CBSE Class 11 Biology Notes Chapter 9: In CBSE Class 11 Biology Notes Chapter 9 about

Biomolecules, you learn about the important molecules that make life possible. These
molecules, like carbohydrates, lipids, proteins, and nucleic acids, are essential for many
functions in living things.

By studying these biomolecules, you get a better understanding of how living organisms work
on a molecular level. The chapter explains these molecules in simple terms, making it easier for
you to grasp their roles and importance in biology.

CBSE Class 11 Biology Notes Chapter 9 Biomolecules

PDF
You can access the CBSE Class 11 Biology Notes Chapter 9 Biomolecules PDF through the link
provided below. This document contains valuable information about biomolecules, which are
essential for life processes.

It covers various topics such as carbohydrates, proteins, lipids, and nucleic acids, explaining
their structures, functions, and significance in living organisms. Whether you're a student or
someone interested in biology, this PDF will help you understand the basics of biomolecules and
their role in biological systems.

CBSE Class 11 Biology Notes Chapter 9 Biomolecules PDF

CBSE Class 11 Biology Notes Chapter 9 Biomolecules

Below, you'll find the solutions to CBSE Class 11 Biology Notes Chapter 9 Biomolecules. These
solutions cover various questions and exercises related to the chapter, helping you understand
the concepts of biomolecules effectively.

By going through these solutions, you can clarify your doubts, reinforce your understanding, and
prepare well for exams. Whether you're a student studying for exams or someone interested in
learning about biomolecules, these solutions will be beneficial in enhancing your knowledge and
problem-solving skills.

Biomolecules
Biomolecules are crucial organic compounds produced by living organisms, serving essential
functions and forming the foundation of life itself. These molecules consist of carbon, nitrogen,
hydrogen, phosphorus, oxygen, and sulfur. Among the various types of biomolecules, four are
particularly common: proteins, carbohydrates, nucleic acids, and lipids. Each of these
biomolecules plays a distinct role in biological processes, contributing to the overall functioning
and structure of living organisms.

Analysis of chemical composition

When analyzing the chemical composition of living tissues, different methods are employed
based on whether the compounds being studied are organic or inorganic. For organic
compounds, such as proteins, nucleic acids, and carbohydrates, the tissues are treated with
trichloroacetic acid. This treatment involves grinding the tissues to create a slurry, which aids in
breaking down the organic matter for analysis.

On the other hand, when analyzing the inorganic chemical composition, such as minerals and
metals, the tissues are burned to form ashes. This process involves heating a sample of tissue
until it combusts completely, leaving behind only the inorganic components as ash. These
methods help scientists understand the chemical makeup of living tissues and provide valuable
insights into their biological functions.

Proteins
In living organisms, there are crucial substances known as proteins, which are a type of
nitrogenous organic compounds made up of long chains of amino acids. Amino acids serve as
the building blocks of proteins, and there are approximately 22 different types found in nature,
consisting of hydrogen, carbon, oxygen, and nitrogen. Each amino acid has an amino group, a
hydrogen atom, a carboxyl group, and a unique side chain bonded to the alpha-carbon.

When dissolved in water, amino acids exist as dipolar ions or zwitterions, capable of either
donating or accepting protons. They exhibit optical activity, meaning they can rotate polarized
light, except for glycine, as they contain a chiral carbon, which is a carbon atom with four
different substituents.

Structure of amino acid

Amino acids can combine to form peptides, with two amino acids creating a dipeptide, three
forming a tripeptide, and 12 to 20 linking to form an oligopeptide chain. When numerous amino
acids join together, they create polypeptides. The first amino acid in a polypeptide chain is
called the N terminal or amino-terminal, while the last one is termed the C terminal or
carboxyl-terminal.

Formation of peptide bond

Proteins exhibit four levels of organization, each contributing to their overall structure and
function:

Primary Structure: This level refers to the linear sequence of amino acids linked together by
peptide bonds.

