Biomolecules

Biomolecules are the complex lifeless molecules which build up living organisms and are required for their
growth, maintenance and ability to reproduce. Some common examples are carbohydrates, proteins,
enzymes, lipids, nucleic acids, amino acids, fats etc. The branch of science which deals with the study of
biomolecules and their role in living systems. called biochemistry. Most of the biomolecules are polymers.

Carbohydrates
These are the naturally occurring organic compounds of C, H and O which are mainly produced by plants. .
In olden days, carbohydrates were regarded as the hydrates of carbon leaving the general formula Cx(H2O)y
Eg: Glucose C6H1206 C6(H2O)6
Sucrose C12H22O11 C12(H2O)11

Limitations of the old definition:

• Several compounds like Rhamnose (C6H12O5)
And deoxyribose (C5H10O4) are carbohydrates but cannot be represented as hydrates of carbon.
• Compounds like formaldehyde [HCHO: C (H2O)] and acetic acid [CH3COOH: C2(H2O)2] which are not
carbohydrates but can be represented by the general formula Cx(H2O)y.

Carbohydrates are defined as optically active polyhydroxy aldehydes or polyhydroxy ketones or the
compounds on hydrolysis.
The carbohydrates which are tasteless, insoluble in water and amorphous are called non- sugars.
Eg: Starch, Cellulose etc.
Carbohydrates are classified into 3 classes depending on upon their behaviour towards hydrolysis.

1. Monosaccharides:
These are the simplest carbohydrates which cannot be hydrolysed into simpler compounds. They
represent the simplest single carbohydrate units.
The common examples are Ribose C5H10O5, Glucose C6H12O6, Fructose C6H12O6 etc.

2. Oligosaccharides:
These are the carbohydrates which give two to ten monosaccharide units on hydrolysis. They are further
classified into disaccharides, trisaccharide, tetrasaccharide etc depending upon the number of
monosaccharides units present in the molecule.

(a) Disaccharides: On hydrolysis gives 2 monosaccharide units. They have the general formula C12H22O11.

(b) Trisaccharide: On hydrolysis gives 3 monosaccharide units. Eg: Raffinose C18H32O16

(c) Tetrasaccharides: On hydrolysis gives 4 monosaccharide units. Eg: Stachyose C24H42O21

3. Polysaccharides:
These are carbohydrates which are polymeric and can be hydrolysed to give many monosaccharide
units. The general formula: (C6 H10 O5)n where n = 100 – 3000.
Eg: Starch, cellulose, glycogen
 REDUCING AND NON – REDUCING SUGARS
Reducing Sugars:
The carbohydrates which reduce Fehling’s solution and Tollen’s reagent are called reducing sugars. They
contain groups which can be easily oxidised by Feling solution or Tollens’s reagent. They contain the full
characteristic groups:
i) Reducing Sugars contain α- hydroxy aldehyde or α hydroxy ketone group.

ii) Reducing sugars contain cyclic hemiacetal or hemiketal groups. In aqueous solutions, these hemiacetals
or hemiketal exist in equilibrium with relatively small concentration of non-cyclic aldehydes or α-hydroxy
ketones having a free -CHO or -CO group.
All monosaccharides are reducing sugars: Glucose, Fructose etc.
Maltose and Lactose are reducing sugars.

Non – Reducing Sugars:

The carbohydrates which do not reduce Fehling’s solution or Tollen’s Reagent are called non- reducing
sugars. They do not contain free aldehydic or ketonic group with – OH group on the c atom adjacent to the
carbonyl group. They contain stable acetals or ketal structures. Their cyclic structures cannot be opened
into an open – chain form having free carbonyl group.
Eg: Sucrose is non – reducing because the reducing groups of glucose and fructose are involved in glycosidic
bond formation. All Polysaccharides [ starch, glycogen, cellulose etc.] are non – reducing sugars.

Monosaccharides:
Monosaccharides are classified as:
i) Aldoses: The monosaccharides containing an aldehyde group are called aldoses. This group is
always present at one end of the C chain [ C1] glucose in an aldose.
ii) Ketoses: The monosaccharides containing a Ketone group is called ketose. In all naturally
occurring ketoses, Keto group is present at the C next to the terminal C [C2]. Fructose is a ketose.

