S.D.

JADHAV ENGLISH MEDIUM SCHOOL,

Shaha, Tal. Sinnar, Dist. Nashik

11 Class State Board

th

Chapter 6
*Biomolecules*
L1
MR. PAWAR NAYAN
BIOLOGY EXPERT
 Biomolecules
• Biochemistry
It is also called Biological Chemistry.
It is the study of chemical processes in living
organisms, including. But not limited to living matter.
 Cellular Pool
It is the Sum Total of various biochemical substances
present in a cell.
It exist as a Crystallo Colloid.
It comprises more than 5,000 chemicals.
 Cellular Pool

Aqueous Phase Non-aqueous Phase

Includes substances Includes substances
dissolved in water. which part of cellular
E.g. Glucose, structures.
Amino acids. E.g. Phospholipids
 Biomolecules
All the carbon compounds that we get from living
tissue, can be called biomolecules.
Biomolecules

Organic Inorganic
 Micromolecules Macromolecules
1. Smaller in size (Acid Soluble) 1. Larger in size (Acid insoluble)
2. Low molecular weight 2. High molecular weight
3. Simple structure 3. Complex structure
4. From building blocks of macromolecules 4. Formed by polymerisation of
Micromolecules.
5. Occur as molecular solution 5. Occur as Colloidal solution
E.g. Minerals, Gases, Sugars, Amino acids. E.g. Proteins, Polysaccharides, Nucleic acids
 Analysis of Organic Compounds
Grind a living tissue (a piece of vegetable or liver) in
Trichloroacetic acid in mortar with pestle to obtain
thick slurry.
 Analysis of Organic Compounds
Filter this slurry of living tissue through a cheese cloth or cotton to
obtain two fractions.
Slurry

Filtrate Retentate
 Acid soluble pool.  Acid insoluble pool.
 Micromolecules.  Macromolecules.
 Analysis of Inorganic Compounds
Weigh a small amount of a living tissue and note down its
wet weight.
Dry the living tissue by evaporating its water in an oven and
not down its dry weight.
Burn the dried tissue to oxidize all the organic compounds
to obtain ash which contains inorganic compounds of calcium,
magnesium, etc.
Inorganic compounds like phosphates & sulphates are also
found in acid-soluble fraction.
 Analysis of Inorganic Compounds
Ash or acid-soluble fraction is subjected to elemental
analysis to know elemental composition of living tissues in
the form of
 Carbon, Oxygen, Hydrogen,
 Chloride, Sodium, Potassium
 Calcium, Magnesium,
 NaCl, CaCO3, Phosphates, Sulphates.
 PROTEINS
The term protein means “Preeminent” or “First
Rank”.
The terms was first chosen by Berzelius.
Proteins are most diverse macromolecules in the
living organisms.
These form about 12% of cell content.
Proteins contain C, H, O, N.
Some contains S (Sulphur), I (Iodine), Fe & P
(Phosphorous) also.
 Proteins
The basic structural unit of protein is an amino acid.
They are synthesized in the body from 20-different types
of amino acids only, while in nature approx. 300 amino
acids are known to exist.
Since there are 20 type of amino acids which form protein,
protein is a heteropolymer.
The 20 amino acids are called 20 alphabets of bioprotein
language
 AMINO ACIDS (SUBSTITUTED
METHANES)
These are the building blocks of proteins.
All amino acids contain at least an amino
group and an carboxylic group.
Amino acids are organic compounds
containing an amino group and an acidic
group as substituent on the same carbon
i.e., the a-carbon.
Hence, they are called a-amino acids.
 Amino Acids
When dissolved in water, these exist in solution as the
amino acids are amphoteric in nature (with one amino
group and one carboxylic group).
 Properties of Amino Acids
The chemical and physical properties of amino acids are
essential of the amino carboxyl and the R functional groups.
A particular property of amino acids is the ionizable nature of
–NH2 and –COOH groups.
Hence is solutions of different pHs, the structure of amino
acids change. Fully ionized species called zwitterion have both
positive and negative charge.
 Properties of Amino Acids
All amino acids are laevo-
rotatory except glycine
which is not optically active.
Eukaryotic proteins have L-
amino acids while D-amino
acids occur in bacteria and
antibodies.
L2

TYPES OF AMINO
ACIDS
 Types of Amino
Acids

Protein Non - Protein Rare Amino

Amino acids Amino acids acids
E.g. Glycine, Alanine, E.g. Hydroxyproline,
E.g. Ornithine, Citrulline
Valine Hydroxylysine.
 Aliphatic Glycine, Alanine, Valine, Leucine, Isoleucine, Proline
Hydroxy aliphatic Serine, Threonine
Aromatic Phenylalanine, Tyrosine, Tryptophan
Basic Lysine, Arginine, Histidine.
Acidic Glutamic acid, Aspartic acid
Amide side chain Glutamine, Asparagine
Sulphur containing Cysteine, Methionine
 Essential & Non Essential Amino
Acids
Plants can synthesise all the amino acids required by them.
Humans cannot synthesis certain amino acids.
These are called essential amino acids.
These must be present in diet. Valine (Va)
Leucine (Leu)
Isoleucine (ILe)
Phenylalanine (Phe)
Tryptophan (Trp)
Lysine (Lys)
Methionine (Met)
Threonine (Thr)
 Essential & Non Essential
Amino Acids
Essential (can’t be Non essential (Can be Semi essential
produced by the human produced by the amino acids)
body) human body)
Valine (Va) Alanine (Al) Arginine
Leucine (Leu) Asparagine (Asn) Histidine
Isoleucine (ILe) Aspartic Acid (Asp)
Phenylalanine (Phe) Cysteine (Cys)
Tryptophan (Trp) Glutamic Acid (Glu)
Lysine (Lys) Glutamine (Gln)
Methionine (Met) Glycine (Gly)
Threonine(Thr) Proline (Pro)
Serine (Ser)
Tyrosine (Tyr)
 Trick To Learn Essential Amino
Acids
Prime Minister is Very ILL Today
Isoleucine Tryptophan

