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Module 4

Biomolecules are essential organic molecules crucial for the maintenance and metabolic processes of living organisms, categorized into four major classes: carbohydrates, proteins, nucleic acids, and lipids. Carbohydrates, including monosaccharides, disaccharides, and polysaccharides, serve various functions such as energy storage and structural components in cells. Proteins, composed of amino acids, play vital roles in metabolism, movement, and cellular communication.

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0% found this document useful (0 votes)
22 views47 pages

Module 4

Biomolecules are essential organic molecules crucial for the maintenance and metabolic processes of living organisms, categorized into four major classes: carbohydrates, proteins, nucleic acids, and lipids. Carbohydrates, including monosaccharides, disaccharides, and polysaccharides, serve various functions such as energy storage and structural components in cells. Proteins, composed of amino acids, play vital roles in metabolism, movement, and cellular communication.

Uploaded by

Rishabh Singh
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Module 4

BIOMOLECULES
❖ Carbohydrate
❖ Protein
❖ Nucleic acid
❖ Lipid
❖ 2-carbon units

1
BIOMOLECULES
▪ Biomolecules are the most essential organic molecules, which are involved in the maintenance
and metabolic processes of living organisms.
▪ They range from small molecules such as primary and secondary metabolites and hormones to
large macromolecules like proteins, nucleic acids, carbohydrates, lipids etc.
▪ There are four major classes of Biomolecules: Carbohydrates, Proteins, Nucleic acids and Lipids.
Each of them is discussed below.

Micromolecules Macromolecules
Small molecules with relatively low molecular weight. Large, complex molecules composed of repeating subunits
(monomers).
Molecular Weight less than 1,000 Da (Daltons). Molecular Weight above 1,000 Da, often reaching millions of
Daltons.
Highly solubility Low solubility
• Water (H₂O): 18 Da • Proteins (e.g., Haemoglobin): ~64,500 Da
• Glucose (C₆H₁₂O₆): ~180 Da • DNA (per base pair): ~650 Da; entire genome can be
• Amino acids (e.g., Glycine): ~75–204 Da millions to billions of Da
• Acetyl-CoA: ~809 Da • Polysaccharides (e.g., Glycogen): Hundreds of
• Fatty acids (e.g., Palmitic acid): ~256 Da thousands to millions of Da
• Lipids (e.g., Phospholipids in membranes): Varies; some
complex lipids are >1,000 Da 2
CARBOHYDRATES

• Carbohydrates form a very large group of


naturally occurring organic compounds which
play a vital role in daily life.
• Carbohydrates (hydrates of carbon) are
naturally occurring compounds having general
formula Cx(H2O)y.
• They are produced in plants by the process of
photosynthesis.
• The most common carbohydrates are glucose,
fructose, sucrose, starch, cellulose etc.
• Chemically, the carbohydrates may be defined
as polyhydroxy aldehydes or ketones or
substances which give such molecules on
hydrolysis.
• Many carbohydrates are sweet in taste and all
sweet carbohydrates are called as sugars.
• The chemical name of the most commonly used
sugar in our homes is sucrose.
3
BIOLOGICAL IMPORTANCE OF CARBOHYDRATES

• Glucose is the source of storage of


energy. It is stored as glycogen in animals
and starch in plants.
• Ribose and deoxyribose sugars forms the
structural frame of the genetic material,
RNA and DNA.
• They form structural and protective
components, like in cell wall of plants and
microorganisms.
• In animals they are important constituent
of connective tissues.
• They participate in biological transport,
cell-cell communication and activation of
growth factors.

4
CLASSIFICATION OF CARBOHYDRATES

5
MONOSACCHARIDES

• A polyhydroxy aldehyde or ketone


which cannot be hydrolyzed further to a
smaller molecule containing these
functional groups, is known as a
monosaccharide.
• About 20 monosaccharides occur in
nature and glucose is the most
common amongst them.
• Monosaccharides are further classified
on the basis of the number of carbon
atoms and the functional group present
in them. If a monosaccharide contains
an aldehyde group , it is known
as an aldose and if it contains a keto
group , it is known as a ketose.

6
GLUCOSE

➢ Glucose is an aldohexose and occurs in both free and combined forms in nature.
➢ It is present in honey and sweet fruits.
➢ Also, glucose is present in large amounts in ripe grapes, so it is known as grapes sugar.
➢ Glucose is the unit of starch, cellulose and glycogens.

