S.N.B.P.

International School ,Morwadi, Pimpri

Subject : Biology Class : XI Name :

Topic : BIOMOLECULES NCERT solutions Roll No :
Prepared by: Ms Durga Bhavani.P Date :
.

1) What are macromolecules? Give examples.

Sol. A macromolecule is a very large molecule formed due to polymerization of
smaller subunits (monomers). They are typically composed of thousands of atoms
or more.The biomolecules with higher molecular weight (more than 10,000
daltons are) known as macromolecules. Example: Proteins and Polysaccharides.

2. Illustrate a glycosidic, peptide and a phosphodiester bond.

Sol. A glycosidic bond is a certain type of functional group that joins a carbohydrate
(sugar) molecule to another group, which may or may not be another
carbohydrate.

A peptide bond (amide bond) is a chemical bond formed between two molecules
when the carboxyl group of one molecule reacts with the amine group of the other
molecule, thereby releasing a molecule of water (H2O). This is a dehydration
synthesis reaction (also known as a condensation reaction), and usually occurs
between amino acids. The resulting CO-NH bond is called a peptide bond, and
the resulting molecule is an amide. The four-atom functional group -C(= O) NH-
is called an amide group or (in the context of proteins) a peptide group.
Polypeptides and proteins are chains of amino acids held together by peptide
bonds, as is the backbone of PNA. Polyamides, such as nylons and aramids, are
synthetic molecules (polymers) that possess peptide bonds.
 A phosphodiester bond is a group of strong covalent bonds between a phosphate
group and two other molecules over two ester bonds. Phosphodiester bonds are
central to all life on Earth, as they make up the backbone of the strands of DNA.
In DNA and RNA, the phosphodiester bond is the linkage between the 3' carbon
atom of one sugar molecule and the 5' carbon of another, deoxyribose in DNA
and ribose in RNA.

3. What is meant by tertiary structure of proteins?

Sol. Tertiary structure. The overall shape of a protein molecule-- the spatial
relationship of the secondary structures to one another is called tertiary structure
of proteins. Tertiary structure is generally stabilized by non local interactions,
most commonly the formation of a hydrophobic core, but also through salt
bridges, hydrogen bonds, disulfide bonds, and even post translational
modifications. The term "Tertiary structure" is often used as synonymous with the
term fold. The tertiary structure is what controls the basic function of the protein.
The tertiary structure will have a single polypeptide chain "backbone" with one or
more protein secondary structures, the protein domains. Amino acid side chains
may interact and bond in a number of ways. The interactions and bonds of side
chains within a particular protein determine its tertiary structure.

4. Find and write down structures of 10 interesting small molecular weight biomolecules. Find
if there is any industry that manufactures the compounds by isolation. Find out who are the
buyers.

Sol. Small Molecular Weight Biomolecules: Lactic acid, simple sugars, pentoses,
hexoses, lipids, fatty acids, amino acids and nucleotides.
Sugar and cotton, as well as biotechnological industries, manufactures the
 compounds by isolation.

5. Proteins have a primary structure. If you are given a method to know which amino acid is at
either of the two termini (ends) of a protein, can you connect this information to purity or
homogeneity of a protein?

Sol. Yes. The sequence of amino acids or positional information in a protein which is a
first amino acid, which is second and so on, is known as the primary structure of a
protein.

Primary structure of a portion of a hypothetical protein. N and C refer to the two

termini of every protein. Single letter codes and three-letter abbreviations for
amino acids are also indicated.
The difference in one amino acid will make the protein different from each other.
The sequencing of a complete protein by sangers or Edman technique can tell us
about the purity of a protein.
6. Find out and make a list of proteins used as therapeutic agents. Find. other applications of
proteins (e.g., Cosmetics etc.)

Sol. Therapeutic Agents:

Contraceptive pills: As they are mostly hormones, so they are made up of
proteins.
Nutritional Supplements: Many brands are available as protein
supplements.Example: Protinex
Other Uses:
Chicken cubes are used in making soups and dishes.

7. Explain the composition of triglyceride.

Sol. Triglycerides are the predominant component of most food fats and oils. The
minor components include mono- and diglycerides, free fatty acids, phosphatides,
sterols, fatty alcohols, fat-soluble vitamins, and other substances. A triglyceride is
composed of glycerol and three fatty acids. Ester bonds form between each fatty
acid and the glycerol molecule. General structure of a triglyceride is shown
below---
Chemical formula
RCOO - CH2CH(-OOCR) CH2 - OOCR''
where R, R', and R" are longer alkyl chains. The three fatty acids RCOOH,
R'COOH and R"COOH can be or same.
Chain lengths of the fatty acids in naturally occurring triglycerides can be of
varying lengths, but chains consisting of 16, 18 and 20 carbons are the most
common. Natural fatty acids found in plants and animals are typically composed
only of even number of carbon atoms due to the way they are biosynthesized
from acetyl CoA. Bacteria, however, possess the ability to synthesize odd - and
branched-chain fatty acids. Consequently, ruminant animal fat contains odd-
numbered fatty acids, such as 15, due to the action of bacteria in the rumen.

