CHAPTER NO.

01
BIOLOGICAL MOLECULES

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 BIOLOGICAL MOLECULES
• Molecules that are present in living organisms are known as
biomolecules or biological molecules.
Example: Protein, carbohydrates, lipids, nucleic acids etc.

• The study of biological molecules, their processing and impotance

for living organisms is known as Biochemistry.
• Biochemistry helps to understand biological process such as
photosynthesis, cellular respiration, digestion, excretion etc.
• Biochemistry helps to understand abnormalities and diseases.
• Biochemistry helps to understand the nucleic acid (DNA & RNA),
enzymes, protein synthesis etc.
• Biochemistry helps to understand fundamental process in the field of
biological science and medical sciences such zygote, vaccine,
antibiotic etc.
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 COMPOSITION OF PROTOPLASM

• Living material of the cell is known as protoplasm.

• Protoplasm contains Cytoplasm and Nucleoplasm (Nucleus).
• All most of metabolic reactions takes place in protoplasm.

• Protoplasm of living
organism is chemically
composed elements known
as bioelements and
compound are known as
biological compounds.
• Organic compounds exists as
molecules known as
biological molecules.
• Inorganic compounds occurs in the form of minerals.
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 BIOELEMENTS
• Elements that make the bodies of living organisms are known as
bioelements.
NUMBER OF ELEMENTS
• There are 92-natural elements, out of these 92 elements, 25 are
bioelements.
• 16-bioelements are found in human beings.

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 TYPES OF BIOELEMENTS
• There are three types of bioelements
1. MAJOR BIOELEMENTS
• There are six major biolements which makes 99% of the protoplasm
are known as major bioelements.
Example: Carbon, hydrogen, oxygen, nitrogen, calcium and
phosphorous.
Six major bio-elements that constitute the 99% of human body
SNO: Symbol Major Bioelements %
1 O Oxygen 65%
2 C Carbon 18%
3 H Hydrogen 10%
4 N Nitrogen 3%
5 Ca Calcium 2%
6 P Phosphorous 1% 5
2. MINOR BIOELEMENTS:
• These bioelements are found in protoplasm less than 1% are known
as minor bioelements.
Example: Potassium (K), sodium (Na), sulphur (S), chlorine (Cl) and
magnesium (Mg).

Five minor bio-elements that constitute less than 1% of human body

SNO: SYMBOL BIOELEMENTS %
1 K Potassium 0.35%
2 S Suphur 0.25%
3 Na Sodium 0.15%
4 Cl Chlorine 0.15%
5 Mg Magnesium 0.05%

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3. TRACES OF BIOELEMENTS
• These bioelements are found less than 0.01% are known as traces of
bioelements.
Example: Iron (Fe), Copper (Cu), Manganese (Mn), Zinc (Zn) and
Iodine (I).
• Iron is required by all forms of life but other traces of bioelements
are required only by certain species of living organisms.

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 MOLECULES
• In living organisms elements do not occur in isolated forms but these
elements combine with each through ionic and covalent bonding to
form biomolecule.
• This bonding construct the great variety of molecules having
complexity.
 MOLECULES ARE CLASSIFIED INTO:

• These are commonly known as micro molecule or building block.

• Low molecular weight
• They are formed by basic elements such carbon, hydrogen, oxygen,
nitrogen etc.
Example: Glucose, H2O, Amino Acid, Fatty Acid, Nucleotide etc.

• These are commonly known as macro-molecule.

• High molecular weight
• They are formed by the combination of large number of monomers
molecules.
Example: Polysaccharides (starch), Protein, Lipid, Nucleic Acid (DNA &
RNA).
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 FUNDAMENTAL TYPES OF BIOMOLECULES
• Bio-molecules are dividend into following groups on the basis of
variability in their structure and functions in cells and organisms
MOLECULES UNITS LINKAGES
Carbohydrates •Monosaccharides • Glycoside linkage
Proteins •Amino acids • Peptide linkage

Lipids
• Fats & Oils, •Glycerol, Fatty acids. • Ester linkage
Phospholipids • Glycerol, Fatty acids, Phosphate & Choline • Ester & C-C linkage
•Isoprenoids unit • C-C linkage
• Terpenoids

Nucleic acids • Phosphoester

• DNA •Deoxyribonucleotide linkage
• RNA •Ribonucleotide

Conjugated •Different biomolecules • Different linkage

molecules 10
 CHEMICAL COMPOSITION OF CELLS (in %)
S NO: MOLECULE BACTERIAL MAMMALIAN
CELL CELL
1 Water 70 % 70%
2 Proteins 15% 18%
3 Carbohydrates 3% 4%
4 Lipids 2% 3%
5 DNA 1% 0.25%
6 RNA 6% 1.1%
7 Other Organic Compounds 2% 2%
(Enzymes, Hormones etc).
8 Inorganic Ions (Na+ ,K+, Ca++, 1% 1%
Mg++, Cl-, SO4-.
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A. Synthesis of macromolecules (polymers) by condensation
• The process in which Monomer (subunits) combine to form macro-
molecules by the removal of water is known as condensation.

Mechanism:
• Hydroxyl group of one molecule combines with hydrogen atom of other
molecules. As a result water is removed and bond is formed.
• Condensation is known as dehydration synthesis because water is
removed (dehydration) and bond is formed (synthesis).
• Condensation involves use of enzymes in the cell.

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B. Breakdown of macromolecules (polymers) by Hydrolysis
• The process in which break down of the polymers (macromolecule) into
its monomers (sub-units) by the addition of H2O molecule is known as
hydrolysis.
• It is the reverse process of condensation.

Mechanism:
• Hydroxyl group of water is attached to one molecule (monomer) and
hydrogen atom is attached to other monomers
• Hydrolysis involves use of enzymes in the cell.

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 IMPORTANCE OF WATER
• Water is most abundant part of cytoplasm, life can not exist without
water.
• Bodies of living organisms contain about 70% to 90% water.
• Bone contains 20%, brain 85% and blood 88% and jelly fish contains
99% of water.
• All reactions occur in the living organisms due to presence of water.
Example: Photosynthesis, Dark Reaction, Light Reaction, Cellular
Respiration, Digestion etc.
• Water is raw material in photosynthesis.
• Water is universal solvent.

