Biomolecules

Prepared by Vikas Bhatia

Carbohydrates
Cane sugar, glucose, starch and so on are a few examples of carbohydrates. The general formula for carbohydrates is
Cx(H2O)y. Carbohydrates are generally hydrates of carbon, which is where the name was derived. So, carbohydrates on
hydrolysis produce polyhydroxy aldehydes or polyhydroxy ketones.

Classification of Carbohydrates
(a) On the basis of Physical Characteristics
(b) On the basis of Hydrolysis
(c) On basis of test with reagents (like Benedict’s solution, Tollen’s reagent and Fehling’s solution)

(a) On the basis of Physical Characteristics

(i) Sugar: Characteristics of sugars are crystalline substances, taste sweet and readily water soluble. Because of their
fixed molecular weight, sugars have sharp melting points. A few examples of sugars are glucose, fructose, sucrose,
lactose, etc.
(ii) Non-Sugars: Amorphous, Tasteless, water-insoluble substances with variable melting points e.g., Starch.

(b) On the basis of Hydrolysis

(i) Monosaccharides
A carbohydrate that can be hydrolysed only once to break down into simpler units of polyhydroxy aldehyde or ketone is
called monosaccharide. These include glucose, fructose, etc.
(ii) oligosaccharides
Sugars that on hydrolysis produce two or more molecules of monosaccharides are called oligosaccharides. These are
further classified as di-, tri- or tetrasaccharides, etc.
1. Disaccharides
These are sugars that produce two molecules of the same or different monosaccharides on hydrolysis. Examples are
sucrose, maltose, and lactose. An example of disaccharides is sucrose: C12H22O11.
2. Trisaccharides
Sugars that yield three molecules of the same or different monosaccharides on hydrolysis are called trisaccharides. An
example of trisaccharides is Raffinose C18H32O16
(iii) polysaccharides
On hydrolysis, polysaccharides yield a large number of monosaccharides units. An example of a polysaccharide is starch
cellulose.
(c) On basis of test with reagents (like Benedict’s solution, Tollen’s reagent and Fehling’s solution)
1. Reducing sugar
These have a free aldehyde (-CHO) or ketone group.
These have the ability to reduce Fehling’s or Benedict’s Solution or tollen’s reagent.
Examples include maltose, lactose.
2. Non reducing sugar
A free aldehyde or ketonic group is absent.

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They can not reduce tollen’s reagent or fehling’s solution.
Examples are sucrose, raffinose.
Structure of monosaccharides

Open chain structure

D- and L- Sugars
The –OH attached to the carbon adjacent to CH2OH is on right then carbohydrate has D family while on left belongs to L
family.
Glucose
Preparation:
(a) From sucrose (cane sugar): Boiling sucrose with diluted HCl or H2SO4 in alcoholic solution produces glucose and
fructose in equal proportions.

(b) From starch

Industrially, glucose is manufactured by the hydrolysis of starch by boiling it with dil. H2SO4 at 393 K under pressure.

Structures of Glucose
Glucose has one aldehyde group, one primary (—CH2OH) group and four secondary (—CHOH) hydroxyl groups,
(a) Acetylation of glucose with acetic anhydride forms a pentaacetate, proving the presence of five hydroxyl groups
in glucose.
Presence of aldehyde group
(b) Glucose reacts with hydroxylamine to form monoxime and adds up a molecule of hydrogen cyanide to form a
cyanohydrin.

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Presence of six carbon atoms
(b) On prolonged heating with HI, glucose forms n-hexane, indicating that all the six carbon atoms in glucose are
linked linearly.

Oxidation of glucose
Glucose gets oxidised to six carbon carboxylic acid (Gluconic acid) on reaction with bromine water.

