Aromatic amino acids (tyrosine,
NEET 2020
Quick Revision Key Notes
BIOMOLECULES
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1. Trichloroacetic acid (Cl3CCOOH) à
Used to analyse chemical composition of living
tissue
Acid-soluble pool à
Compounds found have molecular weights
ranging from 18 to around 800 daltons (Da)
approximately. @ Micro molecules
Retentate or the acid-insoluble fraction à
Only four types of organic compounds i.e.,
proteins, nucleic acids, polysaccharides and
lipids. @ Macro molecules except Lipid
Except lipids, all have molecular weights
10000 daltons and above.
@
2. All the carbon compounds present in living
tissues à ‘Biomolecules’.
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3. Amino acids à
Organic compounds
Have an amino group and an acidic group on
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the same carbon i.e., the alpha-carbon. Hence,
they are called α-amino acids.
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They are substituted methanes.
There are four substituent groups
Hydrogen, Carboxyl group, Amino group and A
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variable group designated as R group.
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Based on the nature of R group there are many
amino acids.
In proteins à only of 20 types of amino acids .
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The R group à
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The chemical and physical properties of amino
acids determined by à Amino group,
carboxyl group and the R functional groups.
Based on number of amino & carboxyl groups,
o Acidic (e.g., glutamic acid),
o Basic (lysine) and
o Neutral (valine) amino acids.
o
phenylalanine, tryptophan).
o A particular property of amino acids is
the ionizable nature of –NH2 and –
COOH groups. @ Isoelectric pH &
Zwittor ion
o In solutions of different pHs, the
structure of amino acids changes.
4. Lipids
o Generally water insoluble.
o A fatty acid has a carboxyl group
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attached to an R group.
o The R group à Generally 1 carbon to
19 carbons
o Palmitic acid has 16 carbons
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o Arachidonic acid has 20 carbon atoms
o Fatty acids
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§ Saturated (without double bond)
§ unsaturated (with one or more
gm C=C double bonds).
§ Most simple lipid is glycerol
which is trihydroxy propane.
o Many lipids have both glycerol and
fatty acids.
o Oils have lower melting point (e.g.,
gingely oil)
o Some lipids have phosphorous and a
phosphorylated organic compound
à Phospholipids à Found in cell
membrane.
§ Example - Lecithin
o Neural tissues have lipids with more
complex structures.
5. Nitrogen Base à
o Heterocyclic rings
o Nitrogen bases – adenine, guanine,
cytosine, uracil, and thymine.
o Nitrogen base + sugar àNucleosides.
o Adenosine, guanosine, thymidine,
uridine and cytidine are nucleosides.
o Nucleotide = Nucleoside +Phosphate
o Nucleotides à Adenylic acid, thymidylic
acid, guanylic acid, uridylic acid and
cytidylic acid
o Nucleic acids like DNA and RNA consist
of nucleotides only.
o DNA & RNA à Genetic material.
6. PRIMARY AND SECONDARY METABOLITES
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 o Primary metabolites à Have
identifiable functions and play roles in
normal physiological processes.
§ Proteins, amino acids, nucleotides,
carbohydrates, lipids etc.
o Secondary metabolites à Not clear
understanding about the role or
functions of all the ‘secondary
metabolites’ in host organisms.
§ Many useful to ‘human welfare’
§ Some secondary metabolites have
11. The GLUT or SLC2A family are a protein family
that is found in most mammalian cells.
12. GLUT is a type of uniporter transporter protein.
13. Glucose transporter type 4 (GLUT-4) is a protein
encoded, in humans, by the SLC2A4 gene.
14. GLUT4 is the insulin-regulated glucose
transporter found primarily in adipose tissues
and striated muscle (skeletal and cardiac).
15. Collagen is the most abundant protein in
animal world
16. Ribulose bisphosphate Carboxylase-Oxygenase

ecological importance.
§ e.g., rubber, drugs, spices, scents,
pigments, alkaloids, flavonoids,
rubber, essential oils, antibiotics,
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(RuBisCO) is the most abundant protein in the
whole of the biosphere.
17. POLYSACCHARIDES
o Long chains of sugars.

