Chapter

Biomolecules
9
Directions: In the following questions, a statement 8. Assertion: Amino acids are known as a-amino acids.
of assertion is followed by a statement of reason. Reason : Amino acids are organic compounds
Mark the correct choice as: containing an amino group and carboxylic group
as substituent on the a-carbon.
(a) If both Assertion and Reason are true and 9. Assertion: Proteins are a heteropolymer.
Reason is the correct explanation of Assertion. Reason : Dietary proteins are the source of non-
(b) If both Assertion and Reason are true but Reason essential amino acids.
is not the correct explanation of Assertion. 10. Assertion: The long protein chain folds upon
(c) If Assertion is true but Reason is false. itself like a hollow ball giving rise to the tertiary
(d) If both Assertion and Reason are false. structure.
Reason : Tertiary structure gives a 3-dimensional
1. Assertion: The living state is a equilibrium view of a protein.
steady state to be able to perform work. 11. Assertion: Amino acids are amphoteric in their
Reason : Living process is a constant effort to function.
prevent falling into non-equilibrium. Reason: All amino acids are necessary for our
2. Assertion: Living organisms have more body.
nitrogen and oxygen per unit mass than 12. Assertion: Nine amino acids are essential amino
inanimate objects (e.g., earth crust). acids for human.
Reason: Living organisms have more Ca, Mg, Reason: They are essential for human health.
Na in them than inanimate object. 13. Assertion : Vegetable oils are fats which are
3. Assertion: In living system, all the metabolic present in plant cells in soluble form.
conversions are aided by catalyst. Reason : Vegetable oils occur only in cells of embryo.
Reason: The catalyst which hasten the rate of a 14. Assertion : Unsaturated fats are more reactive
given metabolic conversion are not proteins. compared with the saturated fats.
4. Assertion: Secondary metabolites are produced Reason : Unsaturated fats have only single
in small quantities and their extraction from the bonds in their structure. [AIIMS 2010]
plant is difficult and expensive. 15. Assertion: Palmitic acid has 20 carbon atoms
Reason: Secon dary metabolites can be including carboxyl carbon.
commercially produced by using tissue culture Reason : Arachidonic acid has 16 carbon atoms
technique. including carboxyl carbon.
5. Assertion : Comparative biochemistry provides 16. Assertion : Glycosidic bonds are formed by
a strong evidence in favour of common ancestory dehydration.
of living beings. Reason : In polysaccharides, individual
Reason : Genetic code is universal. monosaccharide is linked by glycosidic bond.
6. Assertion : Human diet should compulsorily [AIIMS 2016]
contain glycine, serine and tyrosine. 17. Assertion: The exoskeleton of arthropods is
Reason : Essential amino acids can not be composed of complex polysaccharide called chitin.
synthesized in the human body. [AIIMS 2010] Reason : Plant cell walls are made of cellulose.
7. Assertion : The amino acid glycine comes under 18. Assertion : In a DNA molecule, A–T rich parts
the category of nonessential amino acids. melt before G–C rich parts.
Reason : This is due to the fact that it can not be Reason: In between A and T, there are three
synthesised in the body. [AIIMS 2011] H–bond, whereas in between G and C, there are
two H-bonds. [AIIMS 2017]
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70 Assertion Reason Question Bank

19. Assertion : DNA molecules and RNA molecules 30. Assertion : Enzymes lower the activation
are found in the nucleus of cell. energy.
Reason : On heating, enzymes do not lose their Reason : A substrate molecule can be acted upon
specific activity. by a particular enzyme.
20. Assertion: The heterocyclic compounds in 31. Assertion: All enzymes are not proteins.
nucleic acid are the nitrogenous bases. Reason : RNA molecules that possess catalytic
Reason : Adenine and guanine are substituted activity are called ribozymes.
pyrimidines while uracil, cytosine and thymine 32. Assertion: Inorganic catalysts work efficiently
are substituted purines. at high temperature.
21. Assertion: The bonds attaching second and Reason : Enzymes get damaged at high
third phosphate in higher nucleotide are high temperature.
energy bonds. 33. Assertion: The inhibition of activity of succinic
Reason: The bonds are attached against force dehydrogenase by malonate is the example of
of repulsion. competitive inhibition.
22. Assertion : Allosteric enzymes show feed back Reason : Competitive inhibition is the
inhibition. inhibition of enzyme activity when inhibitor
Reason : The inhibitor is competitive. closely resembles the substrate in its molecular
[AIIMS 2012] structure.
23. Assertion : Enzymes have active sites and 34. Assertion: Each enzyme has a substrate binding
substrates reactive sites on their surfaces site in its molecule which forms higly reactive
respectively. enzyme-substrate complex.