Leucine

Lysine
Methionine

Phenylalanine

Valine
 AMINO ACIDS
• Simplest Amino Acid – Glycine
• Most Complex Amino Acids – Tryptophan
• Imino Acids – Proline
• Double Amino Acids – Cystine
 Glycine
It is the simplest amino acid.
It does not exist in optically active forms.
It is the only amino acid which has symmetrical α-
carbon.
 Metabolic Uses of Amino Acids
Derivatives of amino acid Tyrosine:
It forms:
 Epinephrine (Adrenaline),
 Norepinephrine (Noradrenaline).
 Thyroid hormones (T3 & T4) and Melanin.

Derivatives of amino acid Tryptophan: Melatonin &

Serotonin. (Hormones of Pineal gland)
 Peptide Bonds
A polypeptide is imagined as a line, the left end represented by the first
amino acid and he right end represented by the last amino acid.
The first amino acid is also called as N-terminal amino acid.
The last amino acid is called the C-terminal amino acid.
The different amino acids are attached through – CO –NH bond called
Peptide bond or Amide bond.
 Important Peptides
Glutathione – It is a tripeptide (with 3 amino acids)
having Glycine, Glutamic acid and Cysteine.
It acts as coenzyme, maintains RBC membrane
structure, Protects Hb from getting oxidized from
hydrogen peroxide, involved in transport of amino
acids in intestine.
 Important Peptides
Oxytocin & Vasopressin – They have 9-amino acids
each.
Bradykinin – It has 9-amino acids. It is most potent
pain-producing substances which mediates
prostaglandins.
Angiotensin – Angiotensin – I with 10 amino acids &
Angiotensin – II with 8 amino acids are
vasoconstrictors.
Types of Proteins
• Simple Protein
• Conjugated Proteins
• Derived Proteins
 Simple Proteins
They are composed of amino acids only.
Generally soluble in water.
These can be fibrous or globular.
Fibrous (scleroproteins) proteins are collagen, elastin &
keratin.
Hardness of keratin is due to abundance of cysteine amino
acids in its structure.
 Simple Proteins
RUBISCO
Albumin
Globin (Haemoglobin)
Histone (in DNA of eukaryotes)
Protamines (sperm nucleus)
Prolamins like zein (maize), glutellins (elasticity in
wheat), oryzenin (rice), hordein (barley)
Lectins – They are carbohydrates binding proteins.
E.g. Concanavalin – A and agglutinins.
Conjugated or Compound Proteins
• Proteins combined with carbohydrates. E.g. Hormones (FSH,

Glycoproteins LH, TSH & HCG) Blood group, globulins of blood, mucin in
saliva, serum antigens, plasma membrane, cell wall, Antifreeze
glycoproteins (in Antarctic fishes which live below -2ᵒ C etc.

• Proteins combined with lipids E.g. Cell membrane &

Lipoproteins chylomicrons, LDL (Low density Lipoproteins are bad

cholesterol) and HDL (High density Lipoproteins are good
cholesterol)

• Proteins attached to nucleic acids, E.g. Histones in

Nucleoproteins chromosomes (Histones are basic proteins, i.e. rich in basic

amino acids – lysine and arginine), ribonucleoproteins,
protamines.
 Conjugated or Compound Proteins

Phosphoproteins • Proteins containing phosphorous as prosthetic group, e.g. Casein of milk,

pepsin, egg vitelline, phosvitin.

Metalloproteins • Proteins with metal ions, e.g. Tyrosine (copper), Carbonic anhydrase
(zinc), Cytochrome, Hb (iron), Insulin (Zinc).

• Proteins with pigment of coloured prosthetic group, e.g. flavoproteins

Chromoproteins (yellow), haemoglobin (Fe, Red), Visual pigment (purple), Cytochromes
(Fe, Red), Chlorophyll (Mg, green), Haemocyanin (Cu, Blue) etc.
 Derived Proteins
These are produced during denaturation or digestion of
proteins by
 Heat
 Physical forces
 Chemical forces
E.g. Proteoses, peptones, polypeptides, fibrin, myosin,
cooked egg white etc.
Protein Structure
• Primary structure
• Secondary structure
• Tertiary structure
• Quaternary structure
 Primary Structure
It is the order or sequence in which the specific
amino acids are arranged (by condensation,
forming peptide bonds) in the polypeptide chain.
It determines the diversity of polypeptide.
The positional information in a proteins – which
is first amino acid, which is second etc. is called
the primary structure.
The first amino acid is N-terminal and the last
amino acid is C-terminal.
It is the most unstable structure.
 Secondary Structure
Polypeptide chain repeatedly coiled or folded in patterns due to
formation of hydrogen bonds at regular interval.