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coloured pigments, scents, gums, o Threads containing different
spices. monosaccharides as building blocks.

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Pigments Carotenoids, o cellulose (Polymer of beta-D-glucose) &
Anthocyanins, etc. Starch (Polymer of alpha-D-glucose)
Alkaloids Morphine, Codeine
Terpenoides
Essential oils
Monoterpenes,Diterpenes
Lemon grass oil
gm
18. Cellulose is a homopolymer;
Starch is à A store house of energy in plant
tissues;
Toxins Abrin, Ricin
Glycogen is à A store house of energy in
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Lectins Concanavalin A
Drugs Vinblastin, curcumin
animal tissue
19. Inulin is a polymer of fructose.
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Polymers Rubber, gums, cellulose

20. In Glycogen à The right end is called the
7. PROTEINS reducing end and the left end is called the non-
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o Polypeptides. reducing end.

o Linear chains of amino acids linked by 21. Starch forms helical secondary structures.
peptide bonds Starch can hold I2 molecules in the helical
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o Polymer of amino acids. portion. The starch-I2 is blue in colour.

o 20 types of amino 22. Cellulose does not contain complex helices and
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o Heteropolymer and not a homopolymer. hence cannot hold I2 .

8. Dietary proteins are the source of essential 23. Plant cell walls, Cotton fibre, Paper pulp are
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amino acids. We get through our diet/food. made of cellulose.

9. Proteins carry out many functions in living 24. Complex polysaccharides à Have as building
organisms blocks, amino-sugars and chemically modified
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Protein Functions sugars (e.g., glucosamine, N-acetyl

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Collagen Intercellular ground substance galactosamine, etc.).

Trypsin Enzyme o Exoskeletons of arthropods, (chitin)
Insulin Hormone o These complex polysaccharides are
Antibody Fights infectious agents mostly homopolymers. (2020 – NCERT)
Receptor Sensory reception (smell, taste, 25. NUCLEIC ACIDS:
hormone, etc.) Polynucleotides.
GLUT -4 Enables glucose transport Building block à nucleotide.
into cells
A nucleotide consist of à 3 components
1. N Base, 2. Pentose sugar 3. a phosphate.
10. GLUCOSE TRANSPORTERS are a group of Heterocyclic compounds in nucleic acids are the
membrane proteins that facilitate the transport nitrogenous bases à adenine, guanine, uracil,
of glucose across the plasma membrane. cytosine, and thymine.