Secondary Structure: At this stage, the protein begins to fold into more complex shapes,
typically forming alpha-helices or beta-sheets. These structures are stabilized by hydrogen
bonds between the carbonyl and amino groups along the polypeptide backbone.
Tertiary Structure: This level involves the three-dimensional arrangement of the entire protein
molecule, including interactions between amino acid side chains. Stabilizing forces such as
hydrophobic interactions, hydrogen bonds, electrostatic interactions, van der Waals forces, and
covalent bonds help maintain the structure.

Quaternary Structure: Some proteins consist of multiple polypeptide chains that come together
to form a functional protein complex. The interactions between these individual chains, such as
hydrophobic interactions and hydrogen bonds, contribute to the quaternary structure. Examples
include hemoglobin, which is composed of four subunits.

Levels of protein organization

Proteins can also be classified into two main categories based on their shapes and solubility:

● Fibrous Proteins: These proteins have an elongated, rod-like shape and are insoluble
in water. They primarily serve structural and protective roles in the body.
● Globular Proteins: These proteins have a more spherical shape and are soluble in
water. They perform a wide range of functions, including enzymatic activity, transport,
and immune response.

Nucleic acids
Nucleic acids, discovered by Friedrich Miescher, are another essential class of biomolecules.
There are two main types of nucleic acids: deoxyribonucleic acid (DNA) and ribonucleic acid
(RNA). Nucleic acids are composed of nucleotides, which consist of three components: a
nitrogenous base, a five-carbon sugar (deoxyribose in DNA and ribose in RNA), and a
phosphate group.

Structure of nucleotide
The nitrogenous bases found in nucleic acids are aromatic molecules with a heterocyclic
structure. There are two main types of nucleic acids: purines and pyrimidines.

Purines include adenine and guanine, while pyrimidines include thymine (in DNA), cytosine, and
uracil (in RNA).

DNA, or deoxyribonucleic acid, contains deoxyribose, a 5-carbon sugar, while RNA, or

ribonucleic acid, contains ribose. When a nucleoside (which consists of a nitrogenous base and
a sugar) is combined with a phosphate group, it forms a nucleotide.

Structure of Double-Stranded DNA

There are two main types of DNA structures:

B DNA:

● The long polynucleotide strands coil around an axis.

● The two strands are arranged in an antiparallel manner, meaning they run in opposite
directions.
● Adenine nucleoside base pairs with thymine, while guanine base pairs with cytosine.
● Adenine and thymine are held together by two hydrogen bonds, while guanine and
cytosine are held together by three hydrogen bonds.

Z DNA:

● This DNA structure is thinner compared to B DNA.

● The purine and pyrimidine bases are arranged alternately.
● The DNA has a high salt concentration to stabilize its structure.
Denaturation of DNA occurs when the two strands separate due to exposure to varying pH,
temperature, etc. To restore the original DNA structure, denaturants like pH and temperature
need to be removed, a process known as renaturation or annealing.

RNA
RNA, or ribonucleic acid, is single-stranded and found in various forms within the cell:

(i) Messenger RNA (mRNA): Carries genetic information from DNA to the next generation in the
form of codons (three nucleotides form a codon), aiding in protein synthesis.

(ii) Transfer RNA (tRNA): Facilitates protein synthesis by interacting between the language of
nucleic acid and protein, located in the cytoplasm.

(iii) Ribosomal RNA (rRNA): Constitutes ribosomes, crucial for protein synthesis in both
eukaryotes and prokaryotes.

Carbohydrates
Carbohydrates are organic compounds composed of carbon, hydrogen, and oxygen, including
polyhydroxy aldehydes or polyhydroxy ketones. Among them, monosaccharides like glucose
are the simplest carbohydrates. Disaccharides consist of two monosaccharides joined together,
while oligosaccharides are formed by polymerizing 2 to 10 units of monosaccharides.
Polysaccharides, on the other hand, are formed when hundreds to thousands of
monosaccharides are joined together. Monosaccharides with an aldehyde group are aldoses,
while those with a ketone group are ketoses. Trioses are the simplest monosaccharides.