Secondary Structure

α - Helix β - Pleated
 α - helix
A delicate right handed coil held together by
hydrogen bonds between every fourth peptide bond.
E.g. Keratin in hair in mammals, myosin,
Tropomyosin.
 β - Pleated
In this structure the
polypeptide chains are held
side by H-bonds resembling
pleated folds of drapery.
The polypeptide chain may be
parallel or antiparallel.
E.g. Keratin protein in skin
(sheets parallel) and silk
protein (fibroin) with
antiparallel sheets.
 Tertiary Structure
It may result from further folding and
coiling like a hollow woollen ball.
It is stabilized by different types of bonds:
 Disulphide bonds (second strongest)
 Hydrophobic bonds
 Ionic bonds other than peptide (strongest)
& Hydrogen bonds.
 It is absolutely necessary for many
biological activities of proteins e.g.
Myoglobin.
 Quaternary Structure
Here, more than one polypeptide
chains are involved to forms a large
multi unit protein. E.g. Haemoglobin.
Human haemoglobin consists of 4
subunits.
Two of these are identical to each
other.
Two subunits of type α and two
subunits of type β together constitutes
the human haemoglobin (HbA).
 Functions of Proteins
Formation of cells and tissues for growth.
Repairing of tissues.
For muscles contraction (e.g. Actin, Myosin)
Formation of hormones (e.g. Insulin)
Formation of enzymes.
 Functions of Proteins
Helps in blood clotting.
For transport (e.g. Hb, transferrin, GLUT-4)
For storage (Myglobin & Ferritin)
For Defence against infections (antibodies)
For support (e.g. Collagen & Elastin)
As artificial sweetener (Monellin) which is considered sweetest.
 Protein Functions
1. Collagen Intercellular ground substances
2. Trypsin Enzymes
3. Insulin Hormone
4. Antibody Fights infectious agents
5. Receptor Sensory reception (smell, taste,
hormones etc.)
6. GLUT – 4 Enables glucose transport into
cells.
L3

Enzymes
They acts as catalysts in biological reactions and
therefore, called Biocatalysts.
These are also known as metabolic regulators.
 Discovery of Enzymes
Buchner, a German biochemist,
discovered enzymes in yeast.
Kuhne coined the term ‘enzyme’ (mean
in yeast).
Summer isolated first enzyme (urease) in
pure crystalline form from jack beans.
 Biochemical Nature of Enzymes
Almost all enzymes are proteins.
There are some nucleic acids that behave like
enzymes.
These are called ribozymes (Ribonuclease-P).
 Biochemical Nature of Enzymes
Enzymes

Simple Enzymes Conjugated Enzymes

Made up of amino acids (Holoenzyme)
only E.g. Pepsin

Protein Part Non Protein Part

(Apoenzyme) (Cofactor)
It determines catalytic activity
It determines structure
 Prosthetic group
and specificity of
 Coenzyme
enzymes
 Metal activator
 Properties of Enzyme Action
MECHANISM OF ENZYME ACTION
Enzymes are required in very small
amount.
These reduce the amount of activation
energy required to start the chemical
reaction.
These cannot change equilibrium point
of a reversible reaction.
Enzyme through their active site,
catalyse reactions at a higher rate.
 Enzyme Action
Site of Enzyme
Action

Intracellular/Endo Extracellular/Exo
enzymes enzymes
Work inside the cell Work outside the cell
e.g. Respiratory Enzymes E.g. Pepsin, Trypsin.
 Iso - Enzymes
These are multiple molecular forms of enzyme occurring
in the same organism and having a similar substrate activity.

α amylase of wheat
endosperm 16 – isoenzymes
Lactic acid
dehydrogenase 5 – isoenzymes
Alcohol dehydrogenase 4 – isoenzymes
 Enzyme Catalysed Reactions
These proceed at rates very higher than that of uncatalysed
ones.
Carbonic Anhydrase

If this reaction takes place in presence of carbonic anhydrase the

reaction speeds with about 600,000 molecules being formed
every second while in absence of enzyme, it produces only 200
molecules in an hour.
 Mechanisms of Enzyme Action
The chemical which is converted to product is called a
substrate.
Enzymes have three dimensional structure
including an active site which convert a substrate(S)
into a product (P).
 Mechanism of Enzymes Action
ES complex is formed when enzyme (E) binds with
the substrate (S).
This complex is transient and unstable.
Soon the substrate is converted to product & is
released from the active site.
After the reaction is over enzymes are free to bind
with fresh substrate.
 Nature of Enzyme Action
Enzyme Substrate Complex
Each enzyme (E) has a substrate (S) binding site in its molecule so
that a highly reactive enzyme – substrate complex (ES) is
produced.
This complex is short – lived and dissociates into its products (S)
P and the uncharged enzyme with an intermediate formation of the
enzyme – product complex (EP).
The formation of the ES complex is essential for catalysis.
E + S  ES  EP  E + P
 Mechanism of Enzyme Action
X – axis represents the progression of the structural
transformation.
Y – axis in this graph represent the potential energy content.
 Mechanism of Enzyme Action
If ‘P’ is at lower level than ‘S’, the reaction is an exothermic
reaction if no external energy in the form of heat us supplied.
Whether the reaction is exothermic or endothermic, ‘S’ has to
go through a much higher energy state or transition state.
The difference in average energy content of ‘S’ from that of
this transition state is called activation energy.
Enzymes decrease the activation energy making the transition
of ‘S’ to ‘P’ more easy.
 Active Site/Substrate Site/Active Spot
It is a specific region in the structure of enzyme to which a
substrate binds.
Active site has a specific type and number of amino acids.
An enzyme can have more than one active site also.
It is a small site and covers nearly 5% of the total area in
most of the enzymes.
 Turn Over Number
The number of substrate molecules which can be catalysed
by a single molecule of an enzyme in a unit time.
Maximum turnover number (36-million mol/minute) is of
carbonic anhydrase.
The turnover number depends upon the number of active
sites.
 Catalytic Cycle of an Enzyme
Substrate binds to the
active site of the enzyme,
fitting into the active site.
Binding of the substrate
induces the enzyme to alter
its shape, fitting more
tightly around the substrate.
 Catalytic Cycle of an Enzyme
Active site of the enzyme, now in close proximity of the
substrate breaks the chemical bonds of the substrate and
the new enzyme – product complex is formed.
The enzyme release the products of the reaction and the
free enzymes is ready to bind to another molecule of the
substrate and run through the catalytic cycle once again.
L4