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 Adenine and Guanine are substituted purines
while the rest are substituted pyrimidines.
The sugar found in polynucleotides à either
ribose or 2’ deoxyribose.
A nucleic acid containing deoxyribose à DNA
A nucleic acid containing ribose à RNA
26. STRUCTURE OF PROTEINS
Biologists describe the protein structure at four
levels.
The sequence of amino acids à Primary
structure of a protein.
The first amino acid à N-terminal amino acid.
The last amino acid à C-terminal amino acid.
A protein thread is folded in the form of a helix
à Secondary structure
In proteins, only right handed helices are
observed.
In addition, the long protein chain is also
folded upon itself à Tertiary structure
This gives us a 3-dimensional view of a protein.
Tertiary structure is absolutely necessary for the
many biological activities of proteins.
Some proteins are an assembly of more than
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one polypeptide or subunits. à quaternary
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structure of a protein.
Adult human haemoglobin consists of 4
subunits. @ 2 Alpha & 2 Beta chains
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27. NATURE OF BOND LINKING MONOMERS IN A
POLYMER à
In a protein, amino acids are linked à
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by peptide bond
In a polysaccharide monosaccharides are
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linked à by glycosidic bond.
In a nucleic acid nucleotides are linked à by
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Phosphodiester bond
a phosphate moiety links the 3’-carbon of one sugar
of one nucleotide to the 5’-carbon of the sugar of the
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succeeding nucleotide.
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28. Nucleic acids exhibit a wide variety of
secondary structures.
Secondary structures exhibited by DNA is the
famous Watson-Crick model.
DNA is a double helix.
The two strands are antiparallel i.e., run in the
opposite direction.
The backbone is formed by the sugar
phosphate-sugar chain.
A and G of one strand pairs with T and C, on the
other strand.
2 H - bonds between A and T and 3 H - bonds
between G and C.
Each strand appears like a helical staircase.
Each step of ascent à a pair of bases.
At each step of ascent, the strand turns 36°.
One full turn of the helical strand would
involve ten steps or ten base pairs.
The pitch would be 34Å. The rise per base pair
would be 3.4Å.
This form of DNA with the above mentioned
features is called B-DNA.
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29. Biomolecules have a turn over.
o Constantly being changed into some
other biomolecules and also made from
some other biomolecules.
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o Breaking and making is through
chemical reactions à metabolism.
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o In other words, metabolites are
converted into each other in a series of
gm linked reactions called metabolic
pathways.
o These metabolic reactions is that every
chemical reaction is a catalysed reaction.
o Proteins with catalytic power are named
enzymes.
30. Metabolic pathways can lead to
o More complex structure from a simpler
structure (biosynthetic or anabolic
pathways)
o Simpler structure from a complex
structure (catabolic pathways)
o Anabolic pathways, as expected,
consume energy.
o catabolic pathways lead to the release of
energy.
o Energy currency in living systems is the
bond energy in a chemical called
adenosine triphosphate (ATP).
o ATP is energy currency of cell
31. These biomolecules are in a metabolic flux.
32. Any chemical or physical process moves
spontaneously to equilibrium.
33. The steady state is a non-equilibrium state.
34. The living state is a non-equilibrium steady-
state to be able to perform work
35. Living process is a constant effort to prevent
falling into equilibrium. This is achieved by
energy input.
36. Metabolism provides a mechanism for the
production of energy. Hence the living state
and metabolism are synonymous.
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 37. ENZYMES
o Almost all enzymes are proteins.
o Ribozymes à catalytic RNA.
o An active site of an enzyme is a crevice or
pocket into which the substrate fits.
o Enzymes get damaged at high
temperatures (say above 40°C).
o Thermal stability seen in enzymes
isolated from thermophilic organisms.
38. Rate of a physical or chemical process refers to
the amount of product formed per unit time.
39. There are thousands of types of enzymes each
catalysing a unique chemical or metabolic
reaction.
40. Enzymes eventually bring down activation
energy barrier making the transition of ‘S’ to ‘P’
more easy.
41. Each enzyme (E) has a substrate (S) binding site
in its molecule so that a highly reactive
enzyme-substrate complex (ES) is produced.
42. ES complex is short-lived and dissociates into
its product(s) P and the unchanged enzyme
with an intermediate formation of the enzyme-
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product complex (EP).
43. The catalytic cycle of an enzyme action has
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following steps:
o Active site of Enzyme + Substrate à
Enzyme substrate complex formation
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o In ES complex the substrate ffitted more
tightly
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o Enzyme- product complex is formed
through catalysis (Bond reorganisation)
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o Dissociation of Enzyme Product complex
into enzyme & product
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44. Factors Affecting Enzyme Activity
o The activity of an enzyme can be affected
by a change in the conditions which can
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alter the tertiary structure of the protein.
o Temperature, pH, change in substrate
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concentration or binding of specific
chemicals that regulate its activity.
o Enzymes generally function in a narrow
range of temperature and pH
o Each enzyme shows its highest activity at
a particular temperature & pH called the
optimum temperature & optimum pH.
o Activity declines both below and above
the optimum value.
o Low temperature preserves the enzyme
in a temporarily inactive state
o high temperature destroys enzymatic
activity because proteins are denatured
by heat.
45. Concentration of Substrate à
At fixed enzyme concentration with the
increase in substrate concentration à the
velocity of the enzymatic reaction rises at first.
à reaches a maximum velocity (Vmax) à not
exceeded by any further rise in concentration of
the substrate. à This is because no free
enzyme molecules to bind with the additional
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substrate molecules @ SATURATION EFFECT
46. The Michaelis constant (KM) is defined as the