Reason : Active and reactive sites push the Reason : The enzyme-substrate complex is
enzyme and substrate molecules away from each long-lived and dissociates into its product and
other. unchanged enzyme.
24. Assertion : Enzyme substrate complex does not 35. Assertion: Co-enzyme nicotinamide adenine
remain throughout the reaction. dinucleotide (NAD) and NADP contain a
Reason : The greater the affinity of the enzyme vitamin.
for a substrate, the higher is the catalytic activity. Reason : The association of co-enzyme with
25. Assertion : Desmolysing enzymes are those apoenzyme is enduring.
which catalyse the reactions by hydrolysis. 36. Assertion: Most of the chemical reactions do
Reason : Digestive enzymes are hydrolysing in not start automatically.
nature. Reason : Reactant molecules have an energy
26. Assertion : Coenzymes serve as co-factors in a barrier to become reactive.
number of different enzyme catalyzed reactions. 37. Assertion: Hydrolases are the enzymes which
Reason : Coenzymes and prosthetic groups are catalyse the hydrolysis of ester, ether, peptide,
cofactors. glycosidic, C – C or P – N etc. bonds.
27. Assertion : Enzymes are defined as biological Reason : Lyases are the enzymes catalysing the
proteins. linking together of 2 compounds like joining of
Reason : Chemically all enzymes are globular C – O, C – N, P – O etc. bonds.
proteins. 38. Assertion: The protein part of the enzyme is
28. Assertion : The higher the turn-over number called apoenzyme and non-protein part of the
the more efficient an enzyme is. enzyme is called co-factor.
Reason : It is not dependent upon the number Reason : Zinc is a co-factor for the proteolytic
of active sites present over an enzyme. enzyme carboxypeptidase.
29. Assertion : Enzyme becomes inactive below 39. Assertion: Enzymes lower the activation energy.
minimum temperature. Reason: A substrate molecule can be acted upon
Reason : The inactivity of the enzymes is due to by a particular enzyme.
denaturation.
Biomolecules 71

Solutions
1. (d) The living systems are in metabolic flux and the body, particularly from carbohydrate
thus, maintain the concentration of metabolites. Glycine is one such non
biomolecules, always remaining in non- essential amino acid. On the contrary,
equilibrium steady state where equilibrium essential amino acids are those amino acids
is seldom achieved. No work can be carried which can not be synthesised in the animal
out in equilibrium state. Living systems are body and must be supplied with food in
therefore, regularly receiving an input of adequate amounts. Out of twenty amino
energy to prevent reaching an equilibrium acids, eight are considered essential in
and always remain in non-equilibrium steady human diet.
state. Energy is obtained from metabolism. 8. (a) Amino acids are organic acids (with
Metabolism and living state are thus, carboxylic group – COOH) having amino
complementary and synonymous. group (–NH2) generally attached to a-
2. (c) After performing elemental analysis of a carbon that also bears a variable
plant tissue, animal tissue, microbial paste hydrocarbon or alkyl group R an d
(living matter) and of a piece of earth's crust hydrogen. Amino acids are, therefore,
(animate object), it was found that all living substituted methanes where the four
and non-living systems are made up of substituent groups occupy the four
same chemical i.e., elements (e.g. carbon, valency positions. These are hydrogen,
hydrogen, oxygen and several others). carboxyl group and a variable group
Most living organisms have relatively high designated as R group.
abundance of carbon and hydrogen than 9. (c) Each individual protein is a polymer of
in earth's crust. amino acids. As there are 20 types of amino
3. (c) All the catalysts including those which acids, a protein is a heteropolymer and not
hasten the metabolic conversion rate are a homopolymer. Amino acids can be
proteins. essential or non-essential. Certain amino
4. (b) Secondary metabolites are biosynthetically acids are essential for our health and they
derived from primary metabolites but more have to be supplied through our diet.
limited in distribution in plant kingdom Dietary proteins are thus, a source of
being restricted to a particular taxonomic essential amino acids. Non-essential amino
group. By culture media using tissue acids are those amino acids which are
culture technique, secondary metabolites synthesised in our body.
can be produced on a large scale. 10. (b) The primary structure of protein depicts
5. (b) Comparative biochemistry provides a the sequence of amino acids in a chain or
strong evidence for common ancestors of gives the positional information in a
living beings (e.g. proteins lymph, protein. Protein thread is folded in the form
enzymes, hormones, blood groups etc.) of a helix or in the sheet form in the
6. (d) Essential amino acids are those which are secondary structure. The long protein
taken from food and not synthesized in the chain is also folded upon itself like a hollow
body whereas non-essential amino acids wollen ball, giving rise to the tertiary
need not be supplied in the diet and are structure. This gives us a 3-dimensional
synthesized in the body. Glycine, serine and view of a protein. Tertiary structure is
tyrosine are non-essential amino acids. absolutely necessary for many biological
7. (c) Non-essential amino acids are those amino activities of proteins.