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 HIGH POLARITY OF WATER
• Water is a polar molecule because its hydrogen contains partially
positive charged where as oxygen contains partially negative
charged due to difference in electronegativities of hydrogen and
oxygen atoms.
• Polar covalent bond is formed between hydrogen and oxygen atoms
of water.
• This separation of electrical charges
are known as Dipole.
• Due to polar covalent bond, water is
known as polar molecule and thus
water is the universal solvent for the
polar substance, ionic compounds or
electrolytes.
• Non-polar molecules having charged
groups on their molecules can also
dissolved in water like sugar.
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 HYDROGEN BONDING
• Hydrogen bonding is the type of intermolecular force.
• Force of attraction between highly electronegative atom (partially -
ve) of one molecule and partially +ve hydrogen atom of an other
molecule is called as hydrogen bond.
• Hydrogen bond is represented by dotted lines.
• Hydrogen bond is easily break down by increasing temperature and
by larger change in PH.

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 HYDROGEN BONDING

• Water is polar substances

• Partially negative oxygen atom of one water molecule attracts partially
positive hydrogen atom of an other water molecule.

• Hydrogen bonding makes water a good solvent.

• It gives the water properties of cohesion and adhesion.
• Due to the hydrogen bonding, water has specific boiling and freezing
points (boils at 100°C and freezes at 0°C).

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 COHESION OR AND ADHESION
• Force of attraction between water molecules (similar molecules) is
known as Cohesion while force of attraction between water molecules
with polar surface (dissimilar molecules) is known as Adhesion.
• Cohesion and adhesion properties of water are due to hydrogen
bonding.
• Due to polar nature, water molecules attracts with each other and form
hydrogen bonds between them to form long chain of water molecules
which in it flowing freely.

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 COHESION OR AND ADHESION
• It flows as protoplasm in cell, as blood in blood vessels.
• It flows as transporting fluid in conducting tissues of plants.

• Cohesion and adhesion makes water a good transport medium.

• Water circulates in bodies of living organisms and acts as transport
medium.

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 HIGH SPECIFIC HEAT
• Specific heat capacity of water is required the number of calories to raise
temperature of 1g water by 1°C (15°C to 16°C).
• It is the 1-calorie or 4.18 joules.

• Water has heat capacity due to

hydrogen bond.
• Much heat absorbed by the
water molecules which is
utilized to break down of
hydrogen bond.
• Very large amount of heat can increase very little temperature of water.

• Due high specific heat of water, hot water cools slowly while cool water
hot slowly.
• As a result the temperature of earth and living bodies does not change
quickly and environment remains constant. 20
 HIGH HEAT OF VAPOURIZATION

• Amount of heat energy required to convert unit mass of the liquid

into gases form (vapours) is known as vaporization.

• Number of calories required to convert 1g of water into vapors.

• Water has high heat of vaporization due to hydrogen bonding.
• It is the 574 k calories/gram.

• High heat of vapourization means that a lot of heat can be lost with
minimum loss of water.
• Loss of only 2-ml water out of liters (1000ml) lowers the temperature
of remaining 998 ml water by 1 °C.
• When an organism sweats, body heat is used to vapourize sweat thus
cooling the animals.
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 HYDROPHOBIC EXCLUSION

• Reduction content area between water and hydrophobic substances

which are placed in water is called as Hydrophobic exclusion.

• When few drops of oil are placed on the water surface they tend to
unit (coalesce) to make single drop.

• Hydrophobic exclusion helps in maintaining integrity lipid bilayer of

cell membrane.

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 IONIZATION
• Dissociation (separation) of a molecule into ions is called as ionization.
• It is reversible process.

• Water molecules ionize into equal number of hydrogen ions (H+ ) and
hydroxyl ions (-OH).

• Ionization of water molecules is maintained at equilibrium at 25 °C.

• H+ and -OH ions affect and take part in many reactions that occurs in
cells.
It helps to maintain or change Ph. of water.

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 LOWER DENSITY OF ICE
• Ice is less dense than water therefore it floats on surface of water.

• Ice has giant lattice (web) structure.

It shows the maximum number of hydrogen bonds per water molecule.
• Lattice has large intermolecular spaces i.e; it has loose packing of
molecules therefore ice has less density.

• In freezing weather, ice

forms on the surface of
ponds, sea and lakes.
• Layers of ice provides
insulating layers above and
below water, that makes
the life possible under
frozen water. 24
 CARBOHYDRATES
(Carbo = Carbon + Hydrates = Water)
• Carbohydrates are organic compound, composed of carbon, hydrogen
and oxygen as bio-element where oxygen and hydrogen are present in
simple ration (share) of 2:1 as present in water.
• In Greek ‘Sakcharon’ is used for sugar therefore carbohydrates are
also known as saccharides.
• General formula of carbohydrates is CnH2nOn, where “n” is variable
numbers or whole number.
• They are commonly known as
hydrated carbon ie; water
containing carbon.
• Carbohydrates are simply refers to
as “Staff of life”.
• Main source of carbohydrates are
green living things (plants, algae
and many bacteria). 25
 CARBOHYDRATES
(Carbo = Carbon + Hydrates = Water)
• Chemically (according to IUPAC), they are polyhydroxyl carbonyl
(polyhydroxyl aldehyde or polyhydroxyl ketone)
• Their chemistry is determined by aldehyde or ketone group e.g;
aldehyde are very easily oxidized thus they are powerful reducing
agents.

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 Monosaccharaide Oligosaccharide Polysaccharide
• They consist of • They consist of 2- • They consist of
single saccharide 10 saccharide more than 10
unit. units. saccharide units.
• They are simple • They have less • They have highly
sugar and cannot complex structure complex structure
further change into so they can so they can further
simple sugar. further change change into at least
into 2-10 11Monosaccharaid
Monosaccharaides es
• They are easily • They are less • They are less
soluble in water. soluble in water. insoluble in water.
• They are sweetest • They are less • They are tasteless.
among all sweat in taste.
carbohydrates. 27
 MONOSACCHARAIDES (Gr: Mono = One + Sakcharon = Sugar)
• Monosaccharaides are true carbohydrates which are either polyhydroxy
aldehyde or polyhydroxy ketone .
• They are simple sugar and cannot further change into simple sugar.
• White solid crystals, easily soluble in water and sweat in taste.
• They are found in fruits, vegetables, milk etc.
• All carbons atoms except one carbon have one hydroxyl group.
• The carbon lacking hydroxyl group is the part of aldehyde or ketone
group.
• Their general formula is (CnH2nOn), where “n” is the number of carbon
atoms in monosaccharide.
• The range of carbon atoms in monosaccharaide is 2 to 7.

