Revision Notes On CBSE Class 12 Chemistry Chapter 14 - Biomolecules Free PDF
Revision Notes On CBSE Class 12 Chemistry Chapter 14 - Biomolecules Free PDF
Revision Notes On CBSE Class 12 Chemistry Chapter 14 - Biomolecules Free PDF
Class 12 Chemistry
Chapter 14 Biomolecules
1. Introduction
Biomolecules are complex organic compounds that govern the common activities
of living organisms. Carbohydrates, proteins, nucleic acids, lipids, and other
complex biomolecules make up living systems. Furthermore, simple molecules
such as vitamins and mineral salts play an important role in the functions of
organisms.
2. CARBOHYDRATES
Plants are the primary producers of carbohydrates, which comprise a large group of
naturally occurring organic compounds. Cane sugar, glucose, starch, and other
common examples The majority of them have the general formula C x H2 y O y and
were thought to be carbon hydrates, hence the name carbohydrate. The molecular
formula of glucose C6H12O6 , for example, fits into this general formula,
C6 H2O 6. However, not all of the compounds that fit into this formula are
carbohydrates. Rhamnose, C6H12O5 , is a carbohydrate, but it does not fall under
this definition. Carbohydrates can be defined chemically as optically active
polyhydroxy aldehydes or ketones, or compounds that produce such units upon
hydrolysis. Some carbohydrates with a sweet taste are also known as sugars.
Sucrose is the most common sugar found in our homes, whereas lactose is the
sugar found in milk.
2.1.1 Monosaccharides
Monosaccharides are further classified based on the number of carbon atoms and
the functional group they contain. When a monosaccharide contains an aldehyde
group, it is referred to as an aldose, and when it contains a keto group, it is referred
to as a ketose. As shown by the examples, the number of carbon atoms constituting
the monosaccharide is also introduced in the name.
2.1.2 Oligosaccharides
2.1.3 Polysaccharides
Nonreducing sugars, such as sucrose, are formed when the reducing groups of
monosaccharides, such as aldehydic or ketonic groups, are bonded in
disaccharides. Reducing sugars, on the other hand, are sugars that have these
functional groups free, such as maltose and lactose.
3. GLUCOSE (ALDOHEXOSE)
When sucrose is boiled in alcoholic solution with dilute HCl or H2SO4 , glucose and
fructose are obtained in equal amounts.
H
C12H22O11 H 2O
C6H12O6 C6H12O6
Sucrose Glucose Fructose
H
C6 H10O5 nH2O nC6 H12O6
393 K,2-3 atm
Starch or cellulose Glucose
3.2 Reactions
(A) Oxidation
Note: Reduction with HI yields n-hexane, demonstrating that all six carbons of
glucose are arranged in a straight chain.
(E) Acetylation
D(+)-glucose is the correct name for glucose. The letter ‘D' before the name of
glucose represents the configuration, whereas the letter ‘(+)' represents the
molecule's dextrorotatory nature. It should be noted that the letters 'D' and 'L' have
no bearing on the compound's optical activity. The following is a definition of D–
and L– notations. The letters 'D' or 'L' before the name of any compound indicate
the stereoisomer's relative configuration. This refers to their affinity for a specific
isomer of glyceraldehyde. Glyceraldehyde has one asymmetric carbon atom and
comes in two enantiomeric forms, as shown.
Glucose has been discovered to exist in two different crystalline forms, which are
known as and . The -form of glucose (m.p. 419 K) is obtained by
crystallisation from a concentrated glucose solution at 303 K, whereas the . -form
(m.p. 423) is obtained by crystallisation from a hot and saturated aqueous solution
at 371 K. In aqueous solution, both -D-glucose and -D-glucose undergo
mutarotation. Although the crystalline forms of - and -D (+)-glucose are quite
stable in aqueous solution, each form gradually transforms into an equilibrium
mixture of the two.
This is demonstrated by the fact that the specific rotation of a freshly prepared
aqueous solution of -D(+)-glucose decreases with time from +111° to +52.5°,
whereas that of -D(+)-glucose increases from +19.2° to 52.5°. Thus, mutarotation
refers to the spontaneous change in specific rotation of an optically active
compound with time to an equilibrium value. It was discovered that glucose forms
a six-membered ring, with –OH at C-5 playing a role in ring formation. This
explains the lack of a –CHO group as well as the presence of glucose in two forms,
as shown below. These two cyclic forms coexist with an open chain structure.
A ring of 6 atoms (5 ‘C' and 1 ‘O') is drawn, with the ‘O' atom in the upper right
hand corner, as shown below.
4. FRUCTOSE (KETOHEXOSE)
Fructose has the molecular formula C6H12O6 , and based on its reactions, it was
discovered to have a ketonic functional group at carbon number 2 and six carbons
in a straight chain, just like glucose. It is a laevorotatory compound from the D-
series. D-(–)-fructose is the correct spelling. Its open chain structure is depicted
below.
Haworth structures are used to represent the cyclic structures of two anomers of
fructose.
Property Glucose
Molecular formula C6 H12O6
6. DISACCHARIDES
6.1 Sucrose
C12 H 22O11 H 2O
C6 H12O6 C6 H12O6
Sucrose D- -Glucose D- -Fructose
D 66.5 D 52.5 D 92.4
Thus, hydrolysis of sucrose causes a change in the sign of rotation, from dextro (+)
to laevo (–), and the product is known as invert sugar, and the phenomenon is
known as sugar inversion.