acids which need not be supplied in the 11. (b) Proteins and amino acids are amphoteric in
diet because they can be synthesised by nature, i.e., in aqueous they possess both
 EBD_7166
72 Assertion Reason Question Bank

cationic and anionic groups. All the amino 18. (c) In a DNA molecule, A-T rich parts melt
acids are necessary for the normal function before G-C rich parts because there are two
of the body as they are building blocks of H-bond between A and T whereas in
proteins and enzymes. between G and C, there are three H-bond.
12. (a) Nine amino acids are referred to as the 19. (d) We know that DNA molecules are found
essential amino acids for human. They must primarily in the nucleus of the cell but RNA
be therefore, supplied through diet as our molecules are found outside the nucleus.
body cannot synthesize these. By heating, its special structural
13. (d) Vegetable oils and fats are present in plants arrangement is changed irreversibly. This
in insoluble form. They are extracted mostly results in the conversion of enzyme into a
from seeds. In several cereals, they are fibrous or insoluble form. Due to this
obtained from embryo. Olive and palm oils irreversible change, enzymes lose their
are obtained from flesly pericarp of the fruit. specific activity when heated.
Sometimes oils are also extracted from 20. (c) Nucleic acids are polynucleotides. A
roots, stem and leaves. nucleotide has three chemically distinct
14. (c) Compounds having double bond in their components. One is a heterocyclic
structure are more unstable compounds in compound, the second is a monosaccharide
comparison to single bond holders. and the third a phosphoric acid or
Unsaturated fats those have double bonds phosphate. The heterocyclic compounds in
in their structures are more reactive than nucleic acids are the nitrogenous bases
saturated fats. named adenine, guanine, uracil, cytosine
15. (d) Palmitic acids and arachidonic acids are and thymine. Adenine and guanine are
simple fatty acids. A fatty acid has a substituted purines while the rest are
carboxyl group attached to an R group. The substituted pyrimidines formed from the
R group could be a methyl (–CH3), or ethyl skeletal heterocyclic rings purine and
(–C2H5) or higher number of –CH2 groups pyrimidine respectively.
(1 carbon to 19 carbons). For example, 21. (a) Nucleotides which possess more than one
palmitic acid has 16 carbons including phosphate group are called higher
carboxyl carbon. Arachidonic acid has 20 nucleotides. The second and third
carbon atoms including the carboxyl phosphates of higher nucleotides are
carbon. attached against forces of repulsion
16. (b) In polysaccharides, individual monosaccharide between similarly charged phosphate
is linked by glycosidic bond. This bond is radicals. Hence, the bonds attaching
formed between two carbon atoms of two second and third phosphates are higher
adjacent monosaccharides. A glycosidic bond energy bonds.
is a type of covalent bond that joins a 22. (c) Feed back inhibition is a type of reversible
carbohydrate molecule to another group, which inhibition found in allosteric enzymes. The
may or may not be another carbohydrate. inhibitor is non-competitive and is usually
Glycosidic bonds are formed by dehydration. a low molecular intermediate or product of
17. (b) Polysaccharides are complex carbohydrates metabolic pathway having a chain of
which are formed by polymerisation of large reactions involving a number of enzymes.
number of monosaccharide monomers. 23. (c) Enzyme has specific site for substrates
Exoskeleton of arthropods, contains a complex called as active sites and substrate has
polysaccharide called chitin. These complex reactive sites. These active and reactive
polysaccharides are heteropolymers. Plant cell sites help in making of substrate enzyme
walls are made of cellulose. Paper made from complex.
plant pulp and cotton fibre is cellulosic. 24. (a) The enzymes substrate complex is short
Cellulose is a homopolysaccharide. lived. The substrate is changed into
products. These products remain
Biomolecules 73

complexed with the active site of the enzyme temperature destroys enzymes by causing
for a brief period. They soon separate and their denaturation.
the active site is free to perform another 30. (b) Activation energy is an external supply of
catalytic act. Enzyme activity depends energy which is needed for the initiation of
upon their affinity of substrates. If turnover the chemical reaction. Activation energy
number of substrate is higher, then required for such a large number of
enzymes show high affinity towards reactions cannot be provided by living
substrate. The number of substrate systems. Enzymes lower the activation
molecules changed per minute by a energy required for a reaction. Enzymes are
molecule or enzyme is called turn over generally specific for their substrates.