Monosaccharides are further classified as trioses, tetroses, pentoses, hexoses etc depending on the
number of C atoms they contain.
The simplest monosaccharides are trioses.
 D AND L CONFIGURATIONS
These configurations are represented with respect to glyceraldehyde as a standard. The D- -configuration
has -OH attached to the C adjacent to -CH₂OH on the right while L-configuration has -OH attached to the C
adjacent to the -CH₂OH on the left.

All naturally occurring sugars belong to D-Series.

[d and I do not represent dextrorotatory as laevorotatory. The optical activity of the molecule is
represented by + and - which represents the direction of rotation of plane. polarised light. ]

D- glucose D- Fructose

GLUCOSE C6H12O6
Glucose has 4 chiral carbons [2,3,4 and 5].
Preparation of glucose:
1. From Sucrose [Cane Sugar]
Sucrose is boiled with dil. HCl of H₂ 3O4 in alcoholic solution, glucose and fructose is obtained in equal
amounts.

2. From Starch
Glucose is produced commercially by the hydrolysis of starch by boiling it with dilute H2 SO4 . It is then
heated under 2-3 atm pressure steam in an autoclave at 393 K.

STRUCTURE OF GLUCOSE
Glucose is an aldohexose. It is also known as dextrose.
It is probably the most abundant compound on earth. Glucose has an aldehydic group, One 1° alcoholic and
four 2° alcoholic group.
The open chain structure of glucose on the basis of the following was assigned on the basis of the following
evidences:
1. The molecular formula of glucose was found to be C6H12O6
2. Glucose on prolonged heating with HI, gave n-hexane. [ Mixture of n-hexane and 2-iodo hexane]. This
reaction proves that all the Six Carbon atoms in glucose lies in a straight chain.

These reactions prove the presence of a carbonyl group on glucose. [It can be an aldehydic group or а
Ketonic group]
4. Glucose on reaction with a mild oxidising agent. like Bromine water gives gluconic acid.

This reaction proves the presence of an aldehydic group on glucose.

5. Glucose reacts with acetic anhydride in the presence of anhydrous ZnCl 2 to give glucose pentaacetate.
This is known as acetylation of glucose.
This reaction the proves presence of fine -OH groups in glucose. Since glucose exists as a stable compound,
the five -OH groups should be attached to different carbon atoms.
6. On oxidation with conc. HNO₂ ((strong oxidising agent), both glucose. and gluconic acid gives saccharic
and [glucaric acid]

This reaction proves the presence of a primary alcoholic group on glucose.

On the basis of the above reaction. Fischer assigned an open chain structure for glucose.

Cyclic structure of D- Glucose

The open-chain structure of glucose failed to explain the following:
Despite the presence of an aldehydic group,
=> Glucose does not react with sodium bisulphite to form addition products.
⇒ Glucose does not react with ammonia to form aldehyde-ammonia adduct.
⇒ Glucose does not give Schiff's test and 2,4-DNP test like other aldehydes.
⇒ Glucose reacts with hydroxylamine to form an oxime but glucose pentaacetate does not react with
hydroxy amine. This shows that -CHO group is not present in glucose pentaacetate.

• D-(+)-glucose exists in 2 Stereoisomeric forms; α-D- glucose and B-D-glucose.

• α-D-(+) - Glucose is obtained when a concentrated aqueous or alcoholic solution is crystallised at 303 K.
It has a melting point of 419 K. It has an optical activity of +111°.
• β-D-(+)- glucose is obtained on crystallisation of glucose from a hot saturated solution at a temperature
above 371 K. It has a melting point of 423k and an optical activity of +19.2°.
• Both α-D-glucose and β-D-glucose undergo mutarotation.
A freshly prepared solution of α-D glucose has specific rotation of +111°. Its specific rotation decreases
to +52.5°.
 A freshly prepared solution of β-D glucose has a specific rotation of +19.2°. Its specific Rotation
increases to +52.5. The change in specific rotation to a constant value with time is called mutarotation.

The 2 forms of glucose are interconvertible, and it forms equilibrium mixture of both α-D glucose and β-D
glucose.

