Biology for Engineers

Module -4

Biomolecules
 The Four Major Macromolecules

All forms of life

has the same
building blocks
and yet the
manifestations
are diverse.

The molecular building blocks of life are made from organic compounds
 Characteristics of Biomolecules
• Biomolecules are the molecules of life; Most of In organic molecules:
these are organic compounds. The core is the carbon skeleton (determines the
• Most of the chemical compounds present in living overall shape of the molecule)
systems always contain carbon and Hydrogen. The length and arrangement of the carbon skeleton.
• Carbon atoms covalently bonded to form straight The kinds and location of the atoms attached to it
chains, branched chains, and ring structures. means the functional groups will determine the
• They are main structural components of cells and specific chemical properties of that molecule.
tissues.
• They participate and control all metabolic reactions.
• Transmits hereditary information as DNA and RNA.
• Biomolecules provide energy for all activities of
living beings.
• They have specific shapes and dimensions.
• Functional groups determines their chemical
properties.
• Biomolecules are polymer molecules and are
constructed from small building block (monomers) .
 Biomolecules are polymers
• Biomolecules are very large molecules –
Macromolecules
• Macro molecules are polymer molecules and are
constructed from small building block (monomers)
molecules.
• Building block (monomers) molecules have simple
structure.

Process of formation of polymers or macromolecules Hydrolysis : breaking of a polymer

is called polymerization or dehydration synthesis.
• Two monomers join together by eliminating one
molecule of water. the reaction involves elimination
of H atom from one monomer and -OH group from
the other.
• Polymers are broken down into monomers via
hydrolysis reactions.
• A polymer is a long molecule consists of many
repeating units of monomers as their building blocks.
Functional groups- types

The compounds of carbon are center to

life on this planet.
All the carbon compounds obtained
from living tissues are known as
biomolecules.
•Functional groups are collections of atoms
that attach the carbon skeleton of an organic
molecule and confer specific properties.
•Each type of organic molecule has its own
specific type of functional group.
•Functional groups in biological molecules
play an important role in the formation of
molecules like DNA, proteins, carbohydrates,
and lipids.
•Functional groups include: hydroxyl, methyl,
carbonyl, carboxyl, amino, phosphate, and
sulfhydryl.
Biomolecules: types
 Carbohydrates: Introduction
• Carbohydrates are compounds of carbon , hydrogen and
oxygen.
• They are known as hydrates of carbon
• Hydrogen and oxygen occur in the ratio of 2:1 similar to
water.
• they are sugars or polymers of sugars or
monosaccharides.
• General formula (CH2O)n
• Chemically carbohydrates are aldehyde or ketone
derivatives of alcohols with more than one -OH group.
• Monosaccharides and disaccharides are commonly
known as sugars.
• They are soluble in water, sweet in taste. considered as
micro molecules that can pass through plasma
membranes whereas polysaccharides are regarded to be
macromolecules.
• Carbohydrates are basic components of food.
• Principal source of energy for all living beings.

Structural isomers- Empirical formula (C6 H12O6), but each has a

different structural formula.

Glucose and fructose are isomers.

 Simple carbohydrates: Monosaccharides
Classification of carbohydrates
On the basis of size
Monosaccharides – (1 sugar molecule) glucose, fructose
Disaccharides - (2 sugar molecules) maltose ,sucrose,
Lactose
Oligosaccharides- (2-10 sugar molecules) Raffinose, pentose
Polysaccharides- (10 or more sugar molecules) starch and
cellulose
Monosaccharides or simple sugars (Mono = single;
Saccharine = sweet, sugar)
• General formula (CH2O)
• No of carbon atoms varies from 3 to 7
• Example of monosaccharides are trioses , tetroses,
pentoses , hexoses.
• Monosaccharide sugars of 5 or more carbon atoms have
cyclic structure.
• Glucose is the most abundant simple sugar
• Serve as basic building block for other
carbohydrates.
• Also called dextrose- found in the sap of
plants, in the human blood stream; it is
called blood sugar.
 Complex carbohydrates : Oligosaccharides
• Oligosaccharides- 2-10 monosaccharide molecules joined together by glycosidic linkage or glycosidic bond.
• Most common are disaccharides formed by the condensation of two molecules of same or different
monosaccharides with the loss of one molecule of water. their empirical formula is C12H22O11. Sucrose(table
sugar), maltose(malt sugar) in plants and lactose(milk sugar) in animals are main disaccharides.