Preparation of Glucose

1. From Sucrose (Cane sugar): Fructose and glucose


are obtained in equal amounts when sucrose is boiled
with dil. HCl or H2SO4 in alcoholic solution.

2. From Starch: Glucose is obtained commercially by the


hydrolysis of starch by boiling it at 393 K with dil. H2SO4.

7
STRUCTURE OF GLUCOSE
Fischer projection Cyclic structure Haworth projection

•The D-glucose is dextro glucose,


which has an optical rotation towards • Pyranose structure is a six-
the right side, meaning it is membered cyclic structure of
dextrorotatory. • α-D(+) Glucose: The a-form of
glucose (α– or β–), in analogy with
glucose (m.p. 419 K) is obtained by pyran.
•The L-glucose is levo glucose, which crystallization from concentrated
has an optical rotation towards left side, • Pyran is a cyclic organic compound
solution of glucose at 303 K. with five carbon atoms and one
meaning it is levorotatory. • β-D(+) Glucose: The b-form (m.p.
oxygen atom in the ring.
•L and D glucose are non- 423 K) is obtained by crystallization • α-D-glucose: The hydroxyl group on
superimposable mirror images of each from hot and saturated aqueous C1 is below the plane of the ring.
other and are called enantiomers. The solution at 371 K. • β-D-glucose: The hydroxyl group on
levo form is the enantiomer of the C1 is above the plane of the ring.
dextro form of glucose. 8
FRUCTOSE
• Fructose is an important ketohexose. Cyclic structure
• It also has the molecular formula
C6H12O6.
• It is obtained along with glucose by
the hydrolysis of disaccharide,
sucrose.
• It is a natural monosaccharide found
in vegetables, fruits and honey.
• In its pure form it is used as a
sweetener.

Fischer projection Haworth projection


The ring has an analogy to the compound furan and is a five-membered ring. It
is a five membered cyclic compound with one O and four C atoms.

9
COMPARISON OF GLUCOSE AND FRUCTOSE

Property Glucose Fructose


Molecular formula C6H12O6 C6H12O6
Nature Polyhydroxy aldehyde Polyhydroxy ketone
Ring Pyran Furan
Melting point 146°C 102°C
Optical nature Dextro rotatory Levo rotatory
Solubility Less water soluble Most water-soluble
compared to fructose sugar of all the sugars

10
DISACCHARIDES

• By the loss of a water molecule, an oxide linkage is formed,


which joins two monosaccharides.
• These two monosaccharides are held together by glycosidic
linkage (oxide linkage) through oxygen atom.
• The reducing groups (aldehydic or ketonic) of
monosaccharides are bonded in disaccharides. Therefore, these
are non-reducing sugars, e.g., sucrose.
• Whereas sugars in which these reducing groups are free,
which are called reducing sugars, for example, lactose and
maltose.

• The small intestine breaks


down lactose into glucose
and galactose, which are
then absorbed into the
bloodstream.
• People who are lactose
intolerant can't digest
lactose.
11
SUCROSE MALTOSE LACTOSE

• One of the common disaccharides is • Another disaccharide, maltose • It is more commonly known
sucrose which on hydrolysis gives is composed of two a-D- as milk sugar since this
equimolar mixture of D-(+)-glucose glucose units in which C1 of disaccharide is found in milk.
and D-(-) fructose. one glucose (I) is linked to C4 of • It is composed of β-D-
• These two monosaccharides are held another glucose unit (II). galactose and β-D-glucose.
together by a glycosidic linkage • The free aldehyde group can be • The linkage is between C1 of
between C1 of α-D-glucose and C2 of
produced at C1 of second galactose and C4 of glucose.
β-D-fructose. Since the reducing
glucose in solution and it Free aldehyde group may be
groups of glucose and fructose are
involved in glycosidic bond shows reducing properties so it produced at C-1 of glucose
formation, sucrose is a non reducing is a reducing sugar. unit; hence it is also a
sugar. reducing sugar.
• Sucrose is dextrorotatory but after
hydrolysis gives dextrorotatory
glucose and levorotatory fructose. 12
POLYSACCHARIDES

• When a large number of monosaccharide units


linked together by glycosidic linkages,
polysaccharides are formed.
• They generally act as the food storage or structural
materials.
• Polysaccharides can be a straight chain of
monosaccharides known as linear polysaccharides,
or it can be branched known as a branched
polysaccharide.