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• There are two types of monosaccharide on the basis of functional
groups:
1. Aldoses or Aldo-sugar
• They contain Aldehyde
Group in their structure.
Example: Glucose and
Galactose which have same
molecular formula but
different structural formula
(isomers).
2. Ketoses or keto-sugar
• They contain ketonic group
in their structure.
Example: Fructose,
sorbose, psicose (isomers).
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• Monosaccharaides are classified into 5-groups on the basis of carbon
atoms.
• Suffix “Ose” use with number of carbon atoms present in
Monosaccharaides as given bellow:
1. Trioses:
• They contain 3-carbon atoms. Example: Glyceraldehyde (Glycerose),
dihydroxy-acetone etc.
2. Tetroses:
• They contain 4-carbon atoms. Example: Erythrose.
3. Pentoses:
• They contain 5-carbon atoms Example: Ribose
4. Hexoses:
• They contain 06-carbon atoms. Example: Glucose.
5. Heptoses:
• They contain 07-carbon atoms. Example: Glucoheptose 30
 Example and functions of Monosaccharaides
Class Formula Aldoses Ketoses Function
Triose C3H6O3 Glyceraldehyde Dihydroxy- It is intermediate in
(3-C) acetone photosynthesis and cellular
respiration.
Tetrose C4H8O4 Erythrose Erythrulose It is intermediate in
(4-C) bacterial photosynthesis

Pentose C5H10O5 Ribose, Ribulose Ribose and deoxyribose are

(5-C) deoxyribose component of DNA and
(C5H10O5) RNA.
Ribulose is intermediate in
photosynthesis.

Hexose C6H12O6 Glucose, Fructose Glucose is respiratory fuel

(06-C) galactose molecule.
Glactose is present in milk.
Fructose is an intermediate
in respiration.
Heptose C7H14O7 Glucoheptose Sedoheptulose It is intermediate in
(07-C) photosynthesis
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• Two types of structure observed in monosaccharaides:
1. Open chain structure in crystalline form
2. Closed chain or ring structure in aqueous solution
• Ring structure are mostly formed by pentose and hexose.

• Ends of carbon chain are free.

• Monosaccharaides are
usually found in open chain
structure in crystalline form.
• When open chain structure in
the form of crystalline
dissolved in water, most of
them (pentose and hexose)
are converted into ring
structure.
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• Ends of carbon chain are connected to each other.
TWO TYPES OF RING STRUCTURE
a) FURANOSE
• It is five membered ring structure (1 O + 4 C).
• Oxygen atom is linked with C1 and C4.
Example: In ribose, oxygen atom aldehyde reacts with C4.
• As results OH group is transferred C4 to C1 and oxygen links to C4.
• All pentoses and keto-hexoses are converted into Furanose ring.

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b) PYRANOSE
• It is the 6-membered ring (1 O + 5C).
• Oxygen is linked with C1 and C5.
• Only aldohexose (glucose) is converted into Pyranose ring.

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 α and β forms of Pentose and Hexose
• Each pentose and hexose molecule in ring structure exist either in α
or β form, depending on position of H and OH-group on C1.
• α forms: If OH group is found downward on C1, it is called as α-sugar
• β forms: If OH group is found upward on C1, it is called as β-sugar

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 STEREOISOMERISM IN MONOSACCHARIDE
• Molecules of monosaccharide that have same molecular formula but
different structural formula (arrangement of atom in 3D space or
three-dimensional space) is known as Stereoisomer and phenomena
is known as Stereoisomerism.
• Many sugar molecules are mirror image with each other.
• Aldo-hexose isomers are glucose, galactose, mannose etc.
• Keto-hexose isomers are fructose, sorbose, psicose etc.

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 ENANTIOMERS
• Those stereoisomers which are non-super-imposable mirror image of
one an other are known as enantiomers.
Example: D-glucose and L-glucose are enantiomers of each other.
• D-glucose is also known as right handed form.
• L-glucose is also known as left handed form.

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 ARTIFICIAL SWEETENERS (Sweetening Agents)
• Laboratory manufactured sugar are commonly known as Left
Handed which are used as sweeteners.
• L-sugars are digested in our body because enzymes in body have
active sites designed by L-sugars.
• Artificial sweeteners are used as alternate for natural sugar because
they contain low calories.
• Artificial sweeteners are many times sweeter than natural sugar
which can not be harmful to humans when taken in extra quantity.
Example: Saccharin
Naturally occurring sugar are Right handed.
• Natural sweeteners give sweetness but they also contain calories
which can be harmful to humans when taken in extra quantity.
Example: Sucrose and fructose.

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 OLIGOSACCHARIDES (Gr: Oligo = Few + Sakcharon = Sugar)
• Carbohydrates which yields 02-10 monosaccharide units upon the
hydrolysis are known as Oligosaccharides
Classification
• On the basis of number of monosaccharide units, Oligosaccharides
are classified as:
1. Disaccharides
2. Trisaccharides
3. Tetrasaccharides
and so on -------

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 DISACCHARIDES (Gr: Di = two + Sakcharon = Sugar)
• Oligosaccharide which yields 02-Monosaccharide units upon the
hydrolysis are known as disaccharides.
• Disaccharide is most common and important carbohydrate.
• These may be reducing or non-reducing sugar.
• They are crystal in form.
• They are less soluble in water.
• They are less sweet in taste.
• Their general formula C12H22O11.
EXAMPLE: Maltose, Sucrose, Lactose.

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• It is commonly known as malt sugar.
• It is intermediate produced in breakdown of polysaccharides (starch
and glycogen).
• Maltose is generally found in germinating seeds.
• It is formed by the condensation of two α glucose molecules.
• -OH group at C1 of one glucose reacts with -OH group at C4 of other
glucose to form maltose molecules by α 1,4-glycosydic linkage.

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• It is commonly known as sugar cane.
• It is widely used as sweetener at home for making sweet dishes.
• In plants, it is also called transport disaccharides because food is
transported in the form sucrose because:
 Sucrose is very soluble in water, Relatively unreactive chemically and It can
be transported in high concentration.
• It is formed by the condensation of two α-glucose and β-fructose.
• -OH group at C1 of glucose linked with -OH group at C2 of fructose to form
sucrose by the removal of water.
• Bond formed is called as α 1,2-glycosydic linkage.

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• It is commonly known as milk sugar.
• It is formed by β-galactose and β-glucose.
• -OH group at C1 of galactose linked with -OH group at C4 of glucose to
form Lactose by the removal of water.
• Bond formed is called as β-1,4-glycosydic linkage.

