.
A fatty acid is a type of organic acid containing one carboxylic acid group attached to a
hydrocarbon. Fatty acids contain even number of carbons from 2 to 30. Each fatty acid is

rg
represented as R-COOH, where R is a hydrocarbon tail. When a glycerol molecule combines
chemically with one fatty acid, a monoacylglycerol (monoglyceride) is formed. When two fatty
acids combine with a glycerol a diacylglycerol (diglyceride) is formed and when three fatty
.o
acids combine with one glycerol molecule a triacylglycerol (triglyceride) is formed.
Triacylglycerols are also called neutral lipid as all three OH groups of glycerol are occupied by
fatty acids and charge bearing OH group is left.
bf
.n
w
w
w

Fig: 2.28: Formation of a triacylglycerol (neutral lipid)

Properties and types of fatty acids
About 30 different fatty acids are found. Fatty acids vary in length. Acetic acid (2C) and
butyric acid (4C) are simplest fatty acid, whereas palmitic acid (16C) and stearic acid (18C) are
most common fatty acids. Some properties of fatty acid are increased with an increase in number
of carbon atoms, such as melting point, solubility in organic solvent and hydrophobic nature.
Some common fatty acids are given in the table 2.6. Fatty acids are either saturated or
unsaturated. Fatty acids in which all of the internal carbon atoms possess hydrogen side groups
are said to be saturated fatty acids because they contain the maximum number of hydrogen
58 2 Biological Molecules
atoms that are possible, e.g., palmitic acid. Saturated fatty acids tend to be solid at room
temperature (higher melting point) and are more common in animal lipids (fats).
Unsaturated fatty acids have one or more pairs of carbon atoms joined by a double
bond. They therefore are not fully saturated with hydrogen, e.g., oleic acid. Unsaturated fatty
acids are liquid at room temperature (lower melting point) and are more common in plant lipids
(oils). Triglycerides containing hydrocarbon chains melt at a low temperature. This is useful for
living things.
Table: 2.6: Common types of fatty acids
No. of Melting
Name Typical source Condensed Formula
Carbon point (oC)

k
Saturated

.p
1.Lauric Coconut oil 12 44

2.Myristic Butter fat 14 58

Most fats and

3.Palmitic 16 63

rg
oils
Most fats and
4.Stearic 18 70
oils
Unsaturated .o
5.Oleic Olive oil 18 4

6.Linoleic Vegetable oils 18 -5

bf
Soybeans and
7.Linolenic 18 -11
canola oils
Lard (present in
8.Arachidonic 20 -50
chicken etc.)
.n

Waxes
Waxes are highly hydrophobic compounds. There are two types of waxes. Natural
waxes are simple lipids. They are typically esters of long chain fatty acids and long chain
w

alcohols, such as bee’s wax (found in honeycomb), lanolin (obtained from sheep wool), cutin
(on leaf surfaces of plants) and suberin (found in cell wall of endodermis of plant roots). These
w

are chemically inert and resistant to atmospheric oxidation. Waxes have protective functions in
plants and animals.
w

Synthetic waxes are generally derived from petroleum or polyethylene and consist of
mixtures of long-chain hydrocarbons (alkanes), alcohols, aldehydes, ketones and fatty acids
e.g., paraffin wax which is used to make candles, wax paper, lubricants, and sealing materials.
Phospholipids
Phospholipid is a type of compound/complex lipids. Commonly occurring phospholipids
are derived from phosphatidic acid. A phospholipid is formed when phosphatidic acid
combines with one of the four organic compounds such as choline (a nitrogenous base),
ethanolamine (an amino alcohol), inositol (an amino alcohol) and serine (an amino acid). A
phosphatidic acid molecule is most similar to diglyceride that it contains a glycerol, two fatty
 2 Biological Molecules 59
acids esterified with first and second OH groups of
glycerol and a phosphate group esterified with third
OH group of glycerol. Most common type of
phospholipid is phosphatidylcholine also called
lecithin in which choline is attached to phosphate
group of phosphatidic acid. One end of the
phospholipid molecule, containing the phosphate
group and additional compound is hydrophilic i.e.,
polar and readily soluble in water. The other end,
containing the fatty acid side chains, is hydrophobic

k
i.e., non-polar and insoluble in water. These
phospholipids are major constituents of lipid bilayer