ENZYME INHIBITION
 Biochemical Nature of Enzymes
Enzymes

Simple Enzymes Conjugated Enzymes

Made up of amino acids (Holoenzyme)
only E.g. Pepsin

Protein Part Non Protein Part

(Apoenzyme) (Cofactor)
It determines catalytic activity
It determines structure
 Prosthetic group
and specificity of
 Coenzyme
enzymes
 Metal activator
Factors Affecting Enzyme Activity
Temperature
Hydrogen ion Concentration (pH)
Substrate Concentration
Product Concentration
Enzyme Concentration
Inhibitors
 Temperature
Enzymes are very sensitive to temperature.
All enzymes are heat sensitive or thermolabile, being
active in narrow range of temperature.
The temperature at which an enzyme shows its highest
activity is called optimum temperature.
Most enzymes operates optimally between 25ᵒ-35ᵒC.
 Temperature
At 0ᵒC Enzymes are temporarily
inactivated.
At 60ᵒC or above Most of the enzymes are
denatured and their
enzymatic activity is lost.

 A general rule of thumb is that reaction rate doubles or decreases by half for
every 10ᵒC change of temperature in either direction.
 Enzymes isolated from organisms who normally live under extremely high
temperatures (e.g. Hot Vents & Sulphur Springs) are stable and retain their
catalytic power even at high temperatures (up to 80ᵒ-90ᵒC).
 Hydrogen ion Concentration (pH)
Enzymes are very sensitive to (pH).
A fall or rise in pH reduces enzyme activity by changing the
degree of ionisation.
Most of the intracellular enzymes function at neutral pH.
Different enzymes have different pH optima.
Pepsin pH – 2
Salivary Amylase pH – 6.8
Trypsin pH – 8.5
 Substrate Concentration
Increase in substrate concentration increase the rate of reaction by

Occupation of more active sites by substrate molecules.

Higher number of collisions between substrate molecules.

 With increase in substrate concentration, rate of reaction increases till the time all
the active sites of all the enzymes are occupied by substrate molecules.
 A stage is reached when enzyme molecules are fully saturated.
 At this stage, initial velocity (Vi) becomes maximum (Vmax).
 Michaelis Menten Constant (Km)
It is the substrate concentration at which the
chemical reaction attains half of its maximum velocity.
Km indicates affinity of enzymes for its substrate.
High Km Value Low affinity
Low Km Value High affinity
 Product Concentration
Accumulation of product in the reaction may lower
the rate of forward reaction by occupying active site
of enzyme.
Reverse reaction my also start.
 Enzyme Concentration
The initial rate of a reaction rises with the increases in
enzyme concentration up to a point called limiting or
saturation point.
Beyond saturation point, increase in enzyme
concentration has little effect.
Enzyme Inhibition
Enzyme Inhibition
Competitive Inhibition
Non-Competitive Inhibition
Feedback Inhibition
 Competitive Inhibition
A chemical, similar in
configuration to the substrate,
competes for the active site of
the enzyme.
E.g. Malonate (Malonic acid)
competes with succinate
(Succinic acid) for the active site
of succinate dehydrogenase.
Malonate is the competitive
inhibitor for the synthesis of
fumarate from succinic acid.
 Methanol Poisoning
Methanol toxicity is similar averted by ethanol, a
competitive inhibitor, for the enzyme alcohol
dehydrogenase.
 Sulfa Drugs
Antibiotics containing sulfa drugs are similar in
structure to PABA (Para-Aminobenzoic acid).
PABA is essential for the growth of many pathogenic
(disease-causing) bacteria.
Sulfa drugs are competitive inhibitors enzyme folic acid
Synthetase.
No change in Vmax, but Km value increases.
Folic Acid Synthetase
PABA ----------------> Folic Acid
 Non – Competitive Inhibition
In this case, the inhibitor does not compete with the
substrate for active site.
It binds with the enzyme at the site other than active site.
The inhibitors changes the configuration of the active site
or the 3-D shape of the enzyme.
 Non – Competitive Inhibition
AchE
• Examples: Acetylcholine ------ > Acetic Acid+Choline
Cyanide stops the functioning of the respiratory enzymes by binding
with the iron of the prosthetic group.
Ions of Heavy metals (like Hg, Ag and Cu) combine with the
disulphide/thiol group and break that to change the 3D shape of the
enzyme, or denature it.
No change in Km value but Vmax decreases.
 Enzyme Inhibition
Allosteric enzymes have allosteric site with the active
site.
The modulator binds to this allosteric site & changes
the rate of chemical reaction.
The inhibitor in such reactions is one of the product of
a long chain of enzymatic reaction.
 Enzyme Inhibition
• Allosteric/Feedback Inhibition
Enzyme phosphofructokinase is activated by ADP
and inhibited by ATP.
Another example is inhibition of threonine
deaminase by isoleucine.
When isoleucine accumulates beyond a threshold, its
further production stops.
L5

CARBOHYDRATES
 Carbohydrates
These are optically active polyhydroxy aldehydes or
ketones or the compounds which produce such units
on hydrolysis.
They contain Carbon, Hydrogen and Oxygen.
In them, ration of hydrogen and oxygen is 2:1 so they
are called hydrates of carbon.
 Carbohydrates
These are the main source of energy for the
body.
These provide 55-65% of energy.
General formula of a carbohydrate is
Cn(H2O)n
n is an integer ranging from 3 to 7.
These are also called saccharides because
their basic components are sugars.
 Carbohydrates
Molecules having the general formula of carbohydrates
but are not carbohydrates:

Formaldehyde (HCHO) – CH2O

Acetic acid (CH3COOH) – C2H4O2
Lactic acid (CH3CHOHCOOH) – C3H6O3
 Carbohydrates
Molecules not having the general formula of
carbohydrates but are carbohydrates:

Deoxyribose (C6H12O5)
Rhamnose (C6H12O5)
Digitoxose (C6H12O4)
 CARBOHYDRATES

Monosaccharide's Derived Oligosaccharides Polysaccharides

Monosaccharides
Monosaccharides
 Monosaccharides
These are simplest carbohydrates which cannot be
hydrolysed further.
General formula of Monosaccharides is Cn(H2O)n.
n is the number of C-atom in a monosugar which
varies from 3 to 7.
C3H6O3
C4H8O4
C5H10O5
C6H12O6
 Types of Monosaccharides

Aldoses Ketoses
These have free aldehyde These have free ketonic
group group
 Types of Monosaccharides
No. of C Formula Aldoses Ketoses
Trioses 3 C3H6O3 Glyceraldehyde Dihydroxyacetone
Tetroses 4 C4H8O4 Erythrose, Threose Erhthrulose
Pentoses 5 C5H10O5 Ribose, Deoxyribose, Ribulose,
Xylose, Arabinose Xylulose
Hexoses 6 C6H12O6 Glucose, Galactose, Fructose
Mannose
Heptoses 7 C7H14O7 Glucoheptose, Galacto Sedoheptulose
Heptose
 Monosaccharides
Pentose and hexoses exist in both chain and ring
form.
 Biomolecules
Ring Form

Pyranose Furanose
It has hexagon structure It has pentagon structure with
with 5 carbons and 1 oxygen. 4 carbons and 1 oxygen.
 α and β Sugars
Furanose and pyranose forms further are
of two types (anomers):
o α Sugars
o β Sugars
In α form, the hydroxyl group near
the oxygen atom of ring (carbon atom
no. 1) is written below.
In β form, the hydroxyl group near the
oxygen atom of ring (carbon atom no.
1) is written above.
 Levorotatory / Dextrorotatory
Forms
Many monosaccharides have asymmetrical
carbons.
These are able to rotate polarised light to
either:
o Right side (d or dextrorotatory).
o Left side (l or Levorotatory).
l, d should bot be confsed with L, D.
L, D refer to relative configuraton of OH group
around the lowest chiral (asymmetric centre).
Important Monosaccharides
Glyceraldehyde Erythrose
Glucose Ribose
Fructose Deoxyribose
Galactose Xylose
Mannose Arabinos
 Glyceraldehyde
Simplest aldehyde sugar.
 Glucose
Main respiratory substrate for all cells.
Dextrorotatory, so called as dextrose.
Present in grapes so also called as grape sugar.
Also called blood sugar/corn sugar.
 Fructose
Sweetest natural occurring sugar.
Levorotatory so also called as laevulose.
Present in human semen secreted by seminal vesicle.
Present in fruits (fruit sugar).
 Galactose
Also known as brain sugar/cerebrose.
Occurs as part of milk sugar lactose.
Found as a component of glycolipids (e.g.
Cerebrosides).
Synthesized in mammary glands to make
lactose of milk.
 Mannose
Not found in free stage.
Occurs in albumin of egg and in wood as a
component of hemicellulose.
 Erythrose
Erythrose 4-phosphate is an intermediate in the pentose
phosphate pathway and the Calvin Cycle.
A chewing gum formulation to fight cavities comprises
sufficient Erythrose to give the chewing gum anti-caries
properties.
Ribose
Important component of RNA, ATP, NAD and NADP

Deoxyribose

Part of DNA.
 Xylose
It is derived from hemicellulose.
It is found in the embryos of most edible plants.
D-xylose is a sugar widely used as diabetic
sweetener in food and beverage.
 Arabinos
It gets its name from gum Arabic,
from which it was first isolated.
It is an inhibitor of sucrose enzyme
that breaks down sucrose into glucose
and fructose in the small intestine.
The L-arabinose operon, also known
as the araBAD operon, has been the
subject of much biomolecular research.
Derived Monosaccharides
Deoxyribose Sugar
Amino sugar
Sugar acids
Sugar alcohol
 Deoxyribose Sugar
These are formed by Deoxygenation where hydroxyl group
is placed by a hydrogen atom.
Deoxygenation of ribose (at second carbon) produces
Deoxyribose.
 Amino Sugars
Hydroxyl group of sugar is replaced by an amino or
acetylamino group.
E.g. Glycosamine (chitin)and galactosamine
(chondroitin sulphate).
 Sugar Acids
These are produced by oxidation of aldehydic
carbon, terminal hydroxyl carbon or both.
E.g. Glucuronic acid, Galacturonic acid & Ascorbic
acid (Vitamin C).
 Sugar Alcohol
Formed by replacement of –CHO group by –OH.
E.g. Mannitol from mannose & Sorbitol from glucose.
L6

OLIGOSACCHARIDES
 Oligosaccharides
These are small carbohydrates formed by condensation of 2-9
Monosaccharides.