substrate concentration at which the reaction
rate is half of its maximal value (or in other
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words it defines the substrate concentration at
which half of the active sites are occupied).
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47. An enzyme with a high Km has a low affinity for
its substrate, and requires a greater
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48.
concentration of substrate to achieve Vmax
The activity of an enzyme is also sensitive to the
presence of specific chemicals that bind to the
enzyme. When the binding of the chemical
shuts off enzyme activity, the process is called
inhibition and the chemical is called an
inhibitor.
49. When the inhibitor closely resembles the
substrate in its molecular structure and inhibits
the activity of the enzyme, it is known as
competitive inhibitor.
e.g., inhibition of succinic dehydrogenase by
malonate which closely resembles the
substrate succinate in structure. Such
competitive inhibitors are often used in the
control of bacterial pathogens.
50. CLASSIFICATION & NOMENCLATURE OF ENZYMES
On the basis of the type of reactions à 6
classes each with 4-13 subclasses
Named accordingly by a four-digit number.
OXIDOREDUCTASES/DEHYDROGENASES:
Enzymes which catalyse oxidation-reduction
between two substrates
TRANSFERASES:
Enzymes catalysing a transfer of a group
HYDROLASES:
Enzymes catalysing hydrolysis of ester, ether,
peptide, glycosidic, C-C, C-halide or P-N bonds.
LYASES:
Enzymes that catalyse removal of groups from
substrates by mechanisms other than
hydrolysis leaving double bonds.
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 ISOMERASES:
Includes all enzymes catalysing inter-
conversion of optical, geometric or positional
isomers.
LIGASES:
Enzymes catalysing the linking together of 2
compounds, e.g., enzymes which catalyse
joining of C-O, C-S, C-N, P-O etc. bonds.
51. CO-FACTORS à
o Non-protein constituents
o bound to the enzyme to make the
enzyme catalytically active.
o In these instances, the protein portion of
the enzymes is called the APOENZYME.
o Three kinds of cofactors may be
identified:
§ prosthetic groups,
§ co-enzymes and
§ metal ions.
o Prosthetic groups are organic
compounds à tightly bound to the
apoenzyme.
o Co-enzymes are also organic compounds
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à their association with the apoenzyme
is only transient, usually occurring
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during the course of catalysis.
o The essential chemical components of
many coenzymes are vitamins, e.g.,
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coenzyme nicotinamide adenine
dinucleotide (NAD) and NADP contain
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the vitamin niacin.
o A number of enzymes require metal ions
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for their activity
e.g., zinc is a cofactor for the proteolytic
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enzyme carboxypeptidase.
o Catalytic activity is lost when the co-
factor is removed from the enzyme
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which testifies that they play a crucial
role in the catalytic activity of the
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enzyme.
GOLDEN POINTS by BIOMENTORS
1. Living organisms have more carbon, oxygen and
hydrogen per unit mass than inanimate objects
2. Silicon is not found in living organisms
3. Amino acids have both an amino group and a carboxyl
group in their structure.
4. An amino acid under certain condition have both
positive and negative charges simultaneously in the
same molecule. Such a form of amino acid is calledà
Zwitter ionic form
5. Fructose have the same number of carbon as present
in glucose
6. An acid soluble compound formed by phosphorylation
of nucleoside is called à Nucleotide
7. When we homogenise any tissue in an acid the acid
soluble pool represents Cytoplasm
8. The most abundant chemical in living organisms à
Water
9. Proteins are heteropolymers usually made of à20
types of monomers
10. Proteins perform many physiological functions. For
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example some proteins function as enzymes & some
proteins performs as à Hormones
11. Glycogen is a homopolymer made up of Glucose units
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12. The number of ‘ends’ in a glycogen molecule would be
à Equal to the number of branches plus one
13. The primary structure of a protein molecule has àTwo
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ends
14. Dissolving CO2 in water reactions is also enzyme-
gm mediated in biological system
15. 80% of cytoplasm in plant cells is Water
16. Two groups of involved in peptide linkage between
different amino acids are NH2 & COOH
17. Role of enzyme in reactions is to àDecrease activation
energy
18. End product is responsible for inhibition of enzymatic
process during feed back.
19. Enzymes are not found in à Viruses (except Retro
virus family)
20. ATP is a nucleotide
21. Glycoproteins have carbohydrate as prosthetic group.
22. Km value of enzyme is substrate conc. at 1/2 V max
23. Nitroginase Enzyme first used for nitrogen fixation
24. Most of the water in the young plant cell à in
cytoplasm; Mature plant cell à in Central vacuole
25. Osmotically inactive chief stored material in animal
body is Glycogen
26. Lipids are insoluble in water because lipid molecules
are à Hydrophobic
27. Galactose is a reducing sugar
28. Sucrose not give positive Fehling’s test (non reducing
sugar)
29. Mathematical explanation for enzyme action on
substrate was provided byà Michaelis and Menten
30. Km value is dependent upon Substrate concentration
31. The major role of minor elements inside living
organisms is to act as à Co-factors of enzymes
32. Tyrosinase needs copper as an activator
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 33. The catalytic efficiency of two different enzymes can be
compared by the Km value
34. Competitive inhibition is seen when the substrate and
the inhibitor compete for the active site on the
enzyme
35. Enzymes, vitamins and hormones can be classified
into a single category of biological chemicals, because
all of these help in regulating metabolism
36. Nucleotides are building blocks of nucleic acids.
37. Each nucleotide is a composite molecule formed by
Base-sugar-phosphate
38. Carbohydrates, the most abundant biomolecule on
earth, are produced by Some bacteria, algae and
55. In a disaccharide two monosaccharides are linked by a
glycosidic bond.
56. Excess carbohydrates and proteins are stores in the
body as Fats
57. Cellulose is a homopolymer
58. Enzymes require optimum temperature & pH for
maximal activity
59. Enzymes are denatured at high temperature but in
certain exceptional organisms they are effective even
at temperatures 80°-90℃
60. Enzymes are highly specific
61. Remember the figure give below