.p
of cell membrane.
Terpenes

rg
Terpenes are the types of derived lipids. All Fig. 2.29: Phosphatidylcholine (Lecithin)
the terpenes are synthesized from a five-carbon
building block known as isoprene unit. This unit condenses in
.o
different ways to form many compounds. Two isoprene units form a
monoterpene e.g., menthol, four form a diterpene e.g., vitamin A,
phytol (chlorophyll tail) and six form a triterpene e.g., ambrein.
bf
Natural rubber is a polyterpene.
Steroids Fig. 2.30 Isoprene unit
.n

Steroids are lipids of high molecular weight which can be crystalline. A steroid consists
of 17 carbon atoms arranged in four attached rings, three of the rings contain six carbon atoms,
and the fourth contains five. The length and structure of the side chains that extend from these
w

rings distinguish one steroid from other steroids.

These structures are synthesized from isoprene units.
w

Cholesterol is a structural component of cell

membrane. Cholesterol is the precursor of a large
number of equally important steroids which include
w

the bile acids, male sex hormone testosterone,

female sex hormone progesterone and estrogen etc.
Bile salts which emulsify fats and Vitamin D, which
helps to regulate calcium metabolism are also steroid.
Fig. 2.31 Steroid nucleus

Prostaglandins
Prostaglandins exist in virtually every mammalian tissue, acting as local hormones.
Prostaglandins are derived from arachidonic acid (a tetra unsaturated 20C fatty acid). Their
functions vary widely depending on the tissue. Some reduce blood pressure, whereas others
60 2 Biological Molecules
raise it. In the immune system, various prostaglandins help to induce fever and inflammation
and also intensify the sensation of pain. They also help to regulate the aggregation of platelets
an early step in the formation of blood clots. Those synthesized in the temperature-regulating
centre of the hypothalamus cause fever. In fact, the ability of aspirin to reduce fever and
decrease pain depends on the inhibition of prostaglandin synthesis.
Science, Technology and Society Connections
 Relate the role of prostaglandin in inflammation with the inhibition of prostaglandin synthesis through
aspirin.
Prostaglandins play a pivotal role in inflammation a process characterized by redness (rubor), heat (calor),
pain (dolor), and swelling (tumor). The changes associated with inflammation are due to dilation of local blood

k
vessels that permits increased blood flow to the affected area. The blood vessels also become more permeable,
leading to the escape of white blood cells (leukocytes) from the blood into the inflamed tissues.

.p
Aspirin is anti-inflammatory, analgesic, and antipyretic. Aspirin inhibit prostaglandin synthetase salicylate.
This drug affects the metabolism of arachidonate via the lipoxygenase pathway by inhibiting the conversion of
12-hydroperoxy- to 12-hydroxy-5, 8, 10, 14-eicosatetraenoic acid.

rg
2.6 NUCLEIC ACID
Nucleic acids were first reported in 1869 by a Swiss physician when he isolated a new
.o
compound from the nuclei of pus cells (white blood cells). This compound was neither a protein
nor lipid nor a carbohydrate; therefore, it was a novel type of biological molecule. He named this
molecule as nuclein, because it was located in the nucleus. In 1920 the basic structure and
bf
chemical nature of nuclein was determined and was renamed as nucleic acid because of its
acidic nature.
.n

2.6.1 Chemical Structure of Nucleic Acids

Now it has been cleared that nucleic acids are of two types i.e., deoxyribo nucleic acid
w