6.2 Maltose
6.3 Lactose
It is more commonly known as milk sugar since this disaccharide is found in milk.
It is composed of -D-galactose and -D-glucose. Fischer projections of -D-
Glucose and -D-Galactose are drawn below:
7.1 Starch
7.3 Glycogen
7.4 Summary
Note:
8. PROTEINS
Protein is derived from the Greek word "proteios," which means "primary" or "of
primary importance." Proteins are all polymers of -amino acids.
Amino acids have both amino (–NH2) and carboxyl (–COOH) functional groups.
The amino acids are classified as , , , and so on based on the relative position
of the amino group with respect to the carboxyl group. When proteins are
hydrolyzed, only -amino acids are produced. They may also contain other
functional groups.
All -amino acids have innocuous names that usually reflect the compound's or its
source's property. Glycine is named after its sweet taste (glykos means sweet in
Greek), and tyrosine was first obtained from cheese (tyros means cheese in Greek).
The relative number of amino and carboxyl groups in an amino acid molecule
determines whether it is acidic, basic, or neutral.
Non-essential amino acids are amino acids that can be synthesized in the body.
Essential amino acids, on the other hand, are those that cannot be synthesized in
the body and must be obtained through diet.
Amino acids are crystalline, colorless solids. These are water-soluble, high-
melting-point solids that act more like salts than simple amines or carboxylic acids.
The presence of both acidic (carboxyl group) and basic (amino group) groups in
the same molecule causes this behavior.
Except for glycine, all other naturally occurring -amino acids are optically active
due to the asymmetry of the -carbon atom.
These are available in both 'D' and 'L' forms. The majority of naturally occurring
amino acids have an L-configuration. The –NH2 group on the left side is used to
represent L-amino acids.
An amino acid's isoelectric point (pI) is the pH at which it has no net charge. In
other words, it is the pH at which the negative charge on an amino acid exactly
balances the positive charge. pI (isoelectric point) = pH at which no net charge
exists. The pI of an amino acid with no ionizable side chain, such as alanine, is
halfway between its two pKa values. This is due to the fact that at pH = 2.34, half
of the molecules have a negatively charged carboxyl group and half have an
uncharged carboxyl group, and at pH = 9.69, half of the molecules have a
positively charged amino group and half have an uncharged amino group. As the
pH rises from 2.34, more molecules' carboxyl groups become negatively charged;
as the pH falls from 9.69, more molecules' amino groups become positively
charged.
The Peptide Bond Proteins are polymers of -amino acids that are linked together
by peptide bonds or peptide linkage. Peptide linkage is chemically defined as an
amide formed between the – COOH group and the –NH2 group.
The reaction between two molecules of similar or different amino acids is initiated
by the combination of one molecule's amino group with the carboxyl group of the
other. This causes the removal of a water molecule and the formation of a peptide
bond –CO–NH–.
A fibrelike structure is formed when polypeptide chains run parallel and are held
together by hydrogen and disulphide bonds. In general, such proteins are insoluble
in water.
Keratin (found in hair, wool, and silk) and myosin (found in muscles) are two
common examples.
This structure is formed when polypeptide chains coil around to form a spherical
shape. These are usually water soluble. Insulin and albumin are two common
globular proteins. Protein structure and shape can be studied at four different
levels: primary, secondary, tertiary, and quaternary.
A protein's secondary structure is the shape in which a long polypeptide chain can
exist. They have been discovered to exist in two different structures: -helix and
-pleated sheet. These structures form as a result of the regular folding of the
The –NH group of each amino acid residue is hydrogen bonded to the C = O of an
adjacent turn of the helix in one of the most common ways in which a
polypeptide chain forms all possible hydrogen bonds by twisting into a right
handed screw (helix).
All peptide chains in -structure are stretched to nearly maximum extension and
then laid side by side, held together by intermolecular hydrogen bonds.
Some proteins are made up of two or more polypeptide chains known as sub-units.
The relationship of subunits to one another is referred to as quaternary structure.
A native protein is a protein found in a biological system that has a distinct three-
dimensional structure and biological activity. When a protein in its native form is
subjected to physical change, such as temperature change, or chemical change,
such as pH change, the hydrogen bonds are disrupted. As a result, globules unfold,
helixes uncoil, and protein loses biological activity. This is referred to as protein
denaturation. A common example of denaturation is the coagulation of egg white
9. NUCLEIC ACIDS
Adenine (A), guanine (G), cytosine (C), and thymine are the four bases found in
DNA (T). The first three bases of RNA are the same as those of DNA, but the
fourth is uracil (U).
10. ENZYMES
11. Vitamins
12. HORMONES
Hormones are biomolecules that are produced in the ductless (endocrine) glands
and transported by the bloodstream to various parts of the body where they control
various metabolic processes. These are required in minute amounts and, unlike fats
and carbohydrates, are not stored in the body but are constantly produced.
When a protein is treated with concentrated HNO3 , it turns yellow. This test is
performed by a protein composed of -amino acids containing a benzene ring,
such as tyrosine, phenylalanine, and others, and the yellow color is caused by
benzene ring nitration. An important example of this test is when concentrated
Millon's reagent is a nitric acid solution of mercurous nitrate and mercuric nitrate
with little nitrous acid. When Millon's reagent is added to an aqueous protein
solution, a white ppt. is formed. All proteins containing phenolic -amino acids,
such as tyrosine, pass this test. As a result, gelatin that does not contain phenolic
-amino acids fails this test.