Joining of 2 Monosaccharides by glycosidic bond Disaccharides

 Polysaccharides : classification
Polysaccharides ( Poly= many) - they are macromolecules
Complex sugars
Formed by condensation of large number of
monosaccharides.
Monosaccharide units varies from above 10 to many
thousands.
Examples are cellulose , starch and glycogen.
Based on chemical composition polysaccharides are of
two types:
Homopolysaccharides- polymerization of only one type of
monosaccharide units.
Examples are starch and glycogen for the storage of
glucose in plants and animals respectively.
Cellulose and chitin are structural polysaccharides.
Heteropolysachharides - formed of two or more types of
monosaccharide molecules . example are-
mucopolysaccharides , glycoproteins hemicellulose etc.
Polysaccharides- examples
Polysaccharides are also classified based on
their functions as:
• Storage polysaccharides- which serve as food
reserve.(for example , starch and glycogen.
• Structural polysaccharides- which play role in
formation of cell wall in plants( e.g. cellulose)
and skeleton in animals( e.g. chitin)
Examples of homopolysaccharides
 Examples of Heteropolysaccharides
• These are polysaccharides which are formed of
more than one type of monosaccharide units or
their derivatives.
They include glycosaminoglycans (GAGs) formerly
called mucopolysaccharides.
• Mucopolysaccharides help in lubrication of
ligaments and tendons , form synovial fluid.
• They build strength and flexibility of skin,
connective tissues, and cartilage, bind proteins in
cell walls and store water in interstitial spaces.

• Examples are :- agar, pectin , hyaluronic acid

peptidoglycan ,arabinogalactans, heparin etc.
 Significance/Functions of carbohydrates
• Major source of energy- One of the primary functions of carbohydrates is to provide our body with energy.
Our cells convert carbohydrates into the fuel molecule ATP through a process called cellular respiration.

• Storage- carbohydrates are stored in the body for immediate source of energy.
In plants it is stored as starch and in animals it is stored as glycogen.
• Our body can transform extra carbohydrates into stored energy in the form of glycogen. Several hundred
grams can be stored in our liver and muscles.

• Structural components- in plant cells , carbohydrates (cellulose) constitute the structural framework.

• Some glycoproteins act as hormones.

• Fiber is a type of carbohydrate that promotes good digestive health by reducing constipation and lowering
the risk of digestive tract diseases.
• In general, carbs perform these functions in most people. However, if we are following a low-carb diet or
food is scarce, our body will use alternative methods to produce energy and fuel our brain.
 Protein
• Proteins are large biomolecules and macromolecules that comprise one or
more long chains of amino acid residues.
Peptides (2-20 amino acids)
• Proteins perform a vast array of functions within organisms,
including catalyzing metabolic reactions, DNA replication, responding to
stimuli, providing structure to cells and organisms, and transporting
molecules from one location to another. Polypeptide(20- 100 amino
• Proteins differ from one another primarily in their sequence of amino acids, acids)
which is dictated by the nucleotide sequence of their genes.
• A linear chain of amino acid residues is called a polypeptide. A protein contains Proteins ( >50 amino acids)
at least one long polypeptide. Short polypeptides, containing less than 20
amino acid residues, are rarely considered to be proteins and are commonly
called peptides. The individual amino acid residues are bonded together
by peptide bonds with adjacent amino acid residues.
• Once formed, proteins only exist for a certain period and are
then degraded and recycled by the cell's machinery through the process Proteins are polymers of
of protein turnover( replacement of older proteins as they are broken down amino acids.
within the cell). Different types of proteins have very different turnover rates.
 Amino acids: structure