(DNA) and ribo nucleic acid (RNA). Both nucleic acids are linear un-branched polymers. The
monomers of the nucleic acid are called nucleotides.
w

Composition of a nucleotide
Nucleotides of DNA are called deoxyribonucleotides and of RNA are known as
w

ribonucleotides. Each nucleotide consists of pentose sugar, a phosphate and a nitrogen

containing ring structure called base. The pentose sugar in deoxyribonucleotides is
deoxyribose and in ribonucleotides is ribose. Phosphoric acid is a common component of both
nucleotides which provides acidic properties to DNA and RNA. The nitrogen containing ring
structures are called bases because of unshared pair of electron on nitrogen atoms, which can
thus acquire a proton. There are two major classes of nitrogenous bases i.e., single ring
pyrimidine and double ring purines. Pyrimidine bases are or three types i.e., cytosine (C),
thymine (T) and uracil (U). Thymine is only found in DNA while the uracil is only found in RNA.
On the other hand, the purine bases are also of two types i.e., adenine (A) and guanine (G).
 2 Biological Molecules 61

k
.p
rg
.o
Fig. 2.32: Components of nucleotides
bf
During the formation of a
nucleotide, first nitrogenous base is linked
.n

with 1′ carbon of pentose sugar. Such

combination is called nucleoside. When
a phosphoric acid is linked with 5′ carbon
w

of pentose sugar of a nucleoside, the

nucleotide is formed. A nucleotide with
one phosphoric acid is called nucleoside
w

monophosphate with two phosphoric

acids is called nucleoside diphosphate
w

and with three phosphoric acids is called

nucleoside triphosphate.
The nucleotides which take part in
the formation of DNA or RNA must contain
three phosphates but during their
incorporation into DNA or RNA polymer
each nucleotide losses its two terminal
phosphates. Different terms used for
nucleosides and nucleotides are given in Fig. 2.33: Structure of a nucleotide
the table 2.7.
62 2 Biological Molecules
Table: 2.7: Different types of nucleosides and nucleotides of RNA and DNA
Nitrogenous RNA DNA
base
Ribonucleosides Ribonucleotides Deoxyribonucleosides Deoxyribonucleotides
(Ribose + Base) (Ribose+Base+ (Deoxyribose + Base) (Deoxyribose+Base+
Phosphate) Phosphate)
Adenine Adenosine AMP, ADP, ATP d-Adenosine dAMP, dADP, dATP
Guanine Guanosine GMP, GDP, GTP d-Guanosine dGMP, dGDP, dGTP
Cytosine Cytidine CMP, CDP, CTP d-Cytidine dCMP, dCDP, dCTP
Uracil/ Thymine Uredine UMP, UDP, UTP d-Thymidine dTMP, dTDP, dTTP

k
Polymerization of nucleotides (Formation of polynucleotide)

.p
Nucleotides are also joined together by a condensation reaction like other biomolecules.
Unlike proteins, carbohydrates, and lipids, however, the molecule that is released is not water

rg
but pyrophosphate (two phosphate groups bound together). When pyrophosphate is cleaved by the
addition of water, a great deal of free energy is released which derives the process. In this way
nucleotides begin to link by phosphodiester bonds and a polymer of nucleotides (polynucleotide) is
.o
formed. Polynucleotides have a free 5' phosphate group at one end and a free 3' hydroxyl group
at the other end. By convention, these sequences are named from 5' to 3'.
bf
.n
w
w
w

