ISC CHEMISTRY CLASS XII

BIOMOLECULES

The complex organic substances like carbohydrates, proteins etc which combine in a
specific manner to produce living systems and maintain it are called biomolecules.

Carbohydrates

Optically active polyhydroxy aldehydes (aldoses) or ketones (ketoses) or compounds

which on hydrolysis give these units are known as carbohydrates. They are also called
saccharides

(Latin Saccharum = sugar) due to sweet taste of simpler members.

Depending upon their behaviour towards hydrolysis, carbohydrates can be of following

three types

Monosaccharides
These cannot be hydrolysed to simpler molecules and further subdivided into tetroses,
pentoses or hexoses depending upon the number of carbon atoms. These are also
called homopolysaccharides.

 Aldotetroses Erythrose, Threose

 Aldopentoses Xylose, Ribose,
 Aldohexoses Glucose, Galactose,
 Ketohexoses Fructose
All naturally occurring monosaccharides belong to D-series.

Reducing and Non-reducing sugars

Based upon reducing and non-reducing properties, carbohydrates are classified as
reducing and non-reducing sugars. Carbohydrates reducing Fehling reagent or Tollen’s
reagent are termed as reducing carbohydrates. e.g., All monosaccharides and
disaccharides (except sucrose). But carbohydrates which do not reduce such reagents
are known as non-reducing carbohydrates. e.g., sucrose and polysaccharides.

Sugars and Non-sugars

On the basis of their, taste, carbohydrates are classified as sugars and non-sugars. The
monosaccharides and oligosaccharides having sweet taste are collectively known as
sugars. Polysaccharides which are insoluble in water and not sweet in taste, are non-
sugars.

Reactions of glucose
Glucose has one aldehyde group, one primary hydroxyl (-CH2OH) and four secondary
hydroxyl (-CHOH) groups and gives the following reactions:

Glucose reduces ammoniacal silver nitrate solution (Tollen’s reagent) to metallic silver
and also Fehling’S solution or Benedict solution to reddish brown cuprous oxide (Cu2O)
and itself gets oxidised to gluconic acid. This confirms the presence of an aldehydic
group in glucose.
(iv) With mild oxidising agent like bromine water, glucose is oxidised to gluconic acid.
Glucose on oxidation with nitric acid gives saccharic acid.

Cyclic structure of glucose Given by Haworth and Hirst.

Fructose does not reduce Br2 water.

Proteins
Introduction of proteins
o They are high weight polymers.
o They are polyamides that contain C, H, N, O and S.
o Proteins are derived from alpha amino carboxylic acid monomers.
o A simple protein may contain hundred even thousands of amino acid units.
o In living organisms twenty alpha amino acids occur which combine to form
different protein molecules.
Amino acids
o A simple amino acid can be represented as R-CH(NH)2COOH (carboxy group
and amino group is present in it).
o Peptides
o Peptides are condensation products of two or more amino acids.

o
o Two molecules of different amino acids can form two dipeptides.Three molecules
of different amino acids can give six tripeptides.
o Dipeptide has only one peptide bond, tripeptide has two peptide bonds and so
on. Thus, a polypeptide made up of n-amino acids has (n – 1) peptide bonds.

Zwitter Ion:
“A zwitterion is a molecule that has both positive and negative regions of
charge.” In the solid state, amino acids exist as dipolar ions called zwitterions. While
discussing whether a substance is zwitterionic or not, the pH range in which the
information is required must be specified (because a sufficiently alkaline solution will
change the zwitterion to an anion, and a sufficiently acid solution will change it to a
cation).
Some key Characteristics of Zwitterion are;

 They can be formed from compounds like ampholytes which contain both acid
and base groups in their molecules.
 In this type of ions, the charged atoms are usually held together by one or
more covalent bonds.
 Zwitterionic compounds have stable, separated unit electrical charges on atoms.
 These compounds contain quaternary ammonium cations.
Let us further understand the topic by looking at an example of Zwitterion.
Amino acids are the most common example of zwitterions. They are made up of an
ammonium or amino group which contains a positive charge as well as a carboxyl
group which contains a negative charge. The zwitterion form of an amino acid is given
below.