Polysaccharides have the following properties:


1.They are not sweet in taste.
2.Many are insoluble in water.
3.They are hydrophobic in nature.
4.They do not form crystals on desiccation.
5.They are high molecular weight carbohydrates.
6.Inside the cells, they are compact and osmotically
inactive.
13
STARCH
• It is the main storage polysaccharide of plants.
• High content of starch is found in some vegetables, roots, tubers and cereals hence, it is the most important dietary
source for human beings.
• It is a polymer of alpha- glucose and consists of two components—Amylopectin and Amylose.

Amylose Amylopectin

• Amylose constitutes about 15-20% of starch and is • Amylopectin constitutes about 80- 85% of starch and is not
water soluble component. soluble in water. y In it, a chain is formed by C1–C4 glycosidic
• Amylose is formed chemically formed by 200- 1000 a-D- linkage, while branching occurs by C1– C6 glycosidic linkage.
(+)-glucose units held together by C1–C4 glycosidic • It is formed by the branched-chain polymer of a-D-glucose units
linkage, forming long unbranched chain. 14
CELLULOSE

• Cellulose is found only in plants


and is the most abundant organic
substance in the plant kingdom.
• It is a major component of the cell
wall of plant cells, helping plants
remain stiff and upright
• Cellulose is a straight-chain
polysaccharide made up entirely
of β -D glucose units linked
together by a glycosidic linkage
between C1 of one glucose unit
and C4 of the next glucose unit.
• It's the most abundant
biopolymer on Earth .

15
COMPARISON OF CARBOHYDRATES

16
PROTEIN

• Proteins are very large molecules composed of basic


units called amino acids.
• Proteins contain carbon, hydrogen, oxygen, nitrogen,
and sulphur.
• They are the most abundant biomolecules of the living
system. Chief sources of proteins are cheese, milk,
pulses, peanuts, etc.
• Proteins are highly complex molecules that are actively
involved in the most basic and important aspects of life.
These include metabolism, movement, defense, cellular
communication, and molecular recognition.
• Proteins account for more than 50% of the dry mass of
most cells.
• The monomers (building units) of proteins are amino
acids.
• Cells use 20 amino acids to make thousands of
proteins.
17
AMINO ACIDS

Classification of Amino Acids


• Amino acids are carboxylic acids having
an –NH2 group. When the –NH2 group is On the basis of relative no. of carboxyl and amino groups in their
at α-position these are called α-amino molecule, they are classified as acidic, basic or neutral.
acids. 1. Neutral : Equal number of carboxyl and amino groups makes it
• Amino acids can be categorized as α, β, δ, neutral
γ, and so on, it depends on the relative 2. Basic : More number of amino than carboxyl groups makes it
position of amino group with respect to basic
carboxyl group. 3. Acidic : More carboxyl groups as compared to amino groups
• Only α -amino acids are obtained on makes it acidic
hydrolysis of proteins. They also can
contain other functional groups. 1. Non-essential Amino : They are defined as the type of amino
• The property of the compound or its source acids, which can be synthesized in the body. E.g.: alanine, arginine,
are reflected by their trivial names. Glycine asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine,
is so-called as it has a sweet taste, and proline, serine, and tyrosine.
tyrosine (in Greek, tyros means cheese) 2. Essential Amino Acids: They are defined as the type of amino
was first obtained from cheese. acids, which cannot be synthesized in the body and must be obtained
• Amino acids are generally represented by a by the diet. E.g.: histidine, isoleucine, leucine, lysine, methionine,
3-letter symbol, sometimes 1 letter symbol phenylalanine, threonine, tryptophan, and valine.
is also used.
18
Abbreviations for amino acids
Characteristic Features of Amino Acids

• Amino acids are generally colorless, crystalline


solids.
• These are water-soluble and have high melting
point.
• These behave like salts rather than simple amines
or carboxylic acids. This behavior is due to the
presence of both basic (amino group) and acidic
(carboxyl group) groups in the same molecule.
• In aqueous solution, the carboxyl group can lose a
proton and the amino group can accept a proton,
resulting in zwitter ion, a dipolar ion.
• Amino acids exhibit amphoteric behavior in zwitter
Zwitter Ion
ionic form, reacting with both acids and bases.
• Except for glycine, all other naturally occurring
α -amino acids are optically active due to the
asymmetry of the -carbon atom.
• These are available in both 'D' and 'L' forms. The
majority of naturally occurring amino acids have an
L-configuration. The –NH2 group on the left side is
used to represent L-amino acids. 19
PEPTIDE BOND OR PEPTIDE LINKAGE