Fig. 2.34 Polymerization of nucleotides

2.6.2 Chemical Nature and Role of ATP and NAD
Adenosine triphosphate (ATP) is a mononucleotide. As shown in fig. 2.35 ATP has
three parts, connected by covalent bonds: (a) adenine, a nitrogen base, (b) ribose, a five carbon
sugar, (c) three phosphates. The two covalent bonds linking the three phosphates together are
called high-energy bonds. ATP can be converted to ADP and inorganic phosphate (iP) by
 2 Biological Molecules 63
hydrolysis. ATP is known as the energy
currency of cells. ATP is made from the
oxidation of organic molecules during
respiration. Since the energy to add the
phosphate to ADP comes from oxidation, the
process is known as oxidative
phosphorylation. Most of the ATP in the
cell is made in mitochondria.
Nicotinamide adenine dinucleotide

k
(NAD) consists of two nucleotides. One
nucleotide consists of base-nicotinamide,

.p
sugar and phosphate. Other nucleotide
Fig. 2.35 Structure of ATP
consists of base-adenine-sugar and
phosphate. The two nucleotides are joined by

rg
their phosphate group forming a dinucleotide.
NAD is a coenzyme. It works with
dehydrogenases as oxidizing agent. Its
.o
reduced form is NADH+H (NADH2).
2.6.3 Watson and Crick Model of DNA
bf
In 1951, Erwin Chargaff found that the
nitrogenous bases in a DNA show specific
ratios. He observed that amount of adenine is
.n

always equal to the amount of thymine and

amount of guanine is always equal to the
amount of cytosine in DNA. This implies that
w

the total purines and total pyrimidines are in Fig. 2.36 Structure of NAD
1:1 in any DNA. This conclusion is known as Chargaff’s rule. In those days the X-ray
diffraction analysis of DNA by Maurice Wilkins and Rosalind Franklin was published. They
w

first time claimed that DNA is a duplex (double helix) molecule. The width of duplex is 2ηm while
the length of each turn is 3.4ηm. In 1953, on the basis of these observations a graduate
w

student Francis Crick and a research fellow James Watson of Cambridge University proposed
a physical model of DNA which is now called Watson and Crick Model of DNA.
According to this model a DNA is made up of two polynucleotide chains which are
attached together by base pairs. In order to make base pairing the two polynucleotide chains
are opposite in direction i.e., one chain runs from 5′ to 3′ downward and the other chain runs
from 5′ to 3′ upward. Both chains show a constant width of 2 ηm. Therefore, both chains are
supposed be antiparallel to each other. The base pairing is very specific i.e., Adenine makes
the pair with Thymine and Guanine with Cytosine. The base pairs are held together by the
hydrogen bond. There are three hydrogen bonds between Guanine and Cytosine and two
64 2 Biological Molecules
hydrogen bonds between Adenine and Thymine. Therefore, the ratio of A: T and C: G is equal
but the ratio of AT: CG is different. Each turn of the duplex consist of 10 base pairs. Both
polynucleotide chains are complementary to each other. There is no restriction of the sequence
of nucleotides along the length of a DNA strand. The sequence can vary in countless ways. The
sequence is specific for different species, organisms and even individuals.

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(a) Key features of double helix (b) Partial chemical structure

model of DNA
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Fig. 2.37 Watson and Crick model of DNA

2.6.4 Concept of Gene

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A gene is region of DNA which is made up of nucleotides. It is the physical and functional
unit of heredity. Each gene contains the information required to build specific proteins needed
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in an organism, such as they contain the instructions for our individual characteristics – like eye
and hair colour. In order to make proteins, the gene from the DNA is copied into messenger
RNA. The mRNA moves out of the nucleus and uses ribosomes to form the polypeptide that

Science Titbits
Watson and Crick assembled the molecular model and published their two -page article on their
molecular model of DNA in the journal “Nature” in April 1953. Few milestones in the history of biology
have as broad an impact as their double helix. They were awarded Nobel Prize in 1962 for their model of
DNA.
 2 Biological Molecules 65
finally folds and configures to form the protein. Genes possess the data to build and maintain
cells and pass genetic information to offspring.
2.6.5 Ribonucleic Acid (RNA)
RNA is also a polymer of nucleotides. Its detailed chemical nature has already been
discussed in previous topics. Unlike DNA, the RNA is generally single stranded and does not
form a double helix like DNA. However, some RNA shows a secondary double stranded
structure in their complementary regions. There are three major classes of RNA each with a
special function in protein synthesis. These RNA are transcribed from DNA template.