These results show that glucose does not have an open chain structure. Monosaccharide contains a
number of OH- groups and an aldehyde or keto group. Therefore, they undergo intermolecular reactions
[Within the molecule] to form hemiacetals which results in the cyclic structure. In glucose, the cycle is
formed between C1 and C5.

Glucose has 2 isomers which differ in the orientation of H and -OH around C1 atom. These isomers are
known as α-D-glucose and β-D-glucose.
The isomer having -OH group on the right is called α-D-glucose and the isomer having the -OH group on
the left side is called β-D-glucose.
The pairs of optical isomers which differ in the configuration only around the anomeric carbon are called
the anomers. In glucose, C1 is the anomeric C

The above representation is known as Fischer projection formula.

Pyranose structure: Haworth Projection Formula

The structure of α-D and β-D glucose can be drawn in a simple sixmembered ring called pyranose
structure. These resemble pyran which is a 6-membered heterocyclic ring containing 5 C atoms and one
oxygen atom. These structures are called Haworth projection formula or pyranose structures.
 FRUCTOSE – C6H12O6
Fructose contains a keto group at C-2 and the 6 C atoms are arranged in a straight chain. It belongs to D-
series, and it is levorotatory.

Fructose also has a cyclic structure. The hemiacetal is formed by the intramolecular combination of C 2 keto
group and -OH of C5. [C2 – C5 linkage]

These structures can be represented as furanose structures. [Furan is a 5membered structure containing
oxygen atom] Haworth structures of Fructose.

C2 is the Anomeric carbon in fructose.

DISACCHARIDES
The carbohydrates which on hydrolysis give 2 monosaccharide units are called Disaccharides.
The most common disaccharides are sucrose, maltose, and lactose.
The disaccharides are made up of 2 molecules of monosaccharides linked to each other by the
condensation reaction. The hydroxyl groups (-OH) of the monosaccharides condense together eliminating
a water molecule and form a C-O-C linkage. [The linkage between the monosaccharide units and the
oxygen atom is called glycosidic linkage]
SUCROSE
It is the most common disaccharide, widely distributed in plants like sugar cane and sugar beet. The sugar
obtained from sugar beet is called beet sugar.
Sucrose on hydrolysis with dilute acids or in the presence of the enzyme sucrase (invertase), we get an
equimolar mixture of α-D-(+)- glucose and β-D-(-)-glucose fructose.

Sucrose is dextrorotatory, but on hydrolysis, it gives dextrorotatory glucose and levorotatory fructose.
Fructose has a greater specific rotation. Hence the resulting solution upon hydrolysis is levorotatory in
nature. Since there is a change in the sign of rotation from dextro to levo after hydrolysis, the process is
called inversion of sugar and the mixture of glucose and fructose obtained is called invert sugar.

The α-D-glucose and the β-D-fructose are joined to the glycosidic linkage between the C1 of α-D-glucose
and C2 of β-D-fructose.

Sucrose is a non-reducing sugar.

MALTOSE [MALT SUGAR]
Maltose is a disaccharide which on hydrolysis in the presence of maltase enzyme gives 2-α-D-glucose units.

Maltose is a reducing sugar. The glycosidic linkage is formed between C1 of one α-D-glucose and C4 of the
other α-D-glucose.
 LACTOSE [MILK SUGAR]
Lactose is a disaccharide which on hydrolysis in the presence of lactose enzyme gives β-D-glucose and β-D-
Galactose

Lactose is a reducing sugar. The glycosidic linkage in lactose is formed between C1 of the β-D-glucose and C4
of β-D-Galactose.

• Fructose is the sweetest natural sugar. The different artificial sweeteners are saccharin, sucralose,
aspartame and alitame.
• Saccharin is 550 times sweeter than sugar. It is mainly used as a sweetening agent by diabetic
patients.
• Aspartame is nearly 100 times sweeter than sucrose. It decomposes at baking or cooking
temperature and hence can be used only in cold foods and soft drinks.
• Alitame is nearly 2000 times sweeter than sucrose [Higg-potency sweetness]. Its sweetness cannot
be controlled. Hence alitame is not used as an artificial sweetener.
• Sucralose is a tri-chloro derivative of sucrose. It is stable at cooking temperatures. It is also 600
times sweeter than sucrose. It neither provides calories do not cause tooth decay. Hence it is
preferred to be used as an artificial sweetener.
• Sucrose is a non-reducing sugar and is not readily oxidized as a reducing sugar. Therefore, it is
much more useful for preserving foods like jams and jellies. Reducing sugar like glucose would
oxidize and spoil the food.
POLYSACCHARIDES
These are carbohydrates which contain hundreds to thousands of monosaccharides units joined by
glycosidic linkages. They are colorless, tasteless, and insoluble in water.