8. Can you describe what happens when milk is converted into curd or yoghurt from your
understanding of proteins?

Sol. Milk is converted into curd or yogurt by the process of fermentation. Milk
consists of globular proteins. During fermentation, the milk sugar (lactose)
produces lactic acid. Lactic acid acts on the globular proteins present in the milk
and denatures them. This denaturation destroys the tertiary and quaternary
structures of proteins and the globular proteins are converted into fibrous proteins
thus giving a thick texture to the milk due to coagulation of the proteins.is also
called fermentation.
9. Can you attempt building models of biomolecules using commercially available atomic
models (Ball and Stick models).

Sol. Yes, we can make models of biomolecules using commercially available atomic
models.

10. Attempt titrating an amino acid against a weak base and discover the number of
dissociating (ionizable) functional groups in the amino acid.

Sol. On titrating against a weak base the amino acid ionizes into following functional
groups.

• -NH2 (amine group)

• -COOH (carboxyl group)

11. Draw the structure of the amino acid, alanine.

Sol. Alanine: It is a neutral amino acid because it possesses one amino group and one
carboxyl group (mono-amino mono carboxylic acid).

12. What are gums made of ? Is Fevicol different?

Sol. Gums are polysaccharides of natural origin, capable of causing a large viscosity
increase in solution, even at small concentrations.
Fevicol is a synthetic glue. These adhesives are a mixture of ingredients (typically
polymers) dissolved in a solvent. As the solvent evaporates, the adhesive hardens.
Depending on the chemical composition of the adhesive, they will adhere to
different materials to greater or lesser degree. These adhesives are typically weak
and are used for household applications.

13. Find out a qualitative test for proteins, fats and oils, amino acids and test any fruit juice,
saliva, sweat and urine for the same.
Qualitative tests for proteins, amino acids and fats:
Sol.
i. Biuret Test: Biuret test for protein identifies the presence of protein by producing
the violet colour of the solution. Biuret H2NCONHCONH2 reacts with copper ion
in a basic solution and gives violet colour.
 ii. Liebermann-Burchard Test for Cholesterol: This is a mixture of acetic
anhydride and sulphuric acid. This gives a green colour when mixed with
cholesterol.
iii. Grease Test for Oil: Certain oils give a translucent stain on clothes. This test can
be used to show presence of fat in vegetable oils.
These tests can be performed to check presence of proteins, amino acids and fat in
any of the fluid mentioned in the question.

14. Find out how much cellulose is made by all the plants in the biosphere and compare it with
how much of paper is manufactured by man and hence what is the consumption of plant
material by man annually. What is loss of vegetation?

Sol. According to 2006 report from the UN, forests store about 312 billion tons of
carbon in their biomass alone. If you add to that the carbon in deadwood, litter,
and forest soil, the figure increases to about 1.1 trillion tons. The UN assessment
also shows that the destruction of forests add almost 2.2 billion tons of carbon to
the atmosphere each year, the equivalent of what the U.S. emits annually. Many
climate experts believe that the preservation and restoration of forests offers one
of the least expensive and best ways to fight against climate change.
Although it is difficult to get exact data about the quantum of cellulose produced
by plants, but above information can give some idea. About 10% of cellulose is
used in paper making. The percentage is less but wrong practice of cutting wood
and re-plantation makes the problem complicated. Usually older trees are cut for
large quantity of cellulose and re-plantation is limited to selected species of
plants.
Selected species disturbs the biodiversity as it leads to monoculture. Added to this
is the problem of effluents coming out of a paper factory and the problem further
aggravates.

15. Describe the important properties of enzymes.

Sol. Properties of enzymes are as follows:

- Enzymes are proteinaceous in nature. Enzymatic proteins are commonly
globular in nature.
- Lowering the energy of the transition state
- Enzymes are generally hydrophobic colloids.
- Reducing the reaction entropy change
- Increases in temperatures speed up reactions
- Unique enzyme for unique substance
- Small quantity is enough to facilitate faster biochemical change.
- Enzymes generally have high molecular weight.
- Each enzyme has got specific turnover number.