Disaccharides
Trisaccharides
Tetrasaccharides
Pentsaccharides
Hexasaccharides
 Disaccharides
Smallest and commonest oligosaccharides.
Also called double sugars.
Contain 2-monosaccharides units.
E.g. Maltose, Sucrose, Lactose, Trehalose, Cellobiose.
Important Disaccharides
Sucrose
Lactose
Maltose
Trehalose
Trehalose
Cellobiose
 Sucrose
Derived from sugar cane or sugar beat.
Also called as table sugar, cane sugar, beet sugar, commercial
sugar.
Non reducing sugar as it doesn’t a free aldehyde or ketone
group.
Dextrorotatory but after hydrolysis give dextrorotatory glucose
and laevorotatory fructose.
Its hydrolysis brings about a change in rotation from
dextrorotation to laevorotation (invert sugar).
 Lactose
Also called milk sugar.
Least sweet among naturally occurring sugars.
Human milk has high amount of lactose.
Souring of milk is due to conversion of lactose into lactic
acid.
 Maltose
Also called malt sugar.
Present in germinating seed.
Intermediate compound in starch digestion.
 Trehalose
Present in haemolymph of insects.
 Cellobiose
Obtained from partial digestion of cellulose.
Disaccharides and their Linkage
Disaccharide Unit Unit 2 Bond
Sucrose α Glucose β Fructose α (12) β
Maltose α Glucose α Glucose α (14)
Trehalose α Glucose α Glucose α (11)
Cellobiose β Glucose β Glucose β (14)
Lactose (Milk Sugar) β Galactose β Glucose β (14)
 Oligosaccharides
Name No. of Units E.g. Units
Trisaccharides 3 Raffinose Glucose + fructose + galactose
Tetrasaccharides 4 Stachyose Glucose + fructose + 2 galactose
Pentasaccharides 5 Barbascose 2 glucose + fructose + 2 galactose
POLYSACCHARIDES
 Polysaccharides/Glycans
Most commonly encountered carbohydrates in nature.

Contain a large number of Monosaccharides units joined

together by glycosidic linkages.

Right end is called the reducing end and the left end is called
the non-reducing end.
 Polysaccharides
(Glycans)

Homopolysaccharides Heteropolysaccharides
(Homoglycans) (Heteroglycans)
 Homopolysaccharides
Formed by polymerisation of only one type of
Monosaccharides unit.
Depending upon Monosaccharides unit involved,
these can be:

Glucan – Made up of glucose

Fructan – Made up of fructose
Galactan – Made up of Galactose
Araban – Made up of arabinose
 Heterosaccharides
Produced by condensation of either
Monosaccharides derivatives or more than one type
of Monosaccharides unit.
 Polysaccharides
(Glycans)

Food Storage Structural Mucopolysaccharides

Polysaccharides Polysaccharides  Hyaluronic acid
 Heparin
 Starch  Chitin
 Chondroitin sulphate
 Glycogen  Cellulose
 Keratin sulphate
 Inulin  Agar
 Heparan sulphate
 Dermatan sulphate
 Storage Polysaccharides
Carbohydrates like glycogen and starch are easy to
store because of the following advantages.

Chemically non-reactive.
Osmotically inactive.
Stored in bulk.
Storage Polysaccharides
Starch
Glycogen
Inulin
Dextrin
Dextran
 Starch (Amylum)
Main storage polysaccharides of plants.
Most important dietary source for human beings.
High content of starch is found in cereals, tuber, roots and some vegetables.
Forms helical secondary structures.
It can hold iodine molecules in the helical portion.
Starch-iodine is blue in colour.
It consists of two components
o Amylose.
o Amylopectin.
 Amylose
Polymer of 200-1000 D-glucose
Unbranched and spiral chain
compound
Glucose molecules are interlinked by
α (14) glycosidic bond.
It is water soluble compound
It constitutes 15-20% starch.
It gives blue colour with iodine.
Amylopectin
Polymer of 2000-200,000 D-glucose
Branched globular structure.
Branching occurs at every 24-30
glucose units.
α (14) glycosidic bond at linear
chain & α (16) glycosidic bond at
the branch.
It is water insoluble compound
It constitutes 80-85% starch.
It gives red colour with iodine.
 Glycogen
It is present in animals (also called animal starch).
It is branched chain compound and has branching after
8 to 12 glucose units.
It is stored mainly in liver (more), muscles and kidney,
placenta.
It is stored food of many fungi (yeast).
It gives red colour with iodine.
 Inulin
It is a polymer of fructose.
It is found in roots of dahlia, artichoke, sweet potato, onion
and garlic.
It is water soluble polysaccharides.
It is not metabolized in human body and is readily filtered
through kidney, so used in testing of kidney function (GFR).
• Dextrin :
It is an intermediate substance in the digestion of starch and glycogen.
Glucose and maltose are formed by hydrolysis of dextrin.
It also occurs as stored food in yeast and bacteria.

• Dextran :
It is the polymer of glucose produced by microorganism.
They are used as plasma volume expanders in transfusion.
Structural Polysaccharides
Cellulose
Chitin
Agar
 Cellulose
It is most abundant carbohydrates in nature.
It is a fibrous polysaccharides and forms cell wall in plants.
Cellulose molecules have unbranched and linear chains of 6000
or more β-D-glucose.
It forms roughage in human food.
It forms 25 to 50% of wood and about 90% of cotton.
In urochordates, tunicin is present as a covering which is made of
cellulose.
Cellulose does not contain complex helices like starch and hence
cannot hold iodine.
 Cellulose Compounds
Cellulose acetate
Carboxymethyl cellulose
Cellulose nitrate

Used in fabrics, cellulose plastics, shatter proof glass,

cigarette filters.
Added to ice-creams, cosmetics and medicines to emulsify
and give a smooth texture.
Used in propellant explosives.
 Chitin
It is second most abundant organic
substances.
It is polymer of N-acetylglucosamine (NAG).
It is present in the cell wall of fungi (fungal
cellulose).
It forms exoskeleton, mainly in arthropods.
It is soft and leathery, so provides strength and
elasticity.
It hardens due to deposition of proteins and
calcium carbonate.
 Agar
It is a natural component of seaweeds.
It is made up of sulphated Galactose units.
In microbiology, it is used as culture medium.
It is obtained from Gracilaria and Gelidium.
 Mucopolysaccharides
Their building blocks are amino sugars and chemically
modified sugars like glucosamine, N-acetyl galactosamine.
These are commonly known as glycosaminoglycans or
GAG.
These are also present in Bhindi and Isabgol.
Mucopolysaccharides
Hyaluronic acid
Heparin
Chondroitin sulphate
Keratin sulphate
Heparan sulphate
Dermatan sulphate
 Mucopolysaccharides
Hyaluronic acid is found in vitreous humour, umbilical cord, joints and
connective tissue and also as a binding material in animal cell coat (animal
cement).