STARCH (C6H10O5)n
It is the main storage polysaccharide of plants. Starch is mainly present in wheat, rice, maize, potato etc.
Starch is a white powder which is insoluble in cold water.
The presence of starch can be identified using iodine solution. Starch gives a blue-black color when iodine
is added.
Starch on hydrolysis with dilute acids or enzymes gives α-D-glucose units.

Starch is a non-reducing saccharide. Starch has 2 components: Amylose and Amylopectin.

 AMYLOSE
It is water-soluble. It is a linear polymer of α-D-glucose. Amylose contains 200-100 α-D-glucose units linked
through glycosidic linkages involving C1 of one glucose and C4 of the adjacent glucose.

AMYLOPECTIN
It is water-soluble. It is a highly branched polymer. It consists of many short chains each containing 20-25
glucose units which are joined together through glycosidic linkages involving C1 of one glucose with C4 of
the other. The C1 end of the terminal glucose in each chain is further linked to the C6 of some other glucose
in the next chain through C1 - C6 glycosidic linkage.

CELLULOSE
It is present in plants where it constitutes the bulk of the cell wall. Cellulose forms the fibrous component
of plant cell walls. Cellulose is a non-reducing polysaccharide.
Cellulose on hydrolysis gives β-D glucose units. The glycosidic linkage is formed between C1 of one glucose
and C4 of the next glucose unit.
Cellulose finds use in textile, paper when treated with a wide variety of and plastic industries. chemicals it
forms. many useful products, celluloid, rayon, gun cotton (Explosive) cellulose acetate (Plastics and
wrapping films) etc.
GLYCOGEN
Glycogen is a polysaccharide of α-D-glucose. The carbohydrates are stored in animal body as glycogen.
Glycogen is known as animal starch because its structure is like amylopectin. Glycogen is more is more
highly branched than amylopectin. Glycogen is stored in liver, brain and muscles of human beings. when
the body glucose during strenuous exercise needs -fasting, the enzymes De break down glycogen to provide
glucose Glycogen is also present in yeast and fungi.
PROTEINS
biomolecules of amino acids present in all living cells. The chief Source of proteins are milk, fish, meat,
cheese, pulses, peanuts etc. Each living cell is made up of thousands of different proteins. Protein are the
condensation polymers [Polyamides] in which the monomeric units are α- amino acids.
Amino acids are organic compounds containing both amino group and carboxyl group.

The -NH₂ - group is attached to the α-C. Hence it is called α-amino acid. α -amino acids are the building
blocks of proteins. Except Glycine [H₂N-CH₂-COOH], all other α -amino acids have chiral carbon and they are
optically active. All naturally occurring amino acids belong to L-series.

There are so different naturally occurring α Animo acids.

Amino Acid Symbol Side Chain R
Acidic Amino Acids
Aspartic Acid Asp D CH2COOH
Aspargine Asn N CH2CONH2
Lylutamic Acid Lylu E CH2CH2COOH
Basic Amino Acids
Lysine Lys K CH2(CH2)3NH2
Arginine Arg R

Histidine His H

Amino acids are classified as acidic basic or neutral depending on the relative number of amino and
carboxyl groups.
Neutral amino acid: Contains equal number of NH2 and COOH groups. Ex: lylicine, alanine, valine, etc
Acidic amino acids: contain more number of carboxyl groups than amino groups. Ex: Aspartic acid,
lylutamic acid, etc
Basic amino acids: Contain more number of amino groups than carboxyl groups. Ex: lySine, Histidine, etc

Certain amino acids can be prepared by our bodies we do not require them in our diet. These amino acids
are called non-essential amino acids, 10 out of 20 amino acids are prepared by our body. Ex; Glycine,
alanine, Secine, etc

The other 10 amino acids cannot be prepared by our body. They have to be supplied through our diet.
These are called essential amino acids. Ex: Valine, Leucine, Lysine, etc
 PHYSICAL PROPERTIES OF AMINO ACIDS
Usually colourless, non-volatile crystalline solids.
Soluble in water and have high melting points.
Behave like salts due to the presence of both acidic and amino groups in the same molecule. The proton of
the carboxyl group migrates to the amino group.