Central dogma: DNA to RNA to protein

Amino acid: structure

• Proteins are made of long strings of amino acids, which are often
called the "building blocks of life.“
• Amino acids are chemicals that consist of a carbon atom that is
attached to a hydrogen atom, an amine group (a nitrogen atom
bonded with two hydrogen atoms) and an acid group.
• Each amino acid contains another group known as the R group,
which has its own unique hydrocarbon structure. There are 20
amino acids that are essential to bodily functions, eight of which
cannot be manufactured by the human body. That is why proteins
are so important to a person's diet.
Amino acids chain
Peptide bond formation

Amino acid exist as a dipolar zwitterion

The point at which the molecule has equal

positive and negative charges, is called
isoelectric point.at this point amino acid does
not migrate in an electric field.
 Amino acids : types

Histidine and Arginine amino acids are categorized as

semi-essential. They formed in the body but not in
sufficient amount for body requirements especially in
children.
The conditionally Non-essential amino acids are not
Our body makes hundreds of amino acids , but it can’t make usually required in the human diet, but do become
nine of the amino acids we need . we must get them from essential under certain conditions like pregnancy or
the food we eat. adolescent growth.
 Classification of Amino acids
(Amino acids can be classified on the basis of R group)
The levels of structural organization of proteins

Proteins have four levels of organisation

Classification of proteins based on chemical composition
Simple proteins- consist of only amino acids or their
derivatives. These include:
Albumins-water soluble; found in milk , serum albumin in
blood.
Globulins- water insoluble; lactoglobulin in milk.
Histones- water soluble; found in eukaryotic DNA.
Conjugated proteins- consists of simple proteins + some
non protein component. Non protein part is called
prosthetic part. Some examples are:
Nucleoproteins: proteins+ nucleic acids. E.g. Nucleo-
histones.
Glycoproteins – proteins +carbohydrates; e.g.
immunoglobins (antibodies).
Phosphoproteins- proteins+ phosphate containing radical
. e.g. casein of milk.
Chromoproteins- proteins+ pigments; e.g. hemoglobin,
hemocyanin.
Lipoprotein- proteins+ lipids; e.g. high density
lipoproteins, low density lipoproteins.
Metalloproteins- proteins+ metals; e.g. ferritin.
Protein classification: On the basis of overall shape

Fibrous proteins have many

structural functions. For example,
collagen strengthens bones ,
ligaments and tendons and keratin
forms structure of hair and nails and
waterproof the skin.
Globular proteins have metabolic
functions. For example, enzymes
function as catalyst and hemoglobin
transports oxygen.
 Membrane Transport proteins
• The cell membrane separates the cell from the external environment. It is a semipermeable lipid-protein coat existing in all
cell types. The cell membrane contains membrane proteins, providing selective permeability and membrane transport.
These proteins are important to sustaining life, as a cell’s survival depends on its ability to control the different
composition of the extracellular and intracellular environment. Transport proteins, part of the membranes are channel
and carrier proteins.
• Channel proteins are proteins that have the ability to form hydrophilic pores (channels) in cells’ membranes, transporting molecules down
the concentration gradient.
• Carrier proteins are integral proteins that can transport substances across the membrane, both in the direction of and against the
concentration gradient.

Channel protein ; e.g. Aquaporin Carrier protein: e.g. Na+/K+ pump

(Conduct water through the membrane)
 Denaturation of proteins
• The three- dimensional shapes of proteins are dependent on the temperature and chemical
composition of body fluids which in turn are regulated by homeostatic mechanisms.
• If the environment changes , a protein may lose its characteristics shape (secondary, tertiary
and quaternary structure).
• Since denaturation reactions are not strong enough
to break the peptide bonds, the primary structure (sequence of amino acids) remains
the same after a denaturation process.
• Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it
into a random shape.

