Revision Notes for Class 11 Biology

Chapter 9 - Biomolecules
Biomolecules
The living organisms produce an organic molecule called a biomolecule that helps in
performing important functions and acts as a building block of life. They are composed of
carbon, nitrogen, hydrogen, phosphorus, oxygen, and Sulphur. There are four types of
biomolecules that are common, they are proteins, carbohydrates, nucleic acid, and lipids.

Analysis of chemical composition

The living tissues are treated with trichloroacetic acid by grinding them to make a slurry that
is helpful in analyzing the chemical organic compound and its composition while the tissue
should be burned to form ashes in the case of the analysis of the inorganic chemical
composition, a sample of tissue should be burnt to obtain ash.

Primary and Secondary Metabolites:

Primary Metabolites:
 Found in animal tissues.
 Include essential compounds like amino acids, sugars, and lipids.
 Play key roles in normal body functions, growth, and development.

Secondary Metabolites:
 Found mainly in plants, fungi, and microbes.
 Examples include alkaloids, flavonoids, rubber, essential oils, antibiotics, pigments,
and spices.
 Their exact role in the producing organisms is often unknown.
 Many are useful to humans for making medicines, perfumes, and other products.

Class XI Biology www.vedantu.com 1

 Some have ecological importance, helping organisms survive in their environment.

Biomacromolecules:

Molecular Weight:

 Compounds with molecular weights between 18 to 800 daltons (Da) are found in the
acid-soluble pool.

 Compounds with molecular weights above 10,000 Da are found in the acid-insoluble
fraction.

Types of Biomolecules:
 Micromolecules: Small molecules with molecular weights less than 1,000 Da, found
in the acid-soluble pool.
 Macromolecules/Biomacromolecules: Larger molecules are found in the acid-
insoluble fraction, including proteins, nucleic acids, and polysaccharides.

Lipids Exception:
 Lipids, though small (less than 800 Da), are part of the acid-insoluble fraction
because they form structures like cell membranes.
 When tissues are ground, membranes break into vesicles, which are not water-
soluble, making them part of the macromolecular fraction.

Representation of Living Tissue:

 The acid-soluble pool mainly represents the cytoplasmic composition.
 Macromolecules from the cytoplasm and organelles make up the acid-insoluble
fraction.
 Together, these fractions represent the full chemical composition of living tissues.

Class XI Biology www.vedantu.com 2

Abundance of Chemicals:
 Water is the most abundant chemical in living organisms.

Proteins
In living organisms, there are essential substances that are important and belong to any class
of nitrogenous organic compounds having large molecules that are made up of several long
chains of amino acids.
The proteins are composed of amino acids that act as their building blocks. Naturally, around
22 amino acids are found that are made up of hydrogen, carbon, oxygen, and nitrogen. So,
one amino acid is composed of the amino group, hydrogen atom, carboxyl group, and
distinctive side chain that are bonded with the alpha-carbon.

Fig.1. structure of amino acid

Class XI Biology www.vedantu.com 3

The amino acids are present in the form of dipolar ions or zwitterion in solutions when they
get dissolved in the water. They function either as proton donors or proton acceptors.

Fig. 2. Zwitterion

All amino acids are found to rotate along the plane based on the polarized light and are said
to be optically active. They consist of chiral carbon except for glycine. A chiral carbon is one
having four different constituents in a tetrahedral carbon atom.

Two or more amino acids together constitute a peptide and are linked with the help of the
peptide bond that is said to form a dipeptide. A tripeptide is formed when three amino acids
are joined together while an oligopeptide chain is formed when 12 to 20 amino acids are
joined together. When many amino acids are joined together they result in the formation of
polypeptides. The first amino acid in the polypeptide chain is known as the N terminal or
amino-terminal and the last amino acid in the polypeptide chain is known as the C terminal
or carboxyl-terminal.

Class XI Biology www.vedantu.com 4

 Fig. 3. Formation of peptide bond

Protein structure
There are four levels of protein organization in proteins. They are as follows:
(i) Primary structure: This structure of the protein consists of the amino acids sequence
that is joined together by a peptide bond.