Cyclic structure of glucose

The open chain structure of glucose can’t explain the following propertiesGlucose does not react with Schiff’s reagent.
Glucose does not react with sodium hydrogen sulphite.
Penta acetate derivative of glucose does not react with hydroxylamine.
Glucose in open chain structure does not show mutarotation In order to explain these properties, which are not
consistent with the open chain structure, a ring structure was proposed for glucose.
Isomeric forms of cyclic chain of glucose
The cyclic structure is attributed to the formation of hemiacetal the cyclic structure thus formed is a six-membered ring.
In α-D-glucose, the OH group at C1 is towards right while in β-D-glucose, the OH group at C1 is towards left. Such a pair
of stereoisomers which differ in configuration only around C1 are called anomers
Mutatrotation
the interconversion between anomers of a particular carbohydrate to form an equilibrium mixture is called
mutarotation
Fischer projection of glucose

Haworth structure of glucose

The six-membered ring structures of glucose can be called pyranose structures, in analogy with pyran. Hence, the
anomers are called alpha D (+) gluco pyranose and beta D (+) gluco pyranose.

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Fructose
It is a ketohexose as it contains six C- atoms and ketonic group. It is called fruit sugar as it occurs in fruits. It belongs to D-
series and is a laevorotatory compound. It is appropriately written as D-(–)-fructose.

Cyclic structure of Fructose

The cyclic structure is a five-membered ring. Therefore, there are two possible isomeric forms. The two cyclic forms
differ in the configuration of the hydroxyl group at C 2. These isomers are called anomers.

Haworth structure of fructose

The five-membered ring structure of fructose is called furanose. The cyclic structures of the two anomers are named
alpha D (-) fructofuranose and beta D (-) fructofuranose.

Disaccharides
Disaccharides are formed from two monosaccharides, covalently linked together. The three important disaccharides are
sucrose, maltose and lactose.
Glycosidic bond
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The bond between two monosaccharides is called a glycosidic linkage or a glycosidic bond. The two monosaccharides
are joined together through an oxygen atom.

Sucrose
Sucrose is obtained from sugarcane or sugar beets. It has the chemical formula, C12H22O11. Sucrose is made up of C1
of alpha D glucopyranose — and C2 of beta D fructofuranose. sucrose is called a non-reducing sugar.

Properties of sucrose
Sucrose is dextrorotatory but after hydrolysis gives dextrorotatory glucose and laevorotatory fructose.

Maltose
Maltose is disaccharide, which contains two glucose units.
(a) Preparation: Fractional hydrolysis of starch by enzyme diastase.
(b) Units: Two units of α-D glucose.
(c) Reducing sugar
(d) Linkage: α glycosidic linkage between C1 and C4 carbon atoms.

Structure of maltose

Lactose
It is more commonly known as milk sugar since this disaccharide is found in milk. It is composed of β-D-galactose and β -
D-glucose

Sweetness of sugars

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All the monosaccharide and disaccharides are sweet in taste and hence also known as sugars.
Sucrose is given sweetness value of 100. The sweetness of other sugars is compared with the value of sucrose.
The sweetness of fructose -173, invert sugar 130, sucrose 100, glucose 74,glactose 32,maltose 32 and that of lactose is
16.

Polysaccharides
Polysaccharides contain many monosaccharide units joined covalently by glycosidic linkages.
The common polysaccharides are:
(i) Starch
(ii) Cellulose
(iii) Glycogen

(i) Starch
It is the main storage polysaccharide for plants. It is a polymer of alpha-glucose. It consists of two components:
amylase, and amylopectin.
(a) Amylose
Amylose is water soluble component and constitutes about 20% of starch. It is long chain unbranched polymer.
These are linked together by alpha linkage involving C-1 of glucose unit to C-4 of the other.

(b) Amylopectin
Amylopectin is insoluble in water and constitutes about 80% of starch. It is a branched chain polymer.

(ii) Cellulose
It is found in all plants
It constitutes 50% of total organic matter in the living beings.
Cotton is pure cellulose.
Cellulose is linear polymer of beta D-glucose.
Cellulose gives many useful products when treated with different chemicals like rayon, gum, cotton etc.
Cellulose is directly used in making cloth and paper.