• Peptides are those amides which are formed due to condensation


between -NH2 group and–COOH group of two different amino acids.
• The –CO–NH– bond is called peptide linkage or bond.
• The >C=O group of an amide is sp2 hybridized with coplanar
structure.
• To eliminate water molecule and form peptide bond —CONH—, the
combination of the amino group of one molecule with the carboxylic
group of other, there is a reaction between two molecules of similar or
different amino acids The product of the reaction is made up of two
amino acids; hence it is termed dipeptide.
• For example, when carboxyl group of glycine combines with the
amino group of alanine we get a dipeptide, Glycylalanine.
• An amino acid unit having a free NH2 group is known as N-terminal
amino acid while an amino acid with a free –COOH group is known as
C-terminal amino acid.
• A tripeptide contains 3 amino acids linked by 2 peptide linkages,
therefore it can be form if a 3rd amino acid combines to a dipeptide.
• When 4, 5 or 6 amino acids are linked, the respective products are
termed as tetrapeptide, pentapeptide or hexapeptide.
• When the no. of such amino acids is more than 10, then the
products are known as polypeptides. 20
CLASSIFICATION OF PROTEINS

(1) Fibrous Proteins: When the polypeptide


chains are held together by H and S2 bonds
and run parallel, then fibre – like structure is
formed. Proteins are generally insoluble in
water and are quite stable against a
moderate change in temperature and pH
value. E.g. : keratin (present in hair, wool,
silk) and myosin (present in muscles), etc.

(2) Globular Proteins: In such proteins, the


polypeptide intramolecular chains get
folded to give a spheroidal shape due to
intramolecular hydrogen bonding, van
der waals forces, dipolar interaction and
disulphide bridging. These are usually
soluble in water and change with a change
in temperature and pH. E.g.: Insulin,
albumins, haemoglobin and antibodies.
21
STRUCTURE OF PROTEINS

Amino acids are joined together by an amide linkage called


peptide bond. Proteins are long polymers of amino acids linked by
peptide bonds (polypeptides).

1. Primary Structure:
• Frederic Sanger gave Primary structure of Insulin for the
first time. Proteins may have one or more than one
polypeptide chains.
• Amino acids of each polypeptide in a protein are joined to
each other in a specific sequence and this sequence is
termed as primary structure of that protein.
2. Secondary Structure:
• By intramolecular H-bonding between the carboxyl and
amino groups there is regular folding of the backbone of
the polypeptide chain which arises secondary structure.
• Secondary structures are found to present in two different
types of structures viz. α-helix and β-pleated sheet
structure.
22
SECONDARY STRUCTURE OF PROTEINS

α-Helix Structure

• α-Helix is one of the most common ways


in which a polypeptide chain forms all
possible hydrogen bonds by twisting into a
right-handed screw (helix) with the –NH
group of each amino acid residue
hydrogen bonded to the >C=O of an
adjacent turn of the helix.
• Stabilization of an α-helical configuration
by hydrogen bonding.
• The alkyl groups of the alpha-helix chain
are not involved in the H bonds but
maintain the alpha-helix structure.
• E.g. : α-keratin in skin and nails, myosin in
muscles, fibroin in silk.
23
β-pleated sheet structure

• In β-pleated sheet structure all peptide chains are stretched out to nearly maximum extension and then laid side
by side which are held together by intermolecular hydrogen bonds.
• β-pleated sheet structure are parallel and anti-parallel type.
• In parallel form all polypeptide chain run in the same direction (Keratin), while in anti-parallel form, the alternate
polypeptide chain run in same direction (fibroin).

24
DIFFERENCES BETWEEN α-HELIX AND β-PLEATED SHEET

α-Helix β-Pleated Sheet


Amino acids exist in the right-handed Amino acids exist in an almost entirely
coiled rod-like structure. extended conformation, i.e. linear or
sheet-like structure.

Intramolecular hydrogen bonding forms Beta sheets are formed by linking two
within the polypeptide chain to create a or more beta strands by intermolecular
spiral structure. hydrogen bonds.

α-Helix can be a single chain β-Sheet cannot be in a single chain


polypeptide. Polypeptide. There must be two or
more beta-strands

Example: Keratin, Myoglobin and Example: Skin Fibres or Fibroin.