Some common saccharides

Starch, a common saccharide, stores energy in plants. It is composed of several units of

glucose and has a branched structure. Starch comprises two different polymers: amylose and
amylopectin. Amylose is an unbranched polymer of glucose units, while amylopectin consists of
branched polymer chains of glucose units.
Structure of starch

In animals, energy is stored in the form of glycogen, mainly in muscle and liver tissues. Similar
to starch, glycogen consists of two different polymers: amylose and amylopectin. It has a highly
branched structure, as depicted in Fig. 9.

Cellulose, another polysaccharide found in plant cells, as a structural component. It is

composed of unbranched polymer chains of glucose units, providing strength and rigidity to
plant cells.

Chitin is a linear polysaccharide found in the exoskeleton of insects and crustaceans. It is

composed of N-acetyl-D-glucosamine residues.

Reducing sugars, such as monosaccharides, have the ability to reduce ferric or cupric ions. In
contrast, non-reducing sugars like sucrose lack this ability.

Lipids
Lipids are compounds that are poorly or completely insoluble in water but soluble in non-polar
solvents like chloroform, ether, or benzene.

Biological Functions of Lipids

Lipids serve several important biological functions:

Energy Storage: Lipids are a primary storage form of energy in organisms. They can be stored
in adipose tissue and mobilized when energy is needed, providing a long-term energy reserve.

Structural Component of Membranes: Lipids, particularly phospholipids, are essential

components of cell membranes. They form the lipid bilayer, which provides structural integrity to
cell membranes and regulates the passage of molecules in and out of cells.

Protection: In addition to providing structural support, certain lipids act as protective barriers.
For example, lipids found in the skin help prevent water loss and protect against pathogens. In
plants, lipids in the form of waxes provide a protective coating on leaves and stems, reducing
water loss and protecting against pests and pathogens.

Fatty Acids
Fatty acids are fundamental building blocks of lipids, consisting of long hydrocarbon chains with
a carboxyl group at one end. These chains can be either saturated or unsaturated, depending
on the presence of double bonds. Unsaturated fatty acids have one or more double bonds,
which introduce kinks in the chain, resulting in both polar and non-polar ends.

Certain unsaturated fatty acids, like linoleate, are considered essential because mammals
cannot synthesize them and must obtain them from the diet. Conversely, fatty acids that the
body can synthesize are termed non-essential.

Structure of fatty acids

Triacylglycerols, or triglycerides, are another crucial lipid form, composed of fatty acid esters
and glycerol. These molecules are non-polar and hydrophobic, making them excellent for
energy storage due to their high energy density.

Enzymes
Enzymes are vital proteins responsible for catalyzing biochemical reactions in living organisms.
They exhibit various structural levels, including primary, secondary, and tertiary structures, with
an active site that binds to substrate molecules. Enzymes possess several key properties:

● Enzymes are proteins, but not all proteins are enzymes.

● They exhibit specificity towards their substrates, catalyzing specific reactions.
● Enzymes function as catalysts, accelerating chemical reactions without being consumed
in the process.
● There are six major types of enzymes: oxidoreductases, transferases, hydrolases,
lyases, ligases, and isomerases.
● Some enzymes require cofactors or coenzymes for their catalytic activity.
● Cofactors are non-protein molecules that bind to enzymes and activate them, while
coenzymes are transiently bound organic compounds.
● Prosthetic groups are tightly bound organic substances within enzymes.

Various factors influence enzyme activity, including temperature, pH, and substrate
concentration. Enzymes have optimal temperature and pH ranges for activity, and deviations
can lead to inactivation.

Enzyme activity can be modulated by inhibitors, such as competitive inhibitors, which compete
with substrates for binding to the enzyme's active site. For instance, malonate can inhibit
succinate dehydrogenase by competitively binding to its active site.

Benefits of CBSE Class 11 Biology Notes Chapter 9

Biomolecules
● The notes provide a structured overview of the chapter, helping students understand the
key concepts in a systematic manner.
● They cover all essential topics and subtopics included in the CBSE Class 11 Biology
syllabus for Biomolecules, ensuring that students don't miss any important information.
● The notes are written in clear and concise language, making complex concepts easier to
understand and remember.
● Diagrams, figures, and tables are often included in the notes to visually represent key
concepts, aiding in better comprehension and retention.
● They provide a quick reference guide for students to review important points before
exams or quizzes.