All α-amino acids exist largely in In amino acids, the basic character is due to -COO-. group whereas acidic
character is due to -NH3+ group.

when we place the aqueous solution of an amino and in an electric field, its behaviour will depend upon
the acidity of basicity of the solution.
In alkaline solution, the amino acid migrates towards the anode under the influence of electric field.
In acidic solution, the amino acid migrates towards the cathode under the influence of electric field.
The pH at which an amino acid does not migrate towards the anode of cathode under the influence of an
electric field is called isoelectric point. At the isoelectric point, the amino acid has the least solubility in
water and this property is used for the separation of different amino acids.

All alpha-amino acids on treatment with ninhydrin gives purple colouration. This test is called ninhydrin
test used for the detection α-amino acids

Peptides and Proteins:

Peptides are amides formed by the condensation of 2 or more same or different alpha- amino acids with
the elimination of a molecule of water. The resulting -co-NHL linkage is called a peptide linkage or peptide
bond

A dipeptide consists of 2 amino acids with one peptide linkage

A tripeptide consists 3 amino acids with two peptide linkages.
A tetrapeptide consists of 4 amino acids with three peptide linkages

If a large number (α-amino acids (hundreds to thousands) are joined by peptide bonds, the Resulting
polyamide is a polypeptide [A peptide having molecular mass more than 10000 U; is a protein].
Each polypeptide chain has a free amino group at one end and a free carboxyl group at the other end.
The amino acid unit having the feel -NH2 group is called N-terminal amino acid whereas the amino acid unit
having the free - COOH group is called the C-terminal amino acid

Polypeptides amphoteric in nature because are the presence of terminal ammonium and carboxylate ions.
as well as the ionised side chains of amino and residues.
 CLASSIFICATION OF PROTEINS
On the basis classified as of molecular structure, proteins are classified as:
(a) Fibrous Proteins:
• Consists of linear thread-like molecules which tend to lie side by side to form fibres. They. are held
together by hydrogen bonds or disulphide bonds.
• They are insoluble in water due to the strong inter-molecular forces of attraction.
• These proteins are stable to moderate changes in temperature and pressure.
• Fibrous proteins serve as a of animal tissues. chief structural material of animal tissues.
• Eg: Keratin in skin, hair, nails and wool,
Collagen in tendons muscles
Fibroin in silk and
Myosin in Muscles

(b) Globular Proteins:

• The molecules. are folded together into a compact unit forming spherical shapes [spheroidal].
• The рерtide chains are held by hydrogen bonds but these forces are comparatively weak.
• They are soluble in water.
• They are sensible to small changes in temperature and pressure.
• Ex; Albumin, insulin, antibodies, haemoglobin, etc

STRUCTURE OF PROTEINS
Primary structure
Each polypeptide chain in protein has amino acids linked with each other in a specific sequence. This
specific sequence is the primary structure of protein
The importance of 1° structure of a proteins in determining its biological activity is shown by the fact that,
replacement of just one amino and in the sequence of a protein destroys its biological activity.
Eg: Replacement of glutamic by acid by valine in the protein haemoglobin, results in sickle cell anaemia.

Secondary structure
20 structure gives the manner in which the polypeptide chains are folded or arranged. It gives the shape or
conformation of the protein molecule. The peptide bonds and hydrogen bonds stabilize the 2° structure.

(i) α-Helix structure

• The polypeptide chains are folded and twisted into a right-handed helical structure with the - NH
group of amino acid residue hydrogen bonded to the - C=0 group of the adjacent turn of the helix.
• The helix is right-handed.
• The α-helix is also known as 3.613 helix since. each turn of the helix has approximately 3.6 amino
and a 13-membered ring formed by H-bonding.