Hemoglobin.

25
3. Tertiary Structure:

• The tertiary structure of proteins


represents the folding of the polypeptide
chains or folding of the secondary
structure of proteins.
• Tertiary protein structure can involve
further coiling and folding. The tertiary
structure is made up by different
combinations of alpha helices and beta
pleated sheets.
• Tertiary and secondary structures of
proteins are stabilized by the forces of H-
bonds, disulphide linkages, van der
Waals and electrostatic forces of
attraction.
• It gives rise to 2 major molecular shapes
that is fibrous and globular.
• E.g.: α-keratin, immunoglobulins, collagen

26
4.Quaternary Structure:

• Some of the proteins are composed of more


than one polypeptide chains referred to as
sub-units.
• When these sub-units have spatial
arrangement with respect to each other then
they are termed as quaternary structure.
• The quaternary structure refers to the way in
which simple protein chains associate with
each other resulting in the formation of a
complex protein.
• By different modes of bonding in secondary
and tertiary structural levels a protein molecule
appears to have a unique three-dimensional
structure.
• E.g. : Hemoglobin is an aggregate of four sub-
units, two identical α-chains (having 141 Amino
acid residues and two identical β-chains Quaternary Structure of Hemoglobin
(having 146 Amino acid residues).
27
28
NUCLEIC ACID

• For each and every species, every generation


resembles its ancestors in many ways. For this
transmission of inherent characters nucleus of a
living cell is responsible, which is also termed as
heredity.
• Chromosomes are particles made up of proteins
and another type of biomolecules called nucleic
acids and present in the nucleus of the cell is
responsible for heredity.
• Deoxyribonucleic acid (DNA) and ribonucleic acid
(RNA) are two types of nucleic acids. They are
also called polynucleotides as they are long chain
polymers of nucleotide.
• Nucleic acids contain the elements nitrogen,
carbon, oxygen, phosphorus and hydrogen.
• The Complete hydrolysis of DNA (or RNA) yields
a pentose sugar, phosphoric acid and nitrogen
containing heterocyclic compounds (called
bases).
29
Pentose Sugar Bases

• In DNA molecules, the sugar • The bases that occur in nucleic


moiety is β-D-2- deoxyribose acids are derivatives of pyrimidine
whereas in RNA molecule, it is and purine.
β-D-ribose. • Pyrimidine bases are uracil,
thymine and cytosine.
• The purine bases found in nucleic
acids are adenine and guanine.
• DNA contains 4 bases viz. adenine
(A), guanine (G), cytosine (C) and
thymine (T).
• RNA also contains 4 bases, the
first 3 bases (adenine (A), guanine
(G), cytosine (C)) are same as in
DNA but the fourth one is uracil (U).

30
Chargaff Rule

• In 1955 Erwin Chargaff gave the Chargaff


Rule.
• The rule states that ‘For any given species in
DNA, the ratio of adenine to thymine is equal
to the ratio of cytosine to guanine’. The ratio
is termed as Chargaff’s ratio.
• This rule was important for solving the structure
of DNA.
• Chargaff’s rule: [A] + [G] = [C] + [T]
• DNA from any species of any organism should
have a 1:1 stoichiometric ratio of purine and
pyrimidine bases.

Chargaff’s ule of Base Pairing

• Relation of A with T: The pyrimidine Thymine


(T) always pairs with the purine Adenine (A).
• Relation of C with G: The purine Guanine (G)
always pair with the pyrimidine cytosine (C).
31
STRUCTURE OF NUCLEIC ACIDS

Nucleoside
• Nucleoside is a unit formed by the attachment
of a base to 1 position of sugar.
• Sugar + Base = Nucleoside
• The sugar carbons in nucleosides are labeled
as 1', 2', 3', and so on to differentiate these
from the bases.
Nucleotide
• A nucleotide is formed when a nucleoside is
linked to phosphoric acid by N-glycosidic
bond at the 5'-position of the sugar moiety.
• A nucleotide unit formed by the attachment of a
base 1 position of sugar and attachment of
phosphoric acid with 5 position of sugar.
• Sugar + Base + Phosphoric acid =
Nucleotide
32
• Nucleosides and nucleotides, the pentose
sugar exists in the furanose form,
meaning it adopts a five-membered ring
structure.