Apart from amino acids, any compound that contains acid and base centres can obtain a
Zwitterion form. Some more examples include tricine, bicine, solid sulfamic acid,
alkaloids like psilocybin amongst others
Isoelectric point
 o Due to the zwitter ion structure, alpha amino acids are high meting crystalline
solids and moderately soluble in water.
o In acidic medium caboxylate ion group act as a base and accepts a proton.
Thus alpha amino acids exist as cations (I) under the influence of electric field.

(zwitter ion )

o In alkaline medium, NH3+groups act as an acid and thus loses a proton.

o Due to this, alpha amino acids exist as anions (III) and thus migrate towards
the anode in the electric field.
o However, at some intermediate value of ph, the concentration of cationic
form (I) and the anionic form (III) become equal.
o Hence, there is no migration in electric field. This pH is known as isoelectric
point.
Polypeptide formation
o The interaction between amino group and carboxyl of amino group give
compounds called peptides.
o The amide group –CONH in each such compound is called peptide linkage.
o Depending upon the number of amino acid, residues per molecule they are
called as dipeptide, tripeptide etc.
o Peptides of molecular weight up to 10,000 are known as polypeptides and
those with higher than 10,000 are called as proteins.
o Each polypeptide chain has a free amino group at one end and a free carboxyl
group at other end.
o They are collectively called as end groups.
o The amino acid unit having –NH2group is called N-terminal end and the
amino acid unit having free –COOH group is called C-terminal end.
 o In this NH-CH-CO is the repeating unit in polypeptide.
Structure of proteins
Proteins have three structures:
o Primary structure
o Secondary structure
o Tertiary structure
On the basis of composition, proteins are of following types :
o Simple proteins
o Conjugated proteins
o Derived proteins
o Fibrous proteins
o Globular proteins
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

Fibrous proteins: They are long and thread like and tend to lie side by side to form
fibers .In some cases, they are held together by hydrogen bonds at many points .these
proteins serves as a chief structural material of animal tissues .
Globular proteins: The molecules of these proteins are folded into compact units and
form spheroid shapes .Intermolecular forces are weak. These proteins are soluble in
water or aqueous solution of acids, bases or salts .Globular proteins make up all
enzymes, hormones ,fibrinogen etc.

DENATURATION OF PROTEINS:

Denaturation implies the destruction of the tertiary structure of a protein molecule and
the formation of random polypeptide chains.
Denaturation of proteins is one of the phenomenons that results in the disturbance of
stability and structure of the protein. The chemistry of proteins has always been
important owing to the abundance of these biomolecules in the living system. The
fundamental blocks of our body structure and their functioning require protein. This
protein is supplied to our body through food products such as pulses, cheese, milk,
meat, nuts, etc.

Nucleic acids
o Nucleic acids are the polymers in which nucleotides are monomers. These are
biomolecules present in nuclei of all living cells in the form of nucleoproteins
.They are also called as polynucleotides .
They help in the role of transmission of hereditary characters and synthesis of proteins.

Each nucleotide consists of 3 parts:

 o A pentose sugar
o A nitrogenous base
o A phosphate group
o The nitrogenous base and a pentose sugar are called as nucleoside.
Nitrogenous bases are of two types: Purines and Pyrimidines
o Purines: adenine and guanine
o Pyrimidines: cytosine , thiamine and uracil

Please note that Purines and Pyrimidines are linked together by hydrogen bonds
o Adenine always bond with thiamine by double bond or vice versa.
o Cytosine always pairs with guanine by triple bond or vice versa.
Types of nucleic acids
o Deoxyribonucleic acid (DNA)
o Ribonucleic acid (RNA)
DNA
 o It occurs in nucleus of cell. It has double stranded helical structure
DNA contains:
o Deoxyribose sugar
o Nitrogenous bases :
o Purines (adenine and guanine ), Pyrimidines (thiamine and cytosine )
o A phosphate group
o It can undergo replication
o It helps in transfer of genetic information from parents to offspring
RNA
o It occurs in cytoplasm of cell
It consist of:
o Ribose sugar
o Nitrogenous base
o Purines: adenine and guanine
o Pyrimidines: cytosine and uracil
o A phosphate group
o It has a single strand helical structure
o It doesn’t undergo replication
o It controls synthesis of proteins