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Structure of cellulose

(iii) Glycogen
The glycogen is stored in animal body in the form of glycogen. It also known as animal starch, because its structure is
similar to amylopectin.

Importance of carbohydrates bio molecules

1. Carbohydrates are essential for life in both plants and animals.
2. They form major part of our food and store chemical energy in plants.
3. They act as the major source of energy for all the animals.
4. In the plants they are important constituent of supporting tissues e.g. cellulose in wood, cotton in clothes.
5. The main source of energy of animals is glucose which is in the form of glycogen.

1. What are biomolecules?

Ans: These are complex lifeless complex organic compounds which can combine in specific manner to produce life.

2. What does sucrose give on hydrolysis?

Ans: Sucrose on hydrolysis gives a mixture of glucose and fructose.

3. Name two important polysachharides of D-glucose.

Ans: Amylose and Amylopectin.

4. Why are carbohydrates generally optically active?

Ans: Because they have one or more chiral carbon atom.

5. Name one reducing and one non-reducing disaccharide.

Ans: maltose is reducing and sucrose is non-reducing sugar.

6. Why is glucose given to patients under exhaustion?

Ans: It is an instant source of energy and given to patients under exhaustion.
7. Why is cellulose not distinguishable in human being?
Ans: Because human stomach does not have enzyme capable of breaking cellulose molecules.
8. Why carbohydrates act as biofuel?
Ans: Because their slow oxidations by a series of steps provide energy for living organisms.
9. What is meant by inversion of sugar?
Ans: The change of specific rotation of sugar form dextro rotatory to leavo rotatory is called inversion of sugar.
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10. What is the name given to the linkage which holds together monosaccharide units in polysaccharides?
Ans: Glycosidic linkage

Proteins
Proteins
Proteins are the complex nitrogenous organic substance that occurs in all animals and plants. The word protein is
derived from Greek word, “proteios” which means primary or of prime importance. All proteins are polymers of α-amino
acids.
Functions of proteins
Proteins promote growth
Proteins supply essential amino acids to blood.
They help maintain body tissues.
Proteins synthesize various enzymes.
Proteins protect the body from infections.

Structure of proteins
They are condensation polymers of about 20 different alpha amino acids, which are linked by peptide bonds. A peptide
bond is formed when amino group of one amino acid molecule interacts with the carboxyl group of another amino acid
molecule.

Amino acids
Amino acids are compounds that have one or more amino groups (-NH2)and carboxyl groups (-COOH) in a molecule.
Amino acids are the building blocks of proteins.
Due to transfer of proton from carboxy to amino group, alpha amino acid exists as dipolar ion or called as Zwitter ion.

Types of amino acids on the basis of position of amino groups

On the basis of relative position of amino group with respect to carboxyl group amino acids are classified into alpha,
beta, gamma

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Types of amino acids
1. Essential
2. Non essential
1. Essential amino acids
The amino acids that can’t be made in our body and must be supplied from outside.
2. Non essential amino acids
They are those amino acids that can be synthesized in our body.

Amino Acids Classification

Amino acids are classified into
Acidic amino acid
If numbers of carboxyl groups are more than amino groups the amino acids are acidic. Example-glutamic acid.

Basic amino acid

If numbers of amino groups are more than carboxyl groups, then amino acids are basic in nature. Example-lysine.

Neutral amino acids

The amino acid having equal number of carboxyl and amino groups are called neutral amino acids. Example-valine

Isoelectric Point
The isoelectric point (pI) of an amino acid is the pH at which it has no net charge. In other words, it is the pH at which
the amount of negative charge on an amino acid exactly balances the amount of positive charge

Peptide bond and polypeptide

The amide linkage (-Co-NH-) by which α-amino acids are joined in linear fashion in proteins is called peptide linkage.
Peptide linkage is an amide formed between –COOH and NH3 group by elimination of water.
When many molecules of amino acid joined together by peptide linkages they form polypeptide which is proteins.