Denaturation of proteins involves the disruption and possible destruction of both the
secondary and tertiary structures.
• In tertiary structure there are four types of bonding interactions between "side chains"
including:
hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic
interactions. which may be disrupted.
• The factors that affect the denaturation of proteins include: heating ; pH ;detergents;
oxidizing and reducing agents etc.

Therefore, a variety of reagents and conditions can cause denaturation. The most common
observation in the denaturation process is the precipitation or coagulation of the protein.

Denaturation of proteins
 Proteins: Examples

Myoglobin Chaperonin Immunoglobulins

In muscle cells (Antibodies)
Heat shock protein

RuBisCO Hemoglobin Structural proteins

Most abundant protein in the
 Nucleic acids
• A nucleic acid is a chain of repeating monomers called nucleotides.
• Nucleotides are monomeric unit or building blocks of nucleic acids.
Types of Nucleic acids
1. Ribonucleic acid(RNA): is single stranded, in RNA sugar is ribose. It consists of adenine and guanine as
substituted purines and cytosine and uracil as substituted pyrimidines.
2. Deoxyribonucleic acid(DNA): is double stranded. In DNA, the sugar is 2’deoxyribose. It consists of adenine
and guanine as substituted purines and cytosine and thymine as substituted pyrimidines.

MONOMERS: NUCLEOTIDES

Nucleic acids: DNA and RNA

 Structure of a nucleotide
• A nucleotide is an organic molecule that is the building block of
DNA and RNA . Nucleotides are monomers of nucleic acid and are
macromolecules . they also have functions related to cell signaling
, metabolism , and enzyme reactions.

• A nucleotide consists of three units, which are covalently linked.

They are-
• Nitrogenous bases – Purine and Pyrimidine
• Pentose Sugar – Ribose and Deoxyribose
• Phosphate – monophosphate, diphosphate, triphosphate

• Sugar: A nucleotide comprises a pentose sugar. DNA

(Deoxyribonucleic acid) contains deoxyribose sugar and RNA
(Ribonucleic acid) contains a ribose sugar.

• A Nitrogenous base attached with the sugar is called “Nucleoside”.

A nucleotide
• Phosphate: Phosphate is associated with the sugar of nucleoside
by an ester bond with the 5th C hydroxyl group. Nucleotides at
least contain one phosphate group.
 Different components of Nucleic acids

Pentose sugar

Phosphate group

Different nitrogenous bases and their bonding

Phosphodiester bond
 Concept of Nucleoside and Nucleotide
Nitrogenous base Nucleoside Nucleotide
Adenine Adenosine Adenylate
Guanine Guanosine Guanylate
Cytosine Cytidine Cytidylate
Thymine Thymidine Thymidylate
The molecule without the phosphate group is called nucleoside Uracil Uridine Uridylate

Formation of Nucleosides and Nucleotides

Structure of Nitrogenous bases
❖ Adenine
❖ Adenine is a two ringed purine derived nucleobase that has an amino group
attached to the C6 position. In the nucleotide structure it forms a covalent
bond with the ribose/deoxyribose sugar and hydrogen bond with the
adjacent nucleobase, that is either a thymine or uracil.
Other compounds formed by adenine include vitamin B12, adenosine
triphosphate (ATP), nicotinamide adenine dinucleotide (NAD) and flavin
adenine dinucleotide (FAD).

❖ Guanine
❖ Guanine is another two ringed purine derived nucleobase composed of a
fused pyrimidine-imidazole ring system that is conjugated with double
bonds. It forms hydrogen bonds with cytosine in the nucleotide sequence.
Guanine combines with ribose to form guanosine and with deoxyribose to
form deoxyguanosine.

❖ Thymine
❖ Thymine is an organic compound that belongs to the pyrimidine family. It
forms double hydrogen bonds with adenine in the DNA helix. It is also
known as 5-methyluracil because it is methylated at the C5 position in the
molecule. It is not found in RNA strands.