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 POLYSACCHARIDES (Gr: Poly = Many + Sakcharon = Sugar)
• Carbohydrates that can produce more than 10 monosaccharaides on
hydrolysis are called Polysaccharides.
• It is the largest group of carbohydrates.
• These can be break down into monosaccharaides or disaccharides.

GENERAL FUNCTIONS POLYSACCHARIDE

• Polysaccharides function as food reservoir (starch, glycogen).
• They are suitable storage molecules because:
 They are almost insoluble in water due to their large size.
 They exert no osmotic and chemical influence of the cell.
 They food compact (solid) shapes.
 They are easily converted into simple sugar by hydrolysis.
 They paly a structural role (cellulose, chitin).
Common Example: starch, cellulose, chitin and glycogen etc. 44
 TYPES OF POLYSACCHARIDES
• There are fundamentally two types of polysaccharides:
1.Homopolysaccharides (homoglycans):
• These are only made up of one kind of monosaccharide units.
Example: starch, glycogen, cellulose, chitin etc.
2.Hetropolysaccharides (heteroglycans):
• These are made up of two or more different kinds of monosaccharide
units. Example: Agar, pectin, peptidoglycan.

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 STARCH
• It is the homopolysaccharides made up of hundreds of α-glucose.
• Plants store the food as starch in stem, roots and seeds.
• Cereals grains and potatoes tubers are big source of starch.
• In oral cavity, Amylase digests the starch into maltose.
• In small intestine, Maltase digests the maltose into glucose.

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 CONFIRMATORY TEST OF STARCH
• Present of the starch is confirmed by iodine test.
• Starch gives the blue colour when treated with iodine.
• Blue colour confirmed the presence of starch.

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• There are two types of the starch: Amylose and Amylopectin:
1. AMYLOSE
• It is unbranded (linear).
• Alpha-glucose units are linked with one another by α-1,4 glycosidic
linkage.
• It is soluble in hot water.

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2. AMYLOPECTIN:
• It is the branched structure.
• Alpha-glucose units are linked with one another by α-1,6 glycosidic
linkage.
• It is completely insoluble in water.
• Main chain linkage is α-1,4 glycosidic linkage but branched linkage is
α-1,6 glycosidic linkage.

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 GLYCOGEN
• It is homopolysaccharides.
• It is the polymer of α-glucose.
• It is storage carbohydrates in muscles and liver of animals, bacteria,
fungi therefore it is commonly known as Animal Starch.
• It is insoluble in water due to complex structure in nature.
• It is converted back to glucose (monomers) when needed.
• Digestion of glycogen is also quite similar to that starch.

CONFIRMATORY TEST OF GLYCOGEN

• Present of the glycogen is confirmed by iodine test.
• Glycogen gives the red colour when treated with iodine.
• Red colour confirmed the presence of glycogen.

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 STRUCTURE OF GLYCOGEN
• Structure of glycogen is resembled with amylopectin starch but
glycogen has much more branches than amylopectin.
• Glucose units are linked with one another by α-1,6 glycosidic linkage.
• Main chain linkage is α-1,4 glycosidic linkage but branched linkage is
α-1,6 glycosidic linkage.

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 CELLULOSE
• Cellulose is most abundant carbohydrates on the earth.
• It is the homopolysaccharide but unlike starch and glycogen.
• It is formed by condensation of hundreds of β-glucose.
• Cotton and papers are pure form of cellulose.
• Cellulose is digested by the bacteria which are already present in
alimentary canal of animals.
• Parallel cellulose molecules joined together through hydrogen bond.
• It is structural carbohydrates of plants as it is major constituent of
plant cell wall.

CONFIRMATORY TEST OF CELLULOSE

• Cellulose shows no colour with iodine solution.
• Present of the cellulose is confirmed by iodine test.
• Cellulose shows no colour when treated with iodine.
• No colour confirmed the presence of glycogen.
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 STRUCTURE OF CELLULOSE
• Structure of cellulose resembles with amylose starch in such a way
that it has un-branched structure.
• It is straight chain and no branched chain in cellulose is indicated.
• β-Glucose units are linked by β-1,4 glycosidic linkage.
• In cellulose chain, the β-glucose are alternatively arranged in upright
and inverted manner.

53
 CHITIN
• Chitin is second most abundant organic compound on the earth.
• It is homopolysaccharides.
• It is structural carbohydrates found in the cell wall of fungi as well as
found in exoskeleton of arthropods.
• It is commonly known as fungal cellulose because due to presence of
chitin in fungal cell wall.

54
 STRUCTURE OF CHITIN
• Chitin is the derivative (copied) of N-acetyl glucosamine which is a
modified form of glucose.
• It has an un-branched structure like cellulose.
• It is the polymer of N-acetyl glucosamine (monomers).
• N-acetyl glucosamine units are linked by β-1,4 glycosidic linkage.
• In chitin chain, N-acetyl glucosamine are alternatively arranged in
upright and inverted manner.

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 PROTEIN (GR: PROTEOS = FIRST RANK)
• Proteins are main structural component of cell.
• Chemically proteins are polymers of amino acids or polypeptide
chains.
• Proteins may consists of single polypeptide or more than one
polypeptide.
• Due to the presence of N in large proportion, they are commonly
known as nitrogenous compounds.
CHEMICAL COMPOSITION OF PROTEIN
• Proteins are composed of C, H, O, N and
sometimes phosphorous and sulphur.
• Few proteins have Iron (Fe), Magnesium
(Mg), and Iodine (I).
• Proteins are present in nails, hairs, skin,
feathers, egg, milk, meat, fishes and
pulses (Dal), pulses are major source of
protein. 56
 AMINO ACIDS
• Amino acids are building block of proteins.
• There are 20 common amino acids found in proteins which are involved
during protein synthesis in living organisms from virus to human.
• Proteins are macromolecule (polymers) of amino acids.
• Amino acids are monomers linked together by covalent bond is known
as Peptide bond or Peptide Linkage.
• Amino acids consist of central carbon atom called as alpha carbon.
• Alpha carbon attached to 4-different groups:
1. Hydrogen Atom (H)
2. Amino Group (NH2),
3. Carboxyl Group (COOH),
4. Variable group is known
as-R group.
• R--- is variable and shows
great variety of structure
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of amino acid.
 EXAMPLE OF SIMPLEST AMINO ACIDS
1. Glycine:
• When R is hydrogen (H) in amino acid is known as Glycine.
• Glycine is simplest amino acid.
2. Alanine:
• When R is methyl (CH3) in amino acid is known as Alanine.
3. Serine:
• When R is methylene hydroxyl (CH2-OH) in amino acid is known as
Serine.