N-Glycosidic Bond Formation

• Nucleosides and nucleotides are formed


when a nitrogenous base (either a purine or
pyrimidine) is attached to the pentose sugar
via an N-glycosidic bond.

This bond forms between:


• C-1' of the pentose sugar and N-9 of a
purine base (adenine or guanine) or N-1 of
a pyrimidine base (cytosine, thymine, or
uracil)

33
Phosphodiester Linkage
Nucleotides are joined together by phosphodiester linkage between 5' and 3' carbon atoms of the
pentose sugar.

34
Double stranded helical structure for DNA

• The double strand helix structure of DNA


was proposed by James Watson and
Francis Crick.
• DNA consists of 2 long strands of
polynucleotides coiled around each other in
the form of a double helix (Watson and
Crick model) ladder like structure joint
together by hydrogen bonding.
• Here, hydrogen bonding is in between the
nitrogenous base molecules of the
nucleotide monomer.
• Adenine with thymine forms two hydrogen
bonds while guanine forms three hydrogen
bonds with cytosine.
• Thymine combines only with deoxyribose
sugar while uracil combines with only
ribose sugar.
35
Features of the Watson-Crick model of DNA

• Two helical polynucleotide chains are


coiled around a common axis. The chains
run in opposite directions.
• The sugar-phosphate backbones are on
the outside and, therefore, the purine and
pyrimidine bases lie on the inside of the
helix
• The bases are nearly perpendicular to the
helix axis, and adjacent bases are
separated by 3.4 Å.
• The helical structure repeats every 34 Å,
so there are 10 bases (= 34 Å per
repeat/3.4 Å per base) per turn of helix.
The diameter of the helix is 20 Å.

36
Ribonucleic Acid (RNA)

RNA (ribonucleic acid) is a vital molecule in all living cells. It plays a


key role in carrying genetic information and helping cells make
proteins.
1. What is RNA?
RNA is a nucleic acid, similar to DNA, but with some key differences:
•It is single-stranded (unlike DNA, which is double-stranded).
•It contains ribose sugar instead of deoxyribose.
•It has the nitrogenous base uracil (U) instead of thymine (T).
2. Functions of RNA
RNA is essential for making proteins and has several types, including:
•mRNA (messenger RNA): Carries genetic instructions from
DNA to ribosomes.
•rRNA (ribosomal RNA): Helps form ribosomes, the site of
protein synthesis.
•tRNA (transfer RNA): Brings amino acids to ribosomes to build
proteins.
3. How RNA Works?
1.Transcription: DNA is copied into mRNA.
2.Translation: mRNA directs the ribosome to assemble proteins
using amino acids delivered by tRNA.

37
DNA vs. RNA

38
Functions of DNA

1.Genetic Information Storage: DNA holds the instructions for building and maintaining an organism.
2.Replication: DNA can duplicate itself to pass genetic information to new cells and generations.
3.Gene Expression Regulation: DNA sequences control when and how genes are turned on or off.
4.Mutation and Evolution: Changes (mutations) in DNA contribute to genetic variation and evolution.

Functions of RNA

1.Protein Synthesis: RNA helps translate genetic instructions into proteins (mRNA, tRNA, rRNA).
2.Gene Regulation: Some RNAs (e.g., miRNA, siRNA) help control gene activity.
3.Enzymatic Activity: Certain RNA molecules (ribozymes) act as catalysts in biochemical reactions.
4.Genetic Material in Some Viruses: RNA serves as the genetic material in RNA viruses like SARS-
CoV-2.

39
LIPIDS

• Lipids are organic compounds formed mainly from


alcohol and fatty acids combined together by ester
linkage.
• Lipids are simple fatty acids. Carboxyl group
attached to an R group form fatty acids, it can be ethyl
(–C2H5), or methyl (–CH3) or higher number of –CH2
groups (1 carbon to 19 carbons).
• (i) Palmitic acid has 16 carbons including
carboxyl carbon.
• (ii) Arachidonic acid contains 20 carbon atoms
which includes the carboxyl carbon
• Lipids are insoluble in water, but soluble in fat or
organic solvents (ether, chloroform, benzene, Palmitic acid
acetone).
• Lipids include fats, oils, waxes and related Arachidonic acid
compounds. They are widely distributed in nature both
in plants and in animals

40
Biological Importance of Lipids

1. They are more palatable and more storable to compared to carbohydrates.


2. They have a high-energy value (25% of body needs) and they provide more
energy per gram than carbohydrates and proteins
3. Supply the essential fatty acids that cannot be synthesized by the body.
4. Supply the body with fat-soluble vitamins (A, D, E and K).
5. They are important constituents of the nervous system.
6. Phospholipids are some lipids containing phosphorous and a phosphorylated
organic compound in them. Lecithin is one example. They are found in cell
membrane.