❖ Cytosine
❖ Cytosine is a pyrimidine derived nitrogenous base that has an amino group
at the C4 position. It forms triple hydrogen bonds with guanine in the DNA
helix.
❖ Uracil
❖ Uracil is another pyrimidine derived nitrogenous base that is only found in
RNA molecules in place of thymine. It is a demythlated form of thymine
that is substituted with oxo groups at C2 and C4.
 Ribonucleotides and Deoxyribonucleotides

• Adenylate( Adenosine-5’- monophosphate) • Deoxy adenylate (Deoxyadenosine-5’-monophosphate)

• Guanylate(Guanine-5’-monophosphate) • Deoxy guanylate ( Deoxyguanosine-5’-monophosphate)
• Uridylate (Uridine-5’- monophosphate) • Deoxy thymidylate( Deoxythymine-5’-monophosphate)
• Cytidylate (Cytidine-5’-monophosphate) • Deoxy cytidylate (Deoxycytidine-5’-monophosphate)
Primary structure of DNA
Nucleotides are covalently linked by
phosphate group in which the 5’-phosphate
group of one nucleotide unit is attached to
the 3’hydroxyl group of the next nucleotide.
Forming a phosphodiester linkage.
Secondary structure of DNA
Various bonds are present in the Nucleic acids
CHARGAFF’s RULE: This rule states that there is a
1:1 ratio of purines (A,G) to pyrimidines(T,C).
This is true because A binds with T and G binds
with C.
(%A +%T) + (%G+%C)= 100%

Hydrogen bonds: between nitrogenous

bases
Phosphodiester bond
 RNA World
• RNA is a ribonucleic acid that helps in the synthesis of proteins in our body. This nucleic acid is responsible for the
production of new cells in the human body. It is usually obtained from the DNA molecule. RNA resembles the same as that
of DNA, the only difference being that it has a single strand unlike the DNA which has two strands and it consists of an only
single ribose sugar molecule in it. Hence is the name Ribonucleic acid. RNA is also referred to as an enzyme as it helps in
the process of chemical reactions in the body.
The basic structure of RNA is shown in the figure-

• The ribonucleic acid has all the components same to that of the DNA with only 2 main differences within it. RNA has the
same nitrogen bases called the adenine, Guanine, Cytosine as that of the DNA except for the Thymine which is replaced by
the uracil. Adenine and uracil are considered as the major building blocks of RNA and both of them form base-pair with
the help of 2 hydrogen bonds.
 RNA Types
• RNA Types: There are various types of RNA, out which most well-known and
most commonly studied in the human body are :
tRNA – Transfer RNA
• The transfer RNA is held responsible for choosing the correct protein or the
amino acids required by the body in-turn helping the ribosomes. It is located
at the endpoints of each amino acid. This is also called as soluble RNA and it
forms a link between the messenger RNA and the amino acid.
rRNA-Ribosomal RNA
• The rRNA is the component of the ribosome and are located within the
cytoplasm of a cell, where ribosomes are found. In all living cells, the
ribosomal RNA plays a fundamental role in the synthesis and translation of
mRNA into proteins. The rRNA is mainly composed of cellular RNA and are
the most predominant RNA within the cells of all living beings.
mRNA – Messenger RNA.
• This type of RNA functions by transferring the genetic material into the
ribosomes and pass the instructions about the type of proteins, required by
the body cells. Based on the functions, these types of RNA is called the
messenger RNA. Therefore, the mRNA plays a vital role in the process of
transcription or during the protein synthesis process.
RNA TYPES
• Comprises only 5%of the RNA in the cell . all members of the class function
as messengers carrying the information in a gene to the protein synthesizing
machinery.
 Difference between different types of RNA
Genetic RNA:- In the absence of DNA, sometimes
RNA functions as genetic material from one
generation to another, e.g. TMV,QB
bacteriophage.

Non- Genetic RNA

 Functions of Nucleotide
• Besides being the basic unit of genetic material for all
living things , a nucleotide can have other functions as
well.
• A nucleotide can be a base in another molecule ,
such as adenosine triphosphate (ATP), which is the
main energy molecule of the cell.
• They are also found in coenzymes like NAD and NADP,
which come from ADP; these molecules are used in
Structure of ATP
many chemical reactions that play roles in
metabolism.