• Many fibrous proteins such as keratin in hair, nail, skin and myosin in muscles have α-helix structure.
 • Globular proteins also contain segments of α-helix.
• Because of the helical structure, human hair fibres are stretchable and elastic to a small extent.
When the human hair fibre is stretched, the hydrogen bonds are either stretched or broken but
when the stretching force is removed the hydrogen bonds reforms. This makes the hair fibres
elastic.

b) β-pleated sheet structure

• The polypeptide chains lie side by side in a zig-zag manner with alternate R groups on the same side
situated at fixed distances apart.
• Two such neighbouring polypeptide chains are held together by intermolecular H bonds.
• A number of such chains are inte rbound to form a sheet. These sheets are then stacked one above
the other to form a 3D structure.
• Keratin protein in hair has parallel β-sheet structure and silk protein fibroin has antiparallel β-sheet
structure.

Tertiary structure
• It arises due to folding, coiling and bending of polypeptide chains producing 3D structures.
• This structure gives the overall shape of proteins.
• The structure is stabilized by H bonds, disulphide linkage, Van der Waal's and electrostatic force of
attraction.

Quartenary structure
• Some proteins are composed of 2 or more polypeptide chains called sub units. These may be
identical or different. These are held together by non-covalent forces such as H bonds, electrostatic
interactions and van der Waals interactions.
• The 4° structure refers to the determination of the number of subunits and their arrangement in an
aggregate protein molecule.
• Haemoglobin is a protein possessing a 4° structure.

Denaturation of Proteins
• A protein found in a biological system having a unique 3D structure and specific biological activity is
called a native protein. When a native protein is subjected to physical change like temperature
changes or chemical change in pH (presence of salts or acids), the 20 and 30structure of the protein
is destroyed. Thus, a process that changes the physical and biological properties of proteins without
affecting the chemical composition of a protein is called denaturation.
• The 1° structure of the proteins remains intact during denaturation. Denaturation may be reversible
or irreversible.
• Eg: On boiling, the egg albumin becomes rubbery and insoluble in water. Curdling of milk.

Note: [Deficiency disease of essential amino acid in Kwashiorkor (water balance of the body is disturbed)]

ENZYMES
These are biological catalysts produced by living cells which catalyse the biochemical reactions in living
organisms. Enzymes are simple or conjugated proteins. Almost all enzymes are globular proteins.
Without enzymes the living processes would be very slow to sustain life. Without enzymes it would take 50
years to digest a single meal. All enzymes are specific in nature.
Most of the enzymes are named after the reaction where they are used.
Ex: Oxidoreductase, the enzyme which catalyses the oxidation of one substrate with the simultaneous
reduction of another substrate.

PROPERTIES OF ENZYMES
• Highly efficient: They increase the speed of reactions up to 10 million times because the enzymes
reduce the magnitude of activation energy.
• Extremely small quantities: A small amount (one millionth of mile) can increase the rate of reaction
by 103 to 106
• Specificity: Almost every biochemical reaction is controlled by its own specific enzymes.
Eg: Maltose is converted to glucose in the presence of maltase. No other enzyme can catalyse this
reaction.
• Optimum temperature and pH: The enzymes are active at moderate temperatures (37°C) and pH
(around 7)
• Control of activity of enzymes: The action of enzymes is controlled by various mechanisms and are
inhibited by various organic and inorganic molecules. The activity of most enzymes is closely
regulated.

Coenzymes
• Most active enzymes are associated with some non-protein compounds required for their activity.
These are called prosthetic groups.
• The prosthetic group which is covalently attacked with the enzyme molecule is called cofactor. The
prosthetic groups which get attached to the enzyme at the time of reaction are known as
coenzymes.
• These are generally metal ions of small organic molecules. The common metal ions are Ln, Mg. Mn,
Fe, Cu, Co, Mo, K and Na

Mechanism of Enzyme Action [Lock and key Mechanism]

The various steps involved in the enzyme catalysed reaction

1. Binding of the enzyme (E) to substrate (s) to form a complex.

2. Product formation in the complex.

3. Release of product from enzyme-product complex.

• The catalytic property of enzymes is present at certain specific regions on their surfaces. These sites
are called the active sites.
• The active sites have characteristic shape and fits suitably shaped specific substrate molecules.
Specific binding accounts for the high specificity of these enzyme reactions. The specificity of fitting
together of the substrate structure and the enzyme structure may be compared as a key fitting into
a lock.
• The deficiency of phenylalanine hydroxylase enzyme causes a disease called phenyl-ketone urea
(PKU). This disease causes accumulation of compounds in the body which results into severe brain
damage and mental retardation in children.