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Messenger RNA (mRNA)
mRNA consists of a single strand of variable length. Its length depends upon the size of

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the gene, as well as the protein for which it is taking message. For example, for a protein
molecule consisting of 100 amino acids, the mRNA will have the length of 300 nucleotides.
Actually every three nucleotides in mRNA encode a specific amino acid, such triplets of

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nucleotides along the length of mRNA are called codons of genetic codes. mRNA is about 3
to 4% of the total RNA in the cell. mRNA takes the genetic message from the nucleus to the
ribosome in the cytoplasm to form particular protein. It is transcribed from DNA template i.e., the
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base of sequence of mRNA is according to the base sequence of DNA. It becomes attached to
the ribosome. At ribosome, amino acids are attached one by one to form a polypeptide chain as
per base sequence of mRNA. This process is known as translation.
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Ribosomal RNA (rRNA)
Ribosome consists of rRNA and protein. rRNA is transcribed by the genes present on the
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DNA of the several chromosomes. It is called rRNA because it eventually becomes part of
ribosome. The rRNA is packaged with a variety of proteins into ribosomal subunits. The base
sequence of rRNA is similar from bacteria to higher plants and animals. rRNA have largest size
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among the RNA. Approximately, 80% of total RNA contents of a cell are rRNA. It is a part of
ribosome where protein synthesis takes place. In other words rRNA provides a platform for
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protein synthesis.
Transfer RNA (tRNA)
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It is the smallest of the RNA molecules that it consists of 75 to 90 nucleotides. A tRNA is

a single stranded molecule but it shows a duplex appearance at its some regions where
complementary bases are bonded to one another. It shows a flat cloverleaf shape in two
dimensional views. Its 5′ end always terminates in Guanine base while the 3′ end always is the
base sequence of ACC. Amino acid is attached to tRNA at this end. The nucleotide sequence
of the rest of the molecule is variable. tRNA has three loops. The middle loop in all the tRNA is
composed of 7 bases, the middle three of which form the anticodon; it is complementary to
specific codon of mRNA. For example, a tRNA that has anticodon GAA binds to the codon CUU
and carries amino acid Leucine. The D loop recognizes the activation enzyme. Theta (θ) loop
recognizes the specific place on the ribosome for binding during protein synthesis. There is at
66 2 Biological Molecules
least one tRNA molecule for each of the 20 amino acids found in proteins. Sixty tRNA have been
identified. However, human cells contain about 45 different kinds of tRNA molecules each
transports a specific amino acid from cytoplasm to the surface of ribosome for protein synthesis.

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Fig: 2.38: Cloverleaf model of tRNA

Science, Technology and Society Connections

 Correlate the scanning tunnelling microscope as the

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latest advancement for seeing the atoms of DNA.

The Scanning tunneling microscope was invented in 1980. It
can allow scientists to view atoms on the surface of a solid. It
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is a very powerful tool that can be used to resolve features less Atoms seen on the
surface of a solid
than a nanometer. The microscope’s inventors, Gerd Binnig
and Heinrich Rohrer were awarded Nobel Prize in Physics in
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1986. Seeman's group worked on the DNA nanotechnology. Scanning tunneling