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green plant cells
39. The simplest amino acid is àGlycine
40. Richest source of protein is à Soyabean

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41. This curves shows à

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A B C D
gm
Transition
state
Potential
energy
Activation
energy
without
Activation
energy with
enzyme
enzyme
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62. A disaccharide that gives two molecules of glucose on
A = Normal enzyme action, hydrolysis isà Maltose
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B = Competitive inhibition, 63. The given curve shows enzymatic activity in relation to
C = Non-competitive inhibition temperature
42. An organic substrate bound to an enzyme and
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essential for its activity is calledà Coenzyme

43. About 98 per cent of the mass of every living organism
is composed of just six elements including carbon,
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hydrogen, nitrogen, oxygen and Phosphorus and

sulphur
X axis Y axis
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44. Boron element is very essential for uptake and

utilization of Ca2+ and membrane function. Temperature Enzyme activity
64. The enzymes carries out the initial step in the
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45. In a protein the amino acids are linked by Peptide

bonds digestion of milk in humans is Pepsin
46. Three most abundant elements in protoplasm are 65. In humans, milk protein-digesting enzyme is
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Carbon, hydrogen, oxygen the stomach is pepsin. In calves it is rennin. Rennin is

47. Chitin is present in the cell wall of fungi also present in small amounts in human infants but
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48. Carbohydrates are commonly found as starch in plant

not adults.
storage organs.
66. Pepsin acts on water insoluble caseinogen (milk
49. A competitive inhibitor of succinic dehydrogenase is
àMalonate protein) to form soluble 'casein'.
50. Inulin, a low molecular weight polysaccharide is 67. Lecithin is a component of cell membrane
obtained from roots of à Dahlia ; polymer of D-
fructose in which monomer units are linked together
by beta (1->2) glycosidic linkage.
51. Collagen is à Fibrous protein
52. Spirulina BGA is the rich source of à Protein
53. In human per cent of body weight of carbohydrates,
lipids and proteins respectively is à1, 15, 17
54. Table sugar is Sucrose 68. Glycerol is a trihydroxy propane