58
 DIPEPTIDE & POLYPEPTIDE
a) INTRODUCTION
• Dipeptide & Polypeptide formed by condensation of amino acids on the
ribosomes under the instruction of mRNA which take these instruct
from the DNA, that process is known as translation.
PEPTIDE BOND FORMATION
• -OH from carboxylic group of one amino acid is attached with amino
group of other amino acid by the removal of water (condensation).
• As result bond is formed between “C” of carboxylic group and “N” of
amino group that bond is known as peptide bond.
• A product between two amino acids is formed is known as dipeptide.

59
 DIPEPTIDE:
• Dipeptide has two ends; one end is amino or N-terminal end and other end
is carboxylic or C-terminal end.

• DIPEPTIDE:
• A new amino acid can be added in this chain (dipeptide) from its carboxylic
acid or C-terminal end in same way:
TRIPEPTIDE:
• Tripeptide is the product of three amino acids.
POLYPEPTIDE:
• When several amino acids linked to other by many peptide bonds as results
polypeptide chain is formed.
• Protein may consist of a single polypeptide or more than one polypeptide.
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 SIGNIFICANCE OF AMINO ACIDS
1. SEQUENCE OF AMINO ACID
• F. Sanger was first scientist who determined the sequence of amino acids
in protein molecule.
• F. Sanger found that insulin is composed of 51-amino acids in two chain.
• One chain labelled “A” with 21-amino acids other chain labelled “B” with
30-amino acids which are held together through the disulphide bond.
• Sequence of amino acid in a polypeptide is a characteristic feature of
primary structure of protein.

61
 SIGNIFICANCE OF AMINO ACIDS
1. SEQUENCE OF AMINO ACID
• It is responsible for proper functioning of protein (protein synthesis).
• Sequence of amino acid is determined by the sequence of nucleotide
in DNA (genes).
• Human body has more than 10000 protein molecules.
• All protein molecules in human are unique and specific arrangement
of 20-amino acids.

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2. CHANGE IN SEQUENCE OF AMINO ACIDS
• Sequence of amino acids in particular protein (polypeptide) may be
distributed or replaced due to point mutation,
• It causes simple defects in the body, that defect is known as sickle
cell anemia.
• Sickle cell anemia is a hereditary disease.
More information
Change of single or
few nucleotide in DNA
is known as point
mutation.

63
 a) NORMAL RBCs
• Normal red blood cells are disc-shaped and look like doughnuts
without holes in the center.
• They move easily through blood vessels.
• Red blood cells contain an iron-rich protein known as haemoglobin.
• Haemoglobin carries oxygen from the lungs to the rest of the body.
• Normal haemoglobin (HbA) contains four polypeptides i-e;
 α-Two chains which consists of 141-amono acids each.
 β-Two chains which consists of 146 amino acids each.

64
 b) SICKLE SHAPED RBCs
• Sickle shaped RBCs formed in Sickle cell anemia.
• Sickle cell anemia is serious disorder in which body makes the sickle or
crescent shaped red blood cells.
• Sickle cells contains abnormal hemoglobin (Hbs).
• Sickle haemoglobin (Hbs) makes cell sickle shaped or crescent shaped.
• Sickle cells are stiff (rigid) and sticky.
• Abnormality in hemoglobin, due to change in one amino acids out of 574
amino acids.
• They tend to block blood flow in the blood vessels of limbs and organs.
• Blocked blood flow can cause pain and damage.

65
 c) CAUSES OF SICKLE CELL ANEMIA
• Sickle cell anemia is caused by the point mutation in β-gene.
• In this way only nucleotide is replaced by another place.
• It causes change in sequence of amino acids of β-chain of hemoglobin.
• Glutamic acid (glutamate) is replaced by the valine at the position
number six in β-chain.
• Due to little change of hemoglobin fails to carry the sufficient amount
of oxygen and which leads to death of person.

66
 CLASSIFICATION OF PROTEIN
• Based upon the structure and shape of protein which can be classified
into two groups: Fibrous protein and Globular protein.
Factors Fibrous protein Globular protein
Shape These protein have long fiber These protein have spherical or
or filaments in shape. ellipsoidal in shape.
Structure They exist in secondary They exist either tertiary or
structure (spiral) during quaternary structure during
function. function.
Solubility Insoluble in salt, acid or base. soluble in salt, acid or base.
aqueous medium or alcohol. aqueous medium or alcohol.
Elasticity These are elastic in nature. These are not elastic in nature.
Crystallization Non-Crystallized. Crystallized.
Example Silk, spider web, Collagen, Enzymes, hormone, antibodies,
fibers and clothing, actin and hemoglobin.
myosin in muscles and
keratin of nails and hairs.
67
 LIST OF STRUCTURAL PROTEINS
TYPES ROLE OF STRUCTURAL PROTEIN
Actin • This protein forms the body Muscles.
Amyloid • It works as cell surface proteins.
Caddisfly • It used to bind debris like rocks, sticks, twigs and shells for net of
(fibroin) prey.
Collagen • It gives strength, turned elasticity to skin main component of
cartilages, ligaments, tendon, bone and teeth.
Elastin • It provides resilience (elasticity) to tissues and organs.
Condrocalein • This protein forms extra cellular matrix.
Fibrillin • Glycoprotein provide force bearing structural support in elastic
and non-elastic connective tissues.
Gelatin • Nutritious proteins derived from collagen of skin and bones.
Keratin • This protein forms hairs, nails, quills (feathers), horns, beaks etc.
Titin • It provides elastin stabilization of myosin and actin filaments.
Tubulin • This protein forms the microtubules.
Sclera protein • It includes keratin, collage, elastin and fibrin. 68
 LIST OF THE FUNCTIONAL PROTEINS
TYPES EXAMPLE ROLE OF PROTEIN
Digestive Amylase, • These help in digestion of food into monomers by
Enzymes lipase, pepsin, hydrolysis i.e; they speed of biochemical process.
trypsin
Hormones Insulin, • These help in coordination of different body
thyroxin functions and regulation of physiological activities
such as regulation of glucose, calcium level,
digestion, blood pressure etc.
Defense Immunoglobin, • This protein protects the body from pathogens.
interferon
Transport Hemoglobin, • It is found in RBCs or lymph and involved for
Albumin transport the O2 mainly and CO2 throughout the
body.
Storage Legume storage • Ovalbumin is found in egg whites.
protein, • Both proteins provide nourishment at the time of
Ovalbumin, development.
casein • Casein is found in milk-base protein and both are
involved for storage of amino acids.
69
 LIPIDS
• The term lipid was proposed by Walter Ray Bloor in 1943.
• It is defined as heterogeneous group of organic compounds which
are insoluble in water but soluble in organic solvents or Bloor
reagents such as Acetone, alcohol, ether, benzene, chloroform etc.
• These are generally present in plants and animals.