(ii) Secondary structure: This stricture is a protein organization having a higher level that
is comprised of the alpha-helix and the beta-sheets. These both are stabilized due to the
presence of hydrogen bonds in between the carbonyl and N-H groups in a polypeptide
backbone.

Class XI Biology www.vedantu.com 5

(iii) Alpha helix: When a polypeptide chain twists, it will form a rigid, rod-like structure that
changes into a helical conformation.

(iv) Beta pleated: The arrangement of two or more polypeptide chain segments that are side
by side then it results in the formation of a sheet, and every chain segment is known as beta-
strand.

(v) Tertiary structures: A three-dimensional structure of protein due to the interaction

between the primary structure and its side chains. To make them stabilized, they required
hydrophobic interactions, hydrogen bonds, electrostatic interactions, van der Waals forces,
and covalent bonds.

Fig. 4. Levels of protein organization

(vi) Quaternary structures: They are made up of two or more polypeptide chains that are
joined together with the help of hydrophobic interactions, hydrogen bonds, electrostatic
interactions, etc. For example, hemoglobin.

(vii) Fibrous and globular proteins

Fibrous proteins are long, rod-shaped molecules that are found to be insoluble in water and
are structural and protective in nature while the globular proteins are water-soluble and are
made up of spherical-shaped molecules.

Class XI Biology www.vedantu.com 6

Nucleic acids
Friedrich Miescher was the first to discover nucleic acid from the nuclei of pus cells. The
nucleic acids are of two types: deoxyribonucleic acids (DNA) and ribonucleic acids (RNA).

In nucleic acid, the nucleosides are the monomeric unit consisting of three constituents: - a
nitrogenous base, a five-carbon sugar, and phosphoric acid.

Fig. 5. Structure of nucleotide

The nitrogenous bases are aromatic molecules having a heterocyclic structure. Basically, two
types of nucleic acids are found, that are purines and pyrimidines.

Class XI Biology www.vedantu.com 7

Purines are of two types- adenine and guanine while pyrimidines are of three types thymine,
cytosine, or uracil.

Fig 6: Structure of purines and pyrimidines

DNA is deoxyribose that constitutes 5- carbon sugar while RNA is ribose. Nucleoside when
present with phosphate is known as the nucleotide.

Enzymes
Enzymes are made up of proteins and consist of various structures like proteins that include
the primary, secondary, and tertiary structures. The enzyme consists of an active site that
helps in binding the substrate molecule. The properties of the enzymes are as follows:
• All enzymes are proteins, but all proteins are not enzymes.

• For each substrate, the enzymes are specific.

Class XI Biology www.vedantu.com 8

• Enzymes function as catalysts.

• During the reaction, the enzymes are not used up.

• They are of six major types: oxidoreductases, transferases, hydrolases, lyases, ligases, and
isomerases.

• For an enzyme to function, some of them require a cofactor and/or a co-enzyme to function.

• Co-factor: They are the non-protein constituents that when binds to an enzyme will make
them catalytically active.

• Co-enzyme: They are the organic compounds that during the course of the reaction will
binds to the enzyme transiently.

• Prosthetic groups: they are the organic substances that are bounded to the enzyme very
tightly.

Figure 12: Enzyme-substrate activity

Class XI Biology www.vedantu.com 9

Factors Affecting the Enzyme Activity
The enzyme activity can be affected due to various factors that include temperature, pH, and
substrate concentration. The optimum temperature needs to be maintained or the high or low
temperature will lead to the inactivation of the enzyme activity. The enzyme activity can be
altered due to deprotonation or protonation.
The molecules such as the inhibitors are responsible for the inactivation of the enzymes.
Competitive inhibitors are the most common type of inhibitors that compete to bind to the
active site of the enzyme against the substrates. For example, with the help of Malonate, the
inhibition of succinate dehydrogenase can be done.

Class XI Biology www.vedantu.com 10