6
 69. In a normal adult, ascending order of concentration of
following molecules is: K > Na > Fe > Cu
70. A phosphoglyceride is always made up of saturated or
unsaturated fatty acids esterified to a glycerol
molecule to which a phosphate group is also attached
71. Macromolecule chitin is nitrogen containing
polysaccharide
72. Transition state structure of the substrate formed
during an enzymatic reaction is à Transient and
unstable
73. The essential chemical components of many
metabolism, blood clotting and permeability of cell
membrane. e.g., Lecithin, cephalin
93. Biomarker of human faeces à Coprosterol ; It is
formed as a result of the reduction by bacteria in
intestine from the double bond of cholesterol between
C5 and C6.
94. Terpenes : found in essential oils and present mostly in
oils of camphor, eucalyptus, lemon and mint. Phytol is
a terpenoid alcohol present in Vitamin A, K, E and in
pigments like chlorophyll carotenoid.
95. Total known amino acid are more than 200 out of these

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coenzymes are Vitamins of B complex mainly
only 20 amino acid takes part in protein synthesis
74. Enzymes are denatured at high temperatures
called protein amino acid.
75. Substrate binds with enzyme at its active site
96. Glycine is a simplest amino acid.

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76. A non-competitive inhibitor binds the enzyme at a site
97. Sulphur containing amino acids : They have sulphur
distinct from that which binds the substrate
atom in side chain. e.g., methionine, cysteine.
77. Malonate is a competitive inhibitor of succinic

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dehydrogenase 98. Proline and hydroxyproline have, NH (imino group)

78. Sucrose is a non-reducing carbohydrate.
79. The presence of competitive inhibitor increases the Km
of the enzyme for the substrate
80. A competitive inhibitor reacts reversibly with the
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enzyme to form an enzyme –inhibitor complex
81. In competitive inhibition, the inhibitor molecule is not
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instead of NH 2 hence are called imino acids.
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99. Purines : Purines are 9 membered double ringed
nitrogenous bases which possess nitrogen at 1' ,3' ,7'
and 9' positions. They are adenine (A) and guanine (G).
100. Pyrimidines : They are smaller molecule than purines.
These are 6 membered single ringed nitrogenous

chemically changed by the enzyme bases that contain nitrogen at 1' and 3' positions like
82. The competitive inhibitor does not effect the rate of cytosine (C), thymine (T) and uracil (U).
breakdown of the enzyme substrate complex
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101. ATP was discovered by Karl Lohmann (1929).

83. An allosteric inhibitor of the enzyme acts by binding to 102. Formation of ATP is endergonic reaction.
the non-catalytic site of the enzyme (allosteric site)
103. Glycogen : It is a branched polymer of glucose and
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84. The two polypeptide of human insulin are linked

contain 30,000 glucose units. It is also called animal
together by à Disulphide bridges
starch. It is also found as storage product in blue green
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85. Holoenzyme = Apoenzyme + Cofactor

algae, slime moulds, fungi and bacteria. It is a non-
86. Cofactor à may be Prosthetic group, Co-enzymes or
reducing sugar and gives red colour with iodine. In
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Metal activator
glycogen, glucose molecule are linked by 1 – 4
87. The two functional groups characteristic of sugars are
glycosidic linkage in straight part and 1 – 6 linkage in
Carbonyl and hydroxyl
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the branching part glycogen has branch points about

88. Term lipid was coined by Bloor (1943). These are esters
every 8-10 glucose units.
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of fatty acids and alcohol.