• Lipids are composed of C, H, O like carbohydrates.

• They have relatively less ratio of Oxygen in proportion to carbon,
hydrogen than do carbohydrates.

• Tristearin is a simple lipid which shows molecular formula as

C57H110O6.
• Due to extra high quantity of hydrogen and carbon, they contain
almost double amount of energy than carbohydrates.
70
 GENERAL FUNCTIONS OF LIPIDS
• In general, lipids are components of the cell membrane
(phospholipids and cholesterol).
• They acts as energy stores (triglycerides).
• Many hormones are lipids in nature (steroids hormone).
• Lipids are involved in the protection, waterproofing, insulation and
buoyancy (resistance).

COMMON TYPES OF LIPIDS

1. Acylglycerol (fats and oil)
2. Phospholipids
3. Waxes
4. Terpenoids (Terpenes, Steroids, Carotenoid and Prostaglandin).

71
 Acylglycerol (fats and oil)
• Most abundant lipids in living organisms are Acylglycerols.
• Chemically acylglycerol can be defined as esters of the glycerol and fatty
acids.
• Approximately person contains 16-kg fats which is equal to 144000 KCal (144
x 103) Kcal of energy.
• These are present in animals as well as plants.

• An ester is the compound produced as the results of a chemical reaction of

an alcohol with acids and water molecule is released such reaction is known
as Esterification.

72
 GLYCEROL
• It is the trihydroxyl alcohol which consists of a 3-carbon chain with 3-
hydroxyl groups (OH) attached to each of them.
FATTY ACID
• Fatty acid is the type of organic acid containing carboxylic acid group
attached to a hydrocarbon.
• Fatty acids contain even number of carbons from 2-30.
• Each fatty acid is represented as R-COOH where -R is a hydrocarbon
tail.

73
 TYPES OF THE ACYLGLYCEROL
1. Monoacylglycerol
• It consists of 01-glycerol linked with 1-fatty acids to form
monoacylglycerol.
• It is also called as monoglyceride.

74
2. Diacylglycerol
• It consists of 01-glycerol linked with 2-fatty acids to form
diacylglycerol.
• It is also called as diglyceride.

75
3. Triacylglycerol
• It consists of 01-glycerol linked with 3-fatty acids to form
triacylglycerol.
• It is also called as triglyceride.
• Triacylglycerols are also neutral fats as all three OH-groups of
glycerol are occupied by fatty acids and no charge bearing OH group
is left.

76
• They contain saturated fatty acids in which fatty acids do not contain
double or triple bond between carbon atoms of hydrocarbons atoms.
• They are solid at the room temperature (higher melting point).
• They are more common in animals fats.
Stearin (C57H110O6) found in beef and mutton, cream,
butter, cheese, ice cream etc.

77
• They contain unsaturated fatty acids in which Unsaturated fatty acids
have one or more pairs of carbon joined together by double bond
therefore they are not fully saturated with hydrogen.
• They are liquid at room temperature (lower melting point).
• They are more common in plants liquid (oil).
Example: Linolin (C57H104O6) found in seeds.

78
 PHOSPHOLIPID
• It contains a glycerol, two-fatty acids esterified with 1st and 2nd OH-
group of glycerol and phosphate is esterified with 3rd OH-group of
glycerol.
• Therefore Glycerol is the back bone of phospholipid.
• Phospholipid is most abundant group of lipids according to biological
point of view.

79
 PHOSPHOLIPID
• Phospholipids are similar to acyglycerol except one fatty acid is replaced by
phosphate group which is attached with nitrogen compound choline.
• It consists of two ends, one end is made up of fatty acids which form the non-
polar part therefore fearing, hating and repellant the water known as
hydrophobic (tail).
• An other end is made up of choline and phosphate which form the polar part
therefore loving and attract the water known as hydrophilic(head).

80
 PHOSPHOLIPID
• Phospholipids are present in all living cells form the biological
membrane.
• Phospholipids are associated with cell membrane, help to regulate
permeability of cell and transportation in cell.
• Cell membrane is phospholipid bilayer therefore components of cell
membrane depend on phospholipids.

81
 WAXES
• Waxes are highly hydrophobic compound in nature.
TYPES OF WAXES
1.NATURAL WAXES:
• These are simple lipids in which ester of long chain of fatty acids linked with
long chain of mono-alcohol.
• These are chemical insert and resist to atmospheric oxidation.
• These waxes have the protective functions in plants (stem, stalks, leaves, petals,
fruits skin) as well as animals (skin feathers, fur).
• These are the water repellant and non-reactive due to its hydrophobic nature.
Example: Bee’s wax (found in honey comb) and Cutin (on leaf surface of plants.
2.SYNTHETIC WAXES:
• These waxes are generally derived from petroleum or polyethylene e.g: Paraffin.
• Synthetic waxes are used to make the candles.
• Waxes are used as machine lubricant or engine oil.
• A long time ago sperms of whale were principle source of waxes.
82
 TERPENOID
• These are large and important lipids which consists of isoprenoid ring
(C5H8).
• Terpenes, steroid, carotenoids and prostaglandin are the types of
Terpenoid.
• These are found in the cell membrane as cholesterol, as pigment like
chlorophyll, fragrance like menthol.

83
 i. Terpenes
• All terpenes are synthesized from five carbon building block known as
isoprenoid units (C5H8).
• Building block of terpene is isoprene units.
• These small size terpenes are volatile in nature and produce special
fragrance.
• Two isoprene unit condenses to form monoterpene (C10H16).
Example: Menthol
• Four units of isoprene form a
diterpene.
Example: Vitamin-A, phytol
(chlorophyll tail).
• Six isoprene units form a
triterpene.
Example: Ambrein
• Many isoprene units form
polyterpene.
Example: Natural rubber 84
 ii. Steroids
• Steroids are lipids of high molecular weight, which can be crystalline.
• These structures (steroids) synthesized from isoprenoids units contains
four carbon ring structure; three carbon rings contain six carbons
(hexagonal) and fourth contains five carbon (pentagonal) along with 17-
carbon atoms.
• Cholesterol act as precursor of steroids such as bile acids, sex hormones
such as testosterone (male hormone), estrogen and progesterone
(female hormones).
 iii. Carotenoid
• It is polyterpenes which contains long chain of fatty acids having
double bond and contains six carbon rings at each ends.
• Carotenoids are plant pigments that are widely found in fruits and
vegetables.
• These compounds are pigments producing colours such as red,
orange, yellow, cream and brown colours etc.
• Some carotenoids are plants pigments such as chlorophyll,
cytochrome, phytochromes, latex, rubber etc.
• 600 known carotenoids (colours).
• Beta carotenes are reddish-orange carotenes commonly found in
mangoes, pumpkin, oranges, papayas, carrots and sweet potatoes.