Classification of proteins (on the basis of molecular shape)

Fibrous proteins: The proteins in which the polypeptide chains lie side by side to form fiber like structure. The
polypeptide chain held together by hydrogen bond. Example: keratin ( in hair, skin, nails)
Globular proteins: The proteins have intramolecular hydrogen bonding and are folded to form spherical structures are
called globular proteins. Example: haemoglobin (in blood)

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Classification of proteins
On the basis of composition
Simple proteins: On hydrolysis they give only amino acids.
Example: Globulins and albumin

Conjugated proteins: They contain non protein group attached to the protein part. These non protein groups are called
prosthetic groups.
Example: Nucleo-protein contains nucleic acid, phosphor-protein contains phosphoric acid contains phosphoric acid,
glycol-proteins contains carbohydrates etc.

Derived proteins: These are the degradation products obtained by the hydrolysis of simple and conjugated proteins.
Example: Peptides, peptones etc

Structure of protein
The structure of proteins is studied at four different levels, in the ascending order of their complexity, as primary,
secondary, tertiary and the quaternary structure.
Primary structure of Proteins:
The specific sequence of amino acids in the polypeptide chain reflects the primary structure of proteins.

Secondary structure of protein:

The secondary structure of proteins refers to arrangement of the polypeptide chains in space
types of secondary structure
There are two types of secondary structure :
Alpha helix
Beta pleated sheet

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Alpha helix
If the size of group R is large, intermolecular hydrogen bonds are formed between CO of one amino acid residue and NH
of the fourth amino acid residue in polypeptide chain which gives right handed alpha helix structure to the protein
molecule. Example: Alpha keratin in hair etc
Beta pleated sheet
If the size of group R is small, intermolecular hydrogen bonds are formed between CO of one polypeptide chain with NH
of the other chain. Thus the chains are bonded together forming a sheet which can slide over each other to form a three
dimensional structure called beta pleated sheet. Example: silk
Tertiary structure
The tertiary structure of proteins describes the further folding of the secondary structure. The tertiary arrangement of
helices and sheets is held together by hydrogen bonding, disulphide linkages, van der Waals forces and electrostatic
forces of attraction.
Quaternary structure
Quaternary structure describes how the sub-units are arranged in space relative to one another in the complete protein.

Forces that stabilize protein structures

Hydrogen bonding
ionic bonding
Hydrophobic bonding
Covalent bonding
Hydrogen bonding
These forces operate between a partially positive hydrogen and partially negative atom like O or N on the same or on
another molecule.
ionic bonding
A bonding between cation and anion of side chains resulting in side linkage.
Hydrophobic bonding
In aqueous solutions proteins fold in such a way that these chains get clustered inside the folds .The polar side chains
which are hydrophilic lie on the outside or surface of proteins.
Covalent bonding
The bond occurs between S atoms of two residues between two adjacent chains.
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Denaturation of proteins
The globular proteins, which are soluble in water on heating or on treatment of mineral acids or bases undergo
coagulation or precipitation to give fibrous proteins which are insoluble in water. After coagulation, proteins lose their
biological activity this is called denaturation.

ENZYMES
All biological or bio-catalysts which catalyze the reaction in living organisms is called enzymes. All enzymes are protein.
Enzymes help in the digestion of food and absorption of certain molecule producing energy.
Some important enzymes with their function
Lactase : convert lactose into glucose + glactose
Invertase : convert sucrose into glucose and fructose
Maltase : convert maltose into 2glucose
Emulsion: convert cellulose into n glucose
Urease : convert urea into carbon dioxide and water

Properties of enzymes
Enzymes are required only in small amounts.
They are highly specific.
Enzymes are efficient catalyst: they speed up reaction.
They work at optimum pH, at optimum temperature.
Their mechanism is controlled by various mechanisms and stopped by various organic and inorganic compounds.
The action of enzymes follows lock and key mechanism .however enzyme action is inhibited by certain organic molecules
called inhibitors.

Mechanism of enzymes
Enzymes are needed only in small quantities for the progress of a reaction. Similar to the action of chemical catalysts,
enzymes are said to reduce the magnitude of activation energy.