They constructed molecular building blocks of DNA. microscope

2.7 CONJUGATED MOLECUELS

Molecules when joined by other kinds of molecules are called conjugated molecules. The
examples are glyocolipids, glycoproteins, lipoproteins and nucleoproteins.
Glycolipids are complex lipids containing one or more simple sugars in connection with
long fatty acids or alcohol. The carbohydrates form the polar head to the molecule. Glycolipids
are present in white matter of brain and myelin sheath of nerve fibres and chloroplast membrane.
 2 Biological Molecules 67
Glycoproteins are formed when proteins are covalently attached to carbohydrates.
Glycoproteins are widely distributed in the cells. They function as hormones, transport proteins,
structured proteins and receptors. The blood group antigens contain glycoproteins, which also
play an important role in blood grouping.
Lipoproteins are formed by the combination
of protein with phospholipids. Phospholipid protein
Science Titbits
complexes are widely distributed in plant and animal
Why do the nucleotides in DNA have a
material. They occur in milk, blood, cell nucleus, egg hydrogen atom at the 2' carbon instead of the hydroxyl
yolk membrane and chloroplasts of plants. group in ribose? The answer is that a hydroxyl group at
the 2' position can participate in a reaction that cleaves

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Nucleoproteins consist of simple basic
the phosphodiester bond. Thus, DNA can act as a stable
protein and nucleic acid. They are found in
long-term repository for genetic information. RNA is

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chromosomes and ribosomes. usually degraded within your cells in 30 minutes.

Skills: Analyzing, Interpreting, and Communication

• Draw the Watson—Crick model of DNA

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• Illustrate the formation of phosphodiester linkage
Skills: Initiating and Planning
• Hypothesize, which came first DNA or RNA
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Science Technology and Society Connections
 List the career opportunities in the field of biochemistry.
Biochemistry, the study of chemical processes that take place in living organisms, is a broad field that offers a
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wide range of career options. Biochemists can pursue stem cell or genetic research that has the potential to
result in dramatic medical or scientific breakthroughs. Some biochemists study the body’s immune response to
germs and allergens or the effectiveness of drugs in treating a wide array of afflictions. Other biochemists work
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in the commercial food or agricultural field looking for ways to improve products and crops. The many and diverse
applications of biochemistry include pharmacology, genetics, immunology, bioinformatics, environmental
science, forensics, toxicological studies and food science. The career options are nearly endless, and still
unfolding, as new applications for this exciting field of study continue to evolve.
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Exercise
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MCQs
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1. Select the correct answer

(i) An amino acid molecule has the following structure:

Which two of the groups combine to form a peptide link between two amino acids?
(A) 1 and 2 (B) 1 and 3 (C) 2 and 3 (D) 2 and 4
68 2 Biological Molecules
(ii) Which class of molecule is the major component of cell membrane
(A) phospholipid (B) cellulose
(C) wax (D) triglyceride
(iii) Glycerol is the backbone molecule for
(A) ATP (B) terpenes
(C) neutral lipids (D) steroids
(iv) A fatty acid is unsaturated if it
(A) contains hydrogen (B) contains double bonds
(C) contains an acid group (D) all of them

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(v) In RNA the nitrogen base that takes the place of thymine is

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(A) adenine (B) cytosine
(C) guanine (D) uracil
(vi) The ending—ose means a substance is a

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(A) sugar (B) lipid
(C) protein (D) nucleic acid
(vii) Glycolipids and lipoprotein are important components of
(A) cellular membrane
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(C) both of them (D) none of them
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(viii) When two amino acids are linked to form peptide linkage .......... is removed
(A) hydroxyl (B) water
(C) carbon (D) nitrogen
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(ix) What is the theoretical number of chemically different dipeptides that may be
assembled from two different amino acids.
(A) one (B) two
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(C) three (D) four

(x) A polar molecule is ……………….. in water
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(A) soluble (B) insoluble

(C) reactive (D) innert
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(xi) Which statement correctly describes a property of water?

(A) a relatively large amount of heat is needed to increase its temperature
(B) at normal room temperature, its molecules are bound together by ionic bonds
(C) the highest density of water occurs below its freezing point
(D) water acts as solvent for nonpolar molecules
(xii) Estrogen, vitamin-D and cholesterol are all examples of
(A) glycolipids (B) lipoproteins
(C) terpenes (D) steroids