104. Starch : Starch is formed in photosynthesis and function
89. Linoleic acid, linolenic acid, arachidonic acid are
as energy storing substance. It is found abundantly in
essential fatty acid (Evans and Burr 1928).
rice, wheat, legumes, potato (oval and ecentric
90. Deficiency of essential fatty acid may cause follicular
shaped), banana, etc. Starch is of two types. Straight
hyper keratosis disease.
chain polysaccharides known as amylose and branched
91. Bees wax is a common example of wax. It is a
chain as amylopectin. Both composed of D – glucose
combination of palmitic acid and mericyl alcohol
units jointed by a - 1 - 4 linkage and a - 1 - 6
(C 30 H 61 OH ) .
linkage. It is insoluble in water and gives blue colour
92. Phospholipids : It is amphipathic molecule. These
when treated with iodine.
contain phosphoric acid. It helps in transport,
105. Cellulose : An important constituent of cell wall, made
up of unbranched chain of 6000 b–D glucose units

7
 linked by 1 – 4 glycosidic linkage. It is fibrous, rigid and
insoluble in water. It doesn’t give any colour when
treated with iodine. It is a most abundant
polysaccharide.
106. Chitin : It is a polyglycol consisting of N-acetyl–D–
glucosamine units connected with b - 1, 4 glycosidic
linkage. Mostly it is found in hard exoskeleton of insects
and crustaceans and some times in fungal cell wall.
Second most abundant carbohydrate.
107. Agar-Agar : It is a galactan, consisting of both D and L
synthesis. The sequence of nitrogenous bases is
repeated several times.
121. Chargaff’s rule : Quantitatively the ratio of adenine (A) to
thymine (T) and guanine (G) to cytosine (C) is equal. i.e.,
“Purines are always equal to pyrimidine”.
122. C value : It is the total amount of DNA in a genome or
haploid set of chromosomes.
123. X-Ray crystallography study of DNA : It was done by
Wilkins. It shows that the two polynucleotide chains of
DNA show helical configuration.
124. RNA is second type of nucleic acid which is found in

galactose and it is used to prepare bacterial cultures. It
is obtained from cell wall of red algae e.g., Gracilaria,
Gelidium etc.
108. The common sugars in hemicellulose are D-xylose, L–
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nucleus as well as in cytoplasm i.e., mitochondria,
plastids, ribosomes etc. They carry the genetic
information in some viruses. They are widely

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arabinose, D-galactose, D-mannose and D-glucusonic distributed in the cell. Genomic RNA was discovered by
acid. e.g., hemicellulose. Franklin and Conrat (1957).

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109. Gum : It secreted by higher plants after injury or
pathogenic attacks. It is viscous and seals the wound. It
involves sugars like L-arabinose, D-galactose, D-
glucusonic acid. e.g., gum arabic.
gm NCERT IMAGES

110. Mucopolysaccharides : These are gelatinous substance,

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containing amino sugars, uronic acid, etc. All slimy
substances of plant are mucopolysaccharide. e.g.,
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hyaluronic acid, vitreous humour, chondridine

sulphate, heparin, husk of isabgol and mucilage also.
a1

111. Protein : Word protein was coined by Berzelius (1838)

and was used by G. J. Mulder first time 1840.
112. 15% - 30% of protoplasm is made up of protein.
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Average proteins contain 16% nitrogen, 50–55%

carbon, oxygen 20–24%, hydrogen 7% and sulphur 0.3
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– 0.5%.
113. Phosphoprotein : They composed of protein and
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phosphate e.g., casein (milk) and vitellin (egg).

114. Proteins are the most diverse molecule on the earth.
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115. Monelin protein is the sweetest substance obtained

from African berry (2000 time sweeter than sucrose).
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116. Most abundant protein on earth is RuBisCo

117. Myosin is structural as well as enzymatic protein (ATPase).
118. Nucleic acids were first reported by Friedrich Miescher
(1871) from the nucleus of pus cell. Altmann called it
first time as nucleic acid. Nuclein was renamed nucleic
acid by Altman in (1889). They are found in nucleus.
They help in transfer of genetic information.
119. Term DNA was given by Zacharis.
120. Repetitive DNA : This type of arrangement is found near
centromere of chromosome and is inert in RNA

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 aj
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9
 KEY IMAGES FOR QUICK REVISION

om
l.c
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01
a1
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 aj
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 aj
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Nucleoside
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NUCLEOTIDE

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 aj
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 aj
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