Β-Carotene
86
 iv.Prostaglandins
• The name prostaglandin is derived from prostate gland in human semen.
• They were discovered by the Swedish physiologist Ulf von Euler in 1935.
• They are the group of physiological active lipid compounds made by
mammalian tissues at the site of damage or infection.
• Prostaglandins have been found almost in every tissues of human and
animals that are involved in dealing with injury and illness.
• They are derived from enzymatically from fatty acids.
• Every Prostaglandin contains 20-carbon atoms including a 5-carbon
rings.
• The Prostaglandin maintains the physiological function such as
inflammation, hormones, sensitize spinal neuron for pain, blood flow,
control cell growth, regulate fever and formation of blood clot etc.
• We use aspirin drug to reduce the fever and decreases pain.
• In 1971, aspirin drug could inhabit the synthesis of Prostaglandin.
87
 NUCLEIC ACIDS
• Nucleic acids were isolated by Swiss physician Friedrich Miescher in
1869 from nuclei of pus cell (white blood cells).
• He named this molecule as Nuclein because it was located in
nucleus.
• The Basic structure and
chemical nature of nuclein
was determined by jones in
1920.
• Finally nuclein has acidic
properties was determined
therefore named as Nucleic
Acid.
• This compound was neither
protein nor carbohydrates nor
a lipids therefore it was novel
type biological molecule. 88
 CHEMICAL STRUCTURE OF NUCLEIC ACID
• Nucleic acids are organic compounds present in virus to human.
• Nucleic acids are composed of Carbon, Hydrogen, Oxygen, Nitrogen
and Phosphorous.
TWO TYPES OF NUCLEIC ACID
1. DNA (DEOXYRIBONUCLEIC ACID)
2. RNA (RIBONUCLEIC ACID)
• Both nucleic
acids (DNA &
RNA) are linear
and un-
branched in
manner.
• Monomers of
nucleic acid are
know as
nucleotides. 89
 NUCLEOTIDES
• Nucleotides of DNA is known as deoxyribonucleotides.
• Nucleotides of RNA is known as ribonucleotides.
• Each nucleotide consists of:
Phosphate
Pentose sugar (skeleton of
nucleotide).
Nitrogen containing ring structure
known as basses.
• Pentose sugar in
deoxyribonucleotide is deoxyribose
sugar where as in ribonucleotide is
ribose-sugar.
• Phosphoric is common component
which provides the acidic properties
to DNA and RNA.
• Nitrogen containing ring structure called base because of un shared pair
of electrons on the nitrogen atom, which can thus acquire a proton. 90
 CLASSES OF NITROGEN BASES
1. SINGLE RING PYRIMIDINE
• Single ring Pyrimidine: There are three types of Pyrimidine bases
{cytosine (C), thymine (T) and uracil (U)}.
• Thymine is only found in DNA and uracil is only found in RNA.
2. DOUBLE RING PURINES
• Double ring Purines: There are two types of purine base {Adenine
(A), guanine (G)}.

91
 FORMATION OF NUCLEOTIDE
1st step
• During the formation of nucleotide, 1st nitrogenous base linked with 1st
carbon of pentose sugar to form nucleoside.
2nd step
• Phosphoric acid attached to 5th
carbon of pentose sugar to
form Nucleotide.
• A nucleotide with one
phosphoric acid is called as
nucleoside monophosphate.
• A nucleotide with two
phosphoric acid is called as
nucleoside diphosphate.
• A nucleotide with three phosphoric acid is called as nucleoside
triphosphate.
92
 MONONUCLEOTIDE
• It is the monomer of nucleic acid as polynucleotide.
• It is formed by single nucleotide.
• Some times, it works independently as mononucleotide.
• It is found in single in cell or part of other molecules.
• These nucleotides contain extra phosphate group as ADP (adenosine
diphosphate) or ATP (adenosine Triphosphate).

93
 Chemical Nature & Role of ATP
• Adenosine triphosphate (ATP) is a mononucleotide.
• ATP has three parts, connected by the covalent bond.
 Adenine a nitrogen base.
 Ribose (five carbon sugar).
 Three phosphates,
• Two covalent bonds
linking the three
phosphates
together are called
as high energy
bonds.
• ATP can be converted into ADP and inorganic phosphate (iP) by
hydrolysis.
• ATP is known as energy currency for the cells.
• One ATP = 7.3 K.CAL/MOLE or 31.81 KJ or 7300 calories. 94
 DINUCLEOTIDE
• Two nucleotides covalently bonded
with each other to form
dinucleotide.
Example: NAD (Nicotine amide
adenine dinucleotide).
• Nicotinamide is vitamin
component.
• Two nucleotides linked with each
other through their phosphate
group, One nucleotide contains an
adenine and other nicotinamide.
• NAD is co-enzyme (inorganic non-
protein part of Enzymes) which
binds to protein part of enzyme in
several oxidation reduction
reactions in cells. 95
 Nicotinamide adenine dinucleotide (NAD)
• NAD Consists of two
nucleotides.
• One nucleotide
consists of
Nicotinamide, sugar
and phosphate.
• Other nucleotide
consists of adenine-
sugar and
phosphate.
• Two nucleotides
linked with each
other through their
phosphate group
forming a
dinucleotide.
• NAD is a co-enzyme. 96
 FORMATION OF PHOSPHODIESTER BOND
• The two nucleotide are also joined together by phosphodiester bonds to
form nucleic acid (DNA or RNA).
• It is considered as back bone of the nucleic acid strands.
• It is condensation
result between
phosphate group
(PO₄³⁻) and of
pentose sugar.
• A phosphodiester
bond occurs when
exactly two of the
hydroxyl groups in
phosphoric acid react
with hydroxyl groups
on other molecules
of sugar to form two
ester bonds. 97
 FORMATION OF PHOSPHODIESTER BOND
• The water molecule is removed and the phosphate group from 5’-
carbon of one nucleotide linked with 3’-carbon of another
nucleotide to form phosphodiester bonds or linkage.
• Thus
phosphodiester
acts as back bone.
• Phosphodiester are
bond which holds
the sugar
phosphate
components of
DNA together.
• This reaction is an
example of an
anabolic process.
98
 POLYNUCLEOTIDE
• When many nucleotides are
linked to each other through
phosphodiester linkage to form
polymer.
• DNA and RNA are example of
Polynucleotide.
• They have variety of
functions/role in living organisms.
• DNA is involved to transfer the
hereditary characters from
parents to offspring.
• Genetic information encoded in
DNA in simple fashion in the form
of code.
• RNA plays an important role in
99
protein synthesis.
 The Watson and Crick DNA model
• in 1953, Francis Watson and James Crick proposed the physical
model of the DNA which is now commonly known as Watson and
crick DNA model.
• DNA is composed of the two polynucleotide chain which are
attached together by nitrogen bases.