Classification of Lipids

Lipids are classified into three broad categories on the basis of their molecular
structure and the hydrolysis products.
(i) Simple Lipids: Those lipids which are esters and yield fatty acids and alcohols
upon hydrolysis are called simple lipids. They include oils, fats and waxes.
(ii) Compound Lipids: Compound lipids are esters of fatty acids and alcohol with
additional compounds like phosphoric acid, sugars, proteins etc.
(iii) Derived Lipids: Compounds which are formed from oils, fats etc. during
metabolism. They include steroids and some fat-soluble vitamins.
41
Simple Lipids
The simple lipids are esters.
They are subdivided into two groups, depending on
the nature of the alcohol component.
1. Fats and oils (triglycerides):
• They are the esters of glycerol with three
molecules of long chain fatty acids. On
hydrolysis of a triglyceride molecule, one
molecule of glycerol and three molecules of
higher fatty acids.
• By definition, a fat is that triglyceride which is
solid or semisolid at room temperature and an
oil is the one that is liquid at room temperature.
2. Waxes:
• They are the esters of fatty acids with long chain
monohydroxy alcohols 26 to 34 carbons atoms.
• They form a protective coating on the surfaces of
animals and plants.
• Some insects also secrete waxes. The main
constituent of bee's wax obtained from the honey
comb of bees is myricyl palmitate.
42
Compound Lipids

• Compound lipids on hydrolysis yield some other


substances in addition to an alcohol and fatty
acids.
• The first type of such lipids are called
phospholipids, because they are the
triglycerides in which two molecules of fatty
acids and one molecule of phosphoric acid are Glycolipids
present.
• The membranes bounding cells and
subcellular organelles are composed mainly of
phospholipids. Thus, the transfer of substances
through these membranes is controlled by
properties of phospholipids. E.g.: Lecithins,
Plasmalogens, Cardiolipin, etc.
• Glycolipids contain a sugar molecule in addition
to fatty acid attached to an alcohol.

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Phospholipids
Derived Lipids

• Steroids are another class of lipids which are


formed in our body during metabolism. These
are the compounds with a distinctive ring
system that provides the structural backbone
for many of our hormones. E.g.: estrogen,
progesterone.
• Cholesterol is one of the most widely
distributed steroids in animal and human
tissues.
• Another important group of derived lipids is
that of fat-soluble vitamins. This includes
vitamins A, D, E and K, whose deficiency
causes different diseases.
• Terpenes are a large and diverse class of
organic compounds, produced by a variety of
plants, particularly conifers, though also by
some insects such as termites or swallowtail
butterflies, which emit terpenes from their
osmeteria (defensive organ). 44
2-Carbon Unit Biomolecules

Basic Structure
• These biomolecules contain two carbon atoms, often in
a simple chain, usually attached to other elements like
hydrogen, oxygen, or sulfur.
• The two carbon atoms are commonly part of a
hydrocarbon chain or as part of a functional group
(such as a carboxyl group in acetic acid).
Acetic acid
Functional Groups:
• The two carbons are often bonded to:
• Hydrogen (e.g., in acetic acid).
• Oxygen (e.g., in acetyl-CoA, where the carbonyl
group is present).
• Sulfur (in coenzyme A derivatives like acetyl-CoA).

Acetyl-CoA
45
Role in Metabolism

• Building Block for Biomolecule Synthesis:


The 2-carbon unit is a key precursor in the synthesis of a variety of important molecules,
including:
• Fatty acids: Acetyl-CoA contributes to the elongation of the fatty acid chain.
• Cholesterol: Acetyl-CoA serves as a starting point for the biosynthesis of cholesterol.
• Amino acids: Certain amino acids are synthesized using acetyl-CoA or related 2-
carbon units.
• Energy Metabolism:
• Acetyl-CoA enters the Krebs cycle (TCA cycle) to generate energy in the form of ATP
.This is a pivotal step in cellular respiration.
• Fat Metabolism:
• Acetyl-CoA is also involved in fatty acid synthesis and fatty acid oxidation, playing a
critical role in energy storage and release.

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