number. 31. (a) Almost all enzymes are proteins. They may
25. (b) Desmolysing enzymes are those which have additional inorganic or organic
substances for their activity. Some RNA
catalyse reactions by the other methods
molecules behave like enzymes, which are
other than hydrolysis, e.g., aldolases,
called ribozymes.
dehydrogenases, oxidases, etc. Digestive
32. (a) Inorganic catalysts work efficiently at high
enzymes function by catalysing temperatures and high pressures, while
hydrolysis. Larger molecules are broken enzymes get damaged at high temperatures
into smaller ones. They are grouped into (above 40°C). However, enzymes isolated
three types - proteolytic (breaks protein from organisms who normally live under
molecule), amylolytic (breaks sugar extremely high temperatures (e.g., hot vents
molecule) and lipolytic (breaks lipid and sulphur springs) are stable and retain
molecule). their catalytic power even at high
26. (b) Cofactor may be inorganic or organic in temperatures (upto 80°–90°C).
nature. Organic cofactors are of two types, 33. (a) The activity of an enzyme is highly specific
coenzymes and prosthetic groups. to the presence of chemicals that bind to
Coenzymes are easily separable non- the enzyme. When the inhibitor closely
protein organic cofactors. Prosthetic resembles the substrate in its molecular
groups are non-protein organic cofactors structure and inhibits the activity of the
firmly attached to apoenzymes (protein part enzyme, it is known as competitive inhibitor.
of enzyme). Consequently, the substrate cannot bind
27. (a) We know that all biological reactions are and the enzyme action declines. The
catalysed by special catalysts called inhibition of succinic dehydrogenase by
enzyme, thus enzymes are defined as malonate which closely resembles the
biological proteins. We also know that substrate succinate in structure is the
enzymes are small organic molecules which example of competitive inhibition.
34. (c) A particular substrate molecule is acted
are weakly held to the protein and can be
upon by a particular enzyme. After coming
easily separated by dialysis. Therefore,
in contact with the active site of the enzyme,
chemically all enzymes are globular
the substrate molecules or reactants form
proteins.
a complex called enzyme-substrate
28. (c) The number of substrate molecules
complex. The enzyme substrate complex is
changed per minute by a molecule or
short lived. In the complexed state, the
enzyme is called turn over number. The
molecules of th e substr ate undergo
higher the turn-over number, the more
chemical change. The products remain
efficient an enzyme is. It depends upon the
attached to the enzyme for some time so
number of active sites present over an
that an enzyme product complex is also
enzyme.
formed. However, the products are soon
29. (c) Enzyme becomes inactive below minimum
released and the freed enzyme is able to
temperature. Low temperature preserve the
bind more substrate molecules.
enzymes in the inactive state. High
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74 Assertion Reason Question Bank

35. (c) Co-enzymes are also organic compounds molecules. The phenomenon is called
but their association with the apoenzyme hydrolysis. Lyases are the enzymes which
is only transient, usually occurring during cause cleaveage, removal of groups
the course of catalysis. Co-enzymes serve without hydrolysis, addition of groups to
as cofactors in a number of different enzyme double bonds or removal of a group
catalyzed reactions. The essential chemical producing double bond, e.g., histidine
components of many co-enzymes are decarboxylase breaks histidine to histamine
vitamins, e.g., co-enzyme nicotinamide and CO2.
adenine dinucleotide contain the vitamin 38. (b) Cofactor is a small, heat stable and
niacin. dialysable part of conjugate enzyme. It may
36. (a) The chemical or metabolic conversion be inorganic or organic in nature. Organic
refers to a reaction. Most of the chemical cofactors are of two types, coenzymes and
reactions do not start automatically prosthetic groups. Inorganic cofactors
because the reactant molecules have an include ions of a variety of minerals e.g.,
energy barrier to become reactive. calcium, iron, copper, zinc, magnesium,
Therefore, an external supply of energy is manganese, potassium, nickel,
needed for the start of the chemical molybdenum, selenium, cobalt. They
reaction. It is called activation enegy. usually function as activators. Zinc is
Enzymes lower the activation energy required for carboxypeptidase activity.
required for a reaction. 39. (b) The external supply of energy which is
37. (c) Enzymes are of various types depending needed for the initiation of the chemical
on their action. Hydrolases catalyse the reaction is activation energy. Activation
hydrolysis of ester, ether, peptide, energy required for such a large number of
glycosidic, C – C, C – halide, P – N bonds reactions cannot be provided by living
etc. which are formed by dehydration and systems. Enzymes lower the activation
condensation. Hydrolases break up large energy required for a reaction. Enzymes are
molecules into smaller ones with the help usually specific for their substrates.
of hydrogen and hydroxyl groups of water