Vitamins
They are the chemical substances which are needed in small amounts for the growth of human beings.
They can’t be synthesized in our body therefore need to taken from outsource.
Their deficiency can cause one or other type of disease.

Classification of Vitamins:
Vitamins are typically classified into two groups based on their solubility in fat or water – fat-soluble vitamins and water-
soluble vitamins. Fat-soluble vitamins are soluble in fats or oils.
EX: Vitamins A, D, E and K

On the other hand, water soluble vitamins are soluble in water.

EX: B group vitamins and vitamin C
Fat soluble vitamins

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Vitamin A or Retinol:
It is present in carrots, butter, milk, Fish liver oil etc.
This vitamin is necessary for a clear vision. The deficiency of vitamin A leads to xerophthalmia.
Vitamin D or Calciferol
It is produced when skin is exposed to sunlight.
Food sources of vitamin D include fish and egg yolk.
This vitamin is required for bone growth and calcium metabolism.
Vitamin D deficiency leads to rickets In adults, this is called osteomalacia.
Vitamin E
Dietary sources of vitamin E include vegetable oils and cereal grains.
Vitamin E deficiency leads to more fragile red blood cells and muscular weakness.
Vitamin K
Green leafy vegetables are good dietary sources of vitamin K.
Vitamin K deficiency leads to slower blood clotting.
Water soluble vitamins
Vitamin C (or) ascorbic acid:
Dietary sources of vitamin C include citrus fruits, amla and green leafy vegetables.
This vitamin is required for the synthesis of collagen
It’s deficiency causes scurvy.

B group vitamins
They are found in meat products, whole grains, milk and yeast.
They are essential for metabolism and the proper utilisation of energy sources like carbohydrates, proteins and fats.
B group vitamins include vitamin B1, vitamin B2, vitamin B6 and vitamin B12.
Vitamin B1 or thiamine
The richest source of this vitamin is yeast and the outer layers of cereals like rice, wheat and millets. A deficiency of this
vitamin causes beriberi.
Vitamin B2 or riboflavin
It is mostly found in milk and milk products, eggs, liver, green leafy vegetables, pulses, wheat ... and so on. Insufficient
vitamin B2 leads to cheilosis.
Vitamin B6 or pyridoxine
It is found in meat, liver, egg yolk, cereals, grains and vegetables.
Its deficiency causes convulsions.
Vitamin B12 or cobalamine
It is found in meat, fish egg and curd.
Its deficiency leads to pernicious anaemia, that is, RBC deficient in haemoglobin.

Hormones
Hormones are biomolecules which are produced in the ductless (endocrine) glands and are carried to different parts of
the body by the blood stream where they control various metabolic processes. These are required in minute quantites
and unlike fats and carbohydrates these are not stored in the body but are continuously produced.
Steroidal Hormones
e.g., estrogens and androgens (testosterones).

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glucocorticoids control the carbohydrate metabolism, modulate inflammatory reactions, and are involved in reactions to
stress.
Testosterone is the major sex hormone produced in males. It is responsible for development of secondary male
characteristics (deep voice, facial hair, general physical constitution.
estradiol is the main female sex hormone. It is responsible for development of secondary female characteristics and
participates in the control of menstrual cycle. Progesterone is responsible for preparing the uterus for implantation of
fertilised egg.
Poly peptide hormones
for example insulin and endorphins
amino acid derivatives
epinephrine and norepinephrine

Functions of hormones
They help to maintain the balance of biological activities in the body.
The role of insulin in keeping the blood glucose level within the narrow limit is an example of this function. Insulin is
released in response to the rapid rise in blood glucose level. On the other hand hormone glucagon tends to increase the
glucose level in the blood. The two hormones together regulate the glucose level in the blood.
Epinephrine and norepinephrine mediate responses to external stimuli.
Functions of hormones
Growth hormones and sex hormones play role in growth and development.
Thyroxine produced in the thyroid gland is an iodinated derivative of amino acid tyrosine. Abnormally low level of
thyroxine leads to hypothyroidism which is characterised by lethargyness and obesity. Increased level of thyroxine
causes hyperthyroidism. Low level of iodine in the diet may lead to hypothyroidism and enlargement of the thyroid
gland. This condition is largely being controlled by adding sodium iodide to commercial table salt

NUCLEIC ACID
Nucleus is present in every cell of living organisms. Nucleus has acidic properties and hence it was named as nucleic acid.
It is the substance of heredity. Nucleotide is the structural unit of nucleic acid.