HORMONES
• Hormones are the chemical substances which are produced in the ductless glands in the body.
Hormones are the chemical messengers of the body. The deficiency of hormones causes metabolic
disturbances in the body.
• In mammals, the secretion of hormones is controlled by the anterior lobe of the pituitary gland
present at the base of the brain.
Based on the structure, hormones are classified into 3 types
Steroid hormones: contain a steroid nucleus.

Eg Testosterone,
androgens, etc.

Protein or Polypeptide hormones: contain a peptide chain. Ex; Oxytocin, insulin

Amine hormones: Water-soluble compounds which have amino group and are structurally derived from
amino acids. Eg: Adrenaline and thyroxine.

VITAMINS

• These are organic compounds which cannot be produced by the body and must be supplied in small
amounts in diet to perform specific biological functions for the normal health, growth and
maintenance of the body.
• The absence or deficiency of a vitamin can cause specific diseases. Multiple deficiencies caused. by
lack of more than one vitamin are called avitaminoses.
• The vitamins are designated as A, B, C, D, E and K. Any subgroups of individual vitamins is
designated by the number subscript. Eg. A₁, A2, B1, B2, B6, B12, D1, D₂ etc.

Based on the solubility, they are divided into 2 types.

Water Soluble vitamins:
• Stored in much lesser amounts in the cells.
• Must be supplied regularly in diet because they readily excreted in urine and cannot be stored
(except vitamin B12) in our body.
• Vitamin B and C are water soluble.
Fat Soluble vitamins:
• Vitamin A, D, E and K are fat soluble.
• Vitamin A and D are stored in Liver cells.
• Their deficiency can cause malabsorptive disease.
• These vitamins is harmful and may cause hyper vitaminoses.
 NUCLEIC ACIDS
- Every generation of each and every species resembles its ancestors in many ways.
- The nucleus of a living cell is responsible for the transmission of these characteristics [Heredity]
from generation to generation.
- These are particles present in the nucleus of the cell which responsible for transmission of inherent
characters are called chromosomes which are made up of proteins. combined with biomolecules
known as nucleic acids.
- Nucleic acids are biologically important polymers which are present in all living cells.
- The repeating units of nucleic acids are called nucleotides.
- Nucleic acids are called polynucleotides.
- There are 2 types of nucleic acids: DNA (deoxyribonucleic acid) and RNA (ribonucleic and)

A Nucleotide consists of 3 chemical components:

• A nitrogen containing heterocyclic base [Purines and Pyrimidines]
• A pentose sugar.
• A phosphate group.

Bases:
• Pyrimidines have single heterocyclic a have a fused ring while Purines have two fused rings.
• The purines in nucleic acids are Adenine (A) and Guanine (G).
• The pyrimidines in nucleic acids are cytosine (C), thymine (T) and Uracil (U).
• Adenine, Guanine and cytosine are found in both DNA and RNA.
• RNA contains Uracil instead of thymine [which is present in DNA]

Sugars:
There are two types of sugars in nucleic acids, namely,
- the pentose (5-membered) sugar in RNA is β-D- Ribose and
- the prentose sugar in DNA is β-D-2-deoxyribose

Phosphate group:

Nucleotide and Nucleoside

• The molecules in which one of the nitrogenous base bonded with a sugar.
Base + Sugar → nucleoside.
 • When the phosphate group is attached to the nucleoside, the compound formed is called
nucleotide.
• A nucleotide is a phosphate ester of nucleoside and consists of a purine of pyrimidine base, the
pentose Sugar and one or more phosphate groups. Nucleosides are joined by phosphate linkages to
form nucleotides.