100
 The Watson and Crick DNA model
• In order to make base pairing the two polynucleotide chains are
opposite in direction:
• One chain runs from 5’ to 3’ downward.
• One chain runs from 3’ to 5’ upward.
• Both chains show a constant width of 2nm therefore both chains are
supposed be antiparallel with each other.

101
 The Watson and crick DNA model
• Both strands of DNA are connected with each other through hydrogen
bond.
• Two hydrogen bonds are present between adenine and thymine and
three hydrogen bonds are present between guanine and cytosine.
• Each turn of duplex consists of 10 base pairs.
• The sequence can vary in countless ways. The sequence is specific for
different species, organisms and even individuals.

102
 CONCEPT OF GENE (GR: GENOS = BIRTH OR RACE)
• DNA is hereditary material which carries the genetic information
from parents to offspring in the form of genes.
• Genes are located on the chromosomes and each chromosome is
made of many genes.
• Gene is the part od DNA which has information to synthesis of
proteins, which work as enzymes.
• Genes are
vehicles of
inheritances.
• It is the functional
unit of hereditary
material.
• In human total
genes are 30000
to 35000.
• Genes gives the instructions for developing the characters such as eye
and hair colour by producing the enzymes. 103
 TRANSCRIPTION
• It is process in which, formation of mRNA (messenger RNA) from
DNA is known as transcription. (Messenger RNA) mRNA carries
information from DNA (nucleus) to cytoplasm and finally attached
with ribosome for protein synthesis.
TRANSLATION
• It is process in which, two types of RNA (tRNA and rRNA) take part.
• tRNA and rRNA translated information (amino acids) from mRNA to
cytoplasm and attached to ribosome for protein synthesis.

104
 RNA (RIBONUCLEIC ACID)
• RNA is polymer of RNA nucleotides.
• RNA is single stranded and does not form the double helix like DNA.
• 90% RNA is present in cytoplasm and 10% in nucleus.
• Adenine, guanine, cytosine and uracil are nitrogen bases of RNA.
• RNA contains ribose sugar
(C5H10O5).
• Amount of RNA varies from
cell to cell.
• Some regions of RNA shows
the double stranded in their
complementary region.
• There are three major types
of RNA, each with special
function in protein synthesis.
• These RNA are transcribed
from DNA template.
105
 1. Messenger RNA (mRNA)
• The mRNA consists of a single strand of variable length.
• Length of mRNA depend upon genes as well as protein for which, it
is taking message from DNA.
• It contains the information in the form of genetic codes (CODONS).
• Actually three nucleotide in mRNA encodes a specific one amino
acids.
• Such triple nucleotide
along length of mRNA
are called as codons
of genetic codes.
• The mRNA is about 3-
4% of total RNA of
cell.
• The mRNA takes the genetic message from DNA (nucleus) to
ribosomes for protein synthesis in a cell is known as translation.
106
 2. Transfer RNA (tRNA)
• It is the smallest RNA.
• It consists of 70 to 90 nucleotides.
• The tRNA is the single stranded
molecule but it shows the duplex
appearance at its some regions
where complementary bases are
bonded to one an other.
• It shows flat clover leaf shaped.
• It has anticodon of genetic codes as
its complementary form.
• It transfers the related amino acids
from cytoplasm to ribosomes.
• They are sixty in number but
human cell contains only 45-
different types of tRNA.
• Approximately 10-20% of total RNA content of cell are tRNA.
107
 3. Ribosomal RNA (rRNA)
• Ribosome consists of rRNA and proteins.
• It is present in the ribosomes.
• The rRNA have largest size among the RNA.
• Approximately 80% of total RNA
content of cell are rRNA.
• It is part of ribosome where protein
synthesis take place. In other words,
rRNA provides the platform (site) for
protein synthesis.
• The base sequence of rRNA of all
organisms is similar thus there is only
one type of rRNA.
• It is catalytic component of ribosome.
• It is commonly known as rRNA because it is eventually part of the
ribosomes. 108
 CONJUGATED MOLECULES
• Conjugated molecules are type of molecules that are formed by the
combination of two different groups of molecules.
EXAMPLE: When carbohydrates molecule covalently bonded with
protein and more complex molecule is formed known as
glycoprotein.

1. GLYCOLIPIDS OR CEREBROSIDES
• Carbohydrates combine with lipid and also contain nitrogenous
compounds to form Glycolipids.
• Glycolipids are commonly known as cerebrosides because these are
found in white matter of brain, myelin sheath of neuron.
• These are also present in inner membrane of chloroplast.

109
2. GLYCOPROTEIN OR MUCOIDS
• Carbohydrates combine with protein to form glycoprotein.
• Mostly in animals and plants, oligo and polysaccharides covalently
bonded with protein molecules is known as glycoprotein.
• Glycoprotein contains less than 04% carbohydrates in egg albumin
and gonadotrophic hormone (Prolactin hormone).
• Some amount of glycoprotein is present in cell membrane.
• These involved in many physiological functions including,
immunity, transport proteins, receptors, antigen of blood groups etc.
3. LIPOPROTEIN
• The lipoprotein forms, when lipids combine with protein.
• They help to transport the lipids in blood plasma.
• These are frequently found in cell membrane and other type of
membranes in the cell like mitochondria, endoplasmic reticulum,
nuclear membrane etc.
110
4. NUCLEOPROTEIN
• Nucleoprotein are consisting of a protein linked to a nucleic acid,
either DNA (deoxyribonucleic acid) or RNA (ribonucleic acid).
• These are main component of ribosomes, chromosomes and
chromatin material.

THE END

111