Components of nucleic acid

Sugar: It has deoxyribose sugar in DNA and ribose sugar in RNA. It is pentagonal ring having five carbon atoms.
Phosphate group: it has three active –OH groups of which two groups are involved in the formation of strand.
Nitrogen base: These are cyclic compound named as adenine (A) and guanine (G) called purines and are double ring
compounds, whereas thymine (T), cytosine (C), and uracil (U) are called as pyrimidines and are single ring compounds.

1. Sugars in DNA and RNA

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Nitrogen bases as purines and pyrimidines

Phosphate group

Nucleoside
Nucleoside contains only two basic components of nucleic acids (a pentose sugar and a nitrogenous base). During their
formation, 1- position of pyrimidine or 9 – position of purine moiety is linked to C1 of sugar (ribose or deoxyribose) by
glycosidic bond.
Base + Sugar = Nucleoside

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Base + Sugar = Nucleoside

Structure of nucleotide
When nucleoside is linked to phosphoric acid at 5′-position of sugar, we get nucleotide.
Base + sugar + phosphate group = nucleotide

Primary structure of DNA

The sequence in which the four nitrogen bases are attached to the sugar phosphate backbone of a DNA strand is called
the primary structure of DNA.

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Secondary structure of DNA
DNA forms a secondary structure in the form of a double-stranded helix, like a twisted ladder. The two strands of DNA
are held together by hydrogen bonds between specific pairs of bases. Adenosine always pairs with thymine. Cytosine
always pairs with guanine. The strands are said to be complementary to each other. The complementary strands run in
opposite directions. 2hydrogen bonds are formed when adenine pairs up with thymine. When a guanine base pairs with
cytosine, 3 hydrogen bonds form between the bases.

Structure of DNA

Structure of RNA
Structure of RNA is similar to DNA except that it is a single strand structure.
It consist of: Ribose sugar, Nitrogenous base, Purines: adenine and guanine, Pyrimidines: cytosine and uracil, A
phosphate group
It has a single strand helical structure
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There are three important types of RNA in living systems:
1. Messenger RNA carries genetic information from DNA to ribosomes for the synthesis of proteins.
2. Transfer RNA brings amino acids to the messenger RNA.
3. Ribosomal RNA is the RNA component of the ribosome where proteins are synthesised in the cell.

Functions of nucleic acids

1. Replication
Process by which a single DNA molecule produces two identical copies of itself is called replication. Replication of DNA is
an enzyme catalyzed process. In this process, two strands of DNA helix unwind and each strand serves as a template or
pattern for the synthesis of a new strand. Newly synthesized complementary strand is an exact copy of the original DNA.
In this way hereditary characteristics are transmitted from one cell to another
Replication of DNA

Protein synthesis
The specific information coded on DNA has to be translated and expressed in the form of synthesis of specific proteins
which performs various functions in the cell. This synthesis is done in two steps:
Transcription and translation

(i) Transcription
It is the process of synthesis of RNA (mRNA) by using DNA as template. This process is similar to replication process.
(ii) Translation
It is the process of synthesis of protein. This process is directed by mRNA in the cytoplasm of cell with the help of tRNA
(transfer RNA) and ribosomal particles (RNA – protein complex).
Genetic Code
Segment of DNA is called gene and each triplet of nucleotides is called a codon that specifies one amino acid. This
relationship between nucleotide triplets and amino acids is called genetic code.
Revise the chapter

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