Heparin is an anticoagulant in blood.

Chondroitin sulphate is a component of cartilage, tendons and bones.

Keratin sulphate is found in costal cartilage and cornea.

Dermatan Sulphate is found in wall of arteries.

L7

LIPIDS
Lipids are non-polymers and strictly are not
macromolecules.
Lipids are esters of fatty acids and glycerol.
Lipids are insoluble in water and soluble in organic
solvents.
Consists of carbon, hydrogen, oxygen and sometimes
nitrogen, sulphur, phosphorus.
 Lipids
Lipids provide more energy than carbohydrates.
Lipids provide maximum amount of metabolic water
and require less space for storage as compared to
carbohydrates.
 Fatty Acids
These are basic components of all lipids.
Organic acids having hydrocarbon chain
that ends in –COOH group.
The carboxyl group is attached to R group.
R group can be methyl or ethyl or higher
number of –CH2 groups (1 carbon to 19
carbons).
Common fatty acids have 16 or 18 carbons.
Most fatty acids have even number of
carbons atoms.
 MCQs Quiz
1. Which of the following glucose transporters is insulin-
dependent? (NEET 2019)
a. GLUT IV b. GLUT I c. GLUT II d. GLUT III
2. Concanavalin A is (NEET 2019)
a. A pigment b. An alkaloid c. An essential oil d. A lectin
 Classification of Fatty Acid (FA)
Saturated Fatty Acid (SFA)
Double bonds absent.
Carbon chain is straight.
Fats containing SFA are called Hard fats
(Butter, Lard, Suet).
Solid at room temperature.
Higher melting point.
Mostly present in animal fats.
Increase blood cholesterol.
Less reactive so cause obesity.
Unsaturated Fatty Acid (UFA)
Double bonds present.
Carbon chain has a bend (Kink).
Fats containing UFA are called oils
(Groundnut oil, Olive oil, Gingelly oil)
Liquid at room temperature.
Lower melting point.
Mostly present in plant fats.
Lower blood cholesterol.
More reactive so gives energy.
 Classification of Fatty Acid (FA)
Saturated Fatty Acid (SFA) Unsaturated Fatty Acid (UFA)
Examples: Examples:
1. Palmitic acid (). It can also be written 1. Oleic acid (1 double bond).
as –-COOH
2. Stearic acid () 2. Linoleic acid (2 double bonds).
3. Arachidic acid () 3. Linolenic acid (3 double bonds).
4. Arachidonic acid (4 double bonds).
 ESSENTIAL FATTY ACIDS
Cannot be synthesized in the animal
body and must be supplied with food to
avoid deficeiency.
E.g. Linoleic acid, Linolenic acid,
Archidonic acid.
NONESSENTIAL FATTY ACIDS
Can be synthesized in the body tissues
so many or may not be present in diet.
E.g. Palmitic acid, Stearic acid, Oleic
acid.
 Types of Lipids

Simple Lipids Compound Lipids Derived Lipids

 MCQs Quiz
3. “Rachandran plot” is used to confirm the structure of
a. RNA b. Proteins c. Triacylglycerides d. DNA
4. The two functional characteristic of sugars are (NEET 2018)
a. Hydroxyl and methyl b. Carbonyl and methyl
c. Carbonyl and phosphate d. Carboxyl and hydroxyl
 Simple Lipids
They are esters of long chain fatty acids with various alcohols.

Glycerides (Neutral fats)

Waxes
 Glycerides (Neutral fats)
3-fatty acids are attached to a C-atom
of glycerol by ester linkage.
Molecules of water are released
during its formation (Dehydration).
Glycerol is also called as trihydroxy
propane.
Neutral fats may be monoglyceride
or diglyceride or triglyceride
depending on number of fatty acids.
 Waxes
Esters of one molecule of fatty acids with
alcohols, higher than glycerol.
Alcohol in waxes have only one hydroxyl
group compared to 3 in glycerol.
They form water insoluble coating on hair
and skin in animals and steams, leaves,
fruits of plants.
They are more resistant to hydrolysis and
important for protection.
Waxes Examples
Beeswax
Lanolin (wool wax)
Cerumen or ear wax
Waxes Examples
Sebum in mammalian skin
Spermaceti in whale
Carnauba on leaves
 MCQs Quiz
5. Which of the following is the least likely to be involved in stabilizing
the three-dimensional folding of most proteins? (NEET 2016)
a. Hydrogen bonds b. Electrostatic interaction
c. Hydrophobic interaction d. Ester bonds
6. Which one of the following statements is wrong? (NEET 2016)
a. Uracil is a pyrimidine b. Glycine is a sulphur containing amino acid.
c. Sucrose is a disaccharide d. Cellulose is a polysaccharide
Compound or Conjugates Lipids
Phospholipids
Sphingolipids
Glycolipids
Lipoproteins
 Phospholipids
They are constructed like a neutral fat
except that in place of fatty acid at
third position, there is a phosphate
group and nitrogen containing base is
attached to phosphate group such as
o Choline found in Lecithin
o Ethanolamine found in Cephalin
These amphipathic molecules form
bimolecular layer in cell membranes.
 Examples of
Phospholipids

Lecithin or Present in cell membrane, egg

phosphatidylcholine yolk, oil seeds and blood

Cephalin or Present in nervous tissue and

phosphatidylethanolamine platelets

It acts as surfactant in lungs

Dipalmitoyl lecithin
and prevents their collapse
 Sphingolipids
They are also present in cell membrane
and are comparable to phospholipids
except that spingosine is present
instead of glycerol.
Spingomyelins are Sphingolipids with
additional phosphate attached to
choline.
These occur in myelin sheath of
nerves.
Cerebrosides possess Galactose as
sugar residue and occur in nerve
membrane.
 Glycolipids
They are similar to Sphingolipids except that
oligosaccharide is bonded to sphingosine
instead of the phosphoric acid.
A & B antigens in ABO system of blood
group.
Gangliosides possess sugar residues glucose,
Galactose, Sialic acid etc.
They influence ion transport and are also
found in grey matter.
Their accumulation causes Tay Sachs
diseases.
 Lipoproteins
It contains lipids and proteins.
These are present in blood, milk & egg yolk.