• In nucleotides, the sugar rings are attached to the nitrogen atom of the heterocyclic ring by a bond
between C, atom of sugar and nitrogen atom of heterocyclic ring.
• Nucleotides are joined together by phosphodiester linkages between 5' and 3’ carbon atoms of
pentose sugar.
STRUCTURE OF DNA
(1) Primary structure
- The Sequence of nucleotides in the nucleic acid chain is called its primary structure.
- The 3D Structure of DNA was given by James Watson and Francis Crick called as Watson and Cricle
Model.
- They proposed that DNA have double helical structure. DNA consists of 2 light handed helical
polynucleotide chains coiled around the same central axis.
- The 2 Strands of DNA are antiparallel. [their 5' →3' phosphodiester linkages sun in opposite
directions].
- The nucleotides making up each strand of DNA are connected by phosphate ester bonds.
- This forms the backbone of each DNA strand from which the bases extend.
(2) Secondary structure of DNA
The & strands are held together by Hydrogen bonds. The hydrogen bonding is very specific because the
structures of bases permit only one mode of pairing. [Base Pairing Principle]
Eg: Guanine bonds to cytosine and adenine bonds to thymine.
Thymine and adenine are joined by 2 hydrogen bonds. Guanine and cytosine are joined by 3 hydrogen
bonds.

•
 • The 2 strands of DNA are Complementary to each other in the sense that the sequence of bases in
one Strand automatically determines that of other.
RNA
• The structure of RNA is similar to that of DNA except that it is single stranded.
• There are 3 types of RNA
(1) Messenger RNA (m-RNA)
(2) Ribosomal RNA (r-RNA)
(3) Transfer RNA (t-RNA)
• Sometimes the RNA strand fold back on themselves to form a double helical structure.

Biological functions of Nucleic Acids

DNA controls heredity and it is the reserve of genetic information. The important biological functions of
nucleic acids are:
(1) Replication:
• The process by which a single DNA molecule produces two identical Replication. copies of itself is
called cell division (mitosis).
• Replication of DNA is an enzyme catalyzed process.
• The strands of the DNA partially unwind and each strand serves as a template for the synthesis of a
new DNA molecule.
• Due to the unique specificity of base parking, the newly synthesised complementary strand in each
case is the exact copy of the originally separated DNA.
• One strand comes from parent DNA and the other is newly synthesised.
• In this way, hereditary traits are transmitted from one cell to the other.

• When the DNA strands uncoil, we get 2 strands.

• Each strand acts as a template to build identical double helixes. The complementary strands are:

• These 2 double helices are identical to each other and thus the original DNA strand is repeated.
• The DNA replication is semi-conservative, i.e. only half of the parental DNA is conserved and only
one strand is synthesised.
• DNA replication takes place only in the 5'→3' direction.
(2) Protein Synthesis:
• This process serves as machinery of the living cell.
• The genetic information coded in DNA in the form of specific base sequences is translated and
expressed in the form of sequence of amino acids which results in the synthesis is of specific
proteins.
 • The proteins are synthesised by various RNA molecules but the message for the synthesis of a
particular protein is coded in DNA.
• Transcription and Translation are the 2 main steps in protein synthesis.

3. DNA fingerprinting:
• Each and individual has a unique fingerprint.
• It can be used for identification. However, these maybe altered by surgery.
• The unique fingerprints are due to unique sequences of bases on DNA for every person.
• The technique for identifying individual person based upon the uniqueness of their DNA pattern is
called DNA fingerprinting. It is the same for every cell and cannot be altered in any way.
• The important uses of DNA fingerprinting are:
-In forensic laboratories for identification of criminal.
-To determine paternity of an individual
-To identify dead bodies in any accident by comparing the DNA's prints of parents of
children.
-To identify racial groups to rewrite biological evolution.
4. Mutation:
• It is a chemical change in the sequence of nitrogenous bases in DNA molecule that could lead to
synthesis of proteins with different amino acid sequence the change in DNA molecule can occur
spontaneously De it may be caused by radiation, chemical agents or viruses.
• Most of these changes in DR the DNA molecule are automatically repaired by special enzymes of
the cell.
• The altered proteins caused by mutation may I lose their biological activities and thus cause the
death of a cell. The defective genes can also cause abnormalities of diseases.
LIPIDS
These are oily, fatty or waxy substances present in living organisms. They form part of structure of
biological membranes and store energy for the cell.