Chylomicrons
Very low density Lipoproteins (VLDL)
Low density Lipoproteins (LDL)
High density Lipoproteins (HDL)
 MCQs Quiz
7. Which of the following are not polymeric? (NEET 2017)
a. Proteins b. Polysaccharides c. Lipids d. Nucleic acids
8. A non-proteinaceous enzyme is (NEET 2016)
a. Lysozyme b. Ribozyme c. Ligase d. Deoxyribonuclease
 Derived Lipids
They don’t contain fatty acids but have fat like
properties.
They are derived from simple or compound lipids.
Steroids
Chromolipids (Terpenes)
 Steroids
They exhibit cyclopentanoperhydrophenanthrene nucleus.
It is 19 membered cyclic ring.

Steroids
Bile Acids
Anabolic Steroids
 Steroids
Most common steroids
Important component of plasma membrane, brain,
skin and adrenal gland.
Present in animals fats.
Also synthesized in liver.
 Examples of Steroids
Cholesterol.
7-Dehydrocholesterol (Occurs in skin as a
provitamin) transforms into cholecalciferol ie vit D
in presence of sunlight.
Ergosterols (found in cell membrane of fungi and
protozoa).
Coprosterols (found in stools)
 Bile Acids
These are derived from cholesterol (glycocholic acid,
taurocholic acid).
These combine with sodium to form bile salts.
These help in emulsification of fats.

Sodium Glycocholate
Sodium Taurocholate
 Chromolipids (Terpenes)
These are liquid like hydrocarbons formed of isoprene
(C5H8) units.
They contain pigments such as carotenoids.
E.g. Essential oils, camphor. Menthol, carotene,
vitamin A, E, K & natural rubber.
 MCQs Quiz
9. Which of the following biomolecules does have a Phosphodiester bond?
(NEET 2015)
a. Amino acids in a polypeptide. b. Nucleic acids in a nucleotide.
c. Fatty acids in a diglyceride. d. Monosaccharides in a polysaccharides.
10. Which one of the following is a non-reducing carbohydrate? (NEET 2014)
a. Maltose b. Sucrose c. Lactose d. Ribose 5-phosphate
 Functions of Lipids

Food storage (its primary function)

Steroids Hormones
Thermal Insulation
Required for dissolving vitamins A, D, E & K
 Functions of Lipids

Shock Absorption
Soap Manufacturing
Protective layer over skin and membranes
Integral part of cell membranes
Aromatic Oils
 MCQs Quiz
11.The essential chemical components of many coenzymes are
(NEET 2013)
a. Carbohydrates b. Vitamins c. Proteins d. Nucleic acids
12.Uridine, present only in RNA is a (NEET 2013)
a. Nucleoside b. Nucleotide c. Purine d. Pyrimidine
 Conceptual MCQs
1. RNA does not possess
a. Uracil b. Thymine c. Adenine d. Cytosine
2. Which is wrong about nucleic acids?
a. DNA is single stranded in some viruses b. RNA is double stranded occasionally
c. Length of one helix is 45 in B-DNA d. One turn of Z-DNA has 12 bases
3. Adenine is
a. Purine b. Pyrimidine c. Nucleoside d. Nucleotide
4. An enzyme bring about
a. Decrease in reaction time b. Increase in reaction time
c. Increase in activation energy d. Reduction in activation energy
5. In which one of the following groups, all the three are examples of polysaccharides?
a. Starch, glycogen, cellulose b. Sucrose, maltose, glucose
c. Glucose, fructose, lactose d. Galactose, starch, sucrose
6. The enormous diversity of protein molecules is due mainly to the diversity of
a. Amino group on the amino acids
b. R groups on the amino acids
c. Amino acids sequences within the protein molecule
d. Peptide bonds
7. Lipids are insoluble in water because lipid molecules are
a. Hydrophilic b. Hydrophobic c. Neutral d. Zwitter ions
8. If base order in one chain of DNA is “ATCGA” then how many no. of H-bond found in
DNA duplex-
a. 20 b. 12 c. 10 d. 11
9. Which of the following is the example of acidic amino acids?
a. Lysine b. Glutamic acid c. Aspartic acid d. (b) and (c) both
10. Bond between nitrogenous bases in a nucleotide is –
a. H-bond b. Covalent bond c. Phosphodiester bond d. Sulphide bond
11. Ligase enzyme is used for
a. Denaturation of DNA b. Splitting DNA into small bits
c. Joining bits of DNA d. Digestion of lipids
12. Fats in the body are formed when –
a. Glycogen is formed from glucose
b. Sugar level becomes stable in blood
c. Extra glycogen storage in liver & muscles is stopped
d. All of them
13. Chemical enzymes are –
a. Fats b. Carbohydrates c. Hydrocarbons d. Proteins
14. Characteristics features of haemoglobin –
a. Reversible union with oxygen b. Red colour
c. Presence of Cu d. Presence of globulin protein
15. Which one is the most abundant protein in the animal world?
a. Trypsin b. Haemoglobin c. Collagen d. Insulin
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