• Another molecule that contains a nucleotide is cyclic

AMP (c-AMP), a messenger molecule that is
Cyclic adenosine monophosphate
important in many processes including the regulation
of metabolism and transporting chemical signals to
cells.

• Nucleotides not only make up the building blocks of Coenzymes NAD and NADP
life, but also form many different molecules that
function to make life possible.
 Lipids
• Lipids tend to be hydrophobic, nonpolar, and made up mostly of
hydrocarbon chains, though there are some variations are there. Monoglycerides: 1 attached fatty acids
Diglycerides: 2 attached fatty acids
• The different varieties of lipids have different structures, and Triglycerides: 3 attached fatty acids
correspondingly diverse roles in organisms. For instance, lipids store
energy, provide insulation, make up cell membranes, form water-
repellent layers on leaves, and provide building blocks for hormones like
testosterone.
• Fats are just one type of lipid, a category of molecules united by their
inability to mix well with water.
• fat molecule consists of two kinds of parts: a glycerol backbone and
three fatty acid tails. Glycerol is a small organic molecule with three
hydroxyl (OH) groups, while a fatty acid consists of a long hydrocarbon
chain attached to a carboxyl group.
• A typical fatty acid contains 12–18 carbons, though some may have as
few as 4 or as many as 36.
• To make a fat molecule, the hydroxyl groups on the glycerol backbone
react with the carboxyl groups of fatty acids in a dehydration
synthesis reaction. This yields a fat molecule with three fatty acid tails
bound to the glycerol backbone via ester linkages (linkages containing an
oxygen atom next to a carbonyl, or C=O, group).
• Triglycerides may contain three identical fatty acid tails, or three different
fatty acid tails (with different lengths or patterns of double bonds).
Formation of triglycerides
 Saturated and unsaturated fatty acids
• Saturated and unsaturated fatty acids
• The three fatty acid tails of a triglyceride need not be identical
to each other. Fatty acid chains may differ in length, as well as in
their degree of unsaturation.
• If there are only single bonds between neighboring carbons in
the hydrocarbon chain, a fatty acid is said to be saturated. (The
thing that fatty acids are saturated with is hydrogen; in a
saturated fat, as many hydrogen atoms as possible are attached
to the carbon skeleton.)
• When the hydrocarbon chain has a double bond, the fatty acid is
said to be unsaturated, as it now has fewer hydrogens. If there is
just one double bond in a fatty acid, it’s monounsaturated, while
if there are multiple double bonds, it’s polyunsaturated.
• The double bonds in unsaturated fatty acids, like other types of
double bonds, can exist in either a cis or a trans configuration. In
the cis configuration, the two hydrogens associated with the
bond are on the same side, while in a trans configuration, they
are on opposite sides (see below). A cis double bond generates
a kink or bend in the fatty acid, a feature that has important
consequences for the behavior of fats.
 Trans fats: partial hydrogenation
• Saturated fatty acids tails are straight, so fat molecules with fully saturated tails can pack tightly against one another. This
tight packing results in fats that are solid at room temperature (have a relatively high melting point). For instance, most of
the fat in butter is saturated fat.
• In contrast, cis-unsaturated fatty acid tails are bent due to the cis double bond. This makes it hard for fat molecules with
one or more cis-unsaturated fatty acid tails to pack tightly. So, fats with unsaturated tails tend to be liquid at room
temperature (have a relatively low melting point) – they are what we commonly call oils. For instance, olive oil is mostly
made up of unsaturated fats.
• Trans fats
• At this point, you may be noticing that I’ve left something out: I didn’t say anything about unsaturated fats
with trans double bonds in their fatty acid tails, or trans fats. Trans fats are rare in nature, but are readily produced in an
industrial procedure called partial hydrogenation.
• In this process, hydrogen gas is passed through oils (made mostly of cis-unsaturated fats), converting some – but not all –
of the double bonds to single bonds. The goal of partial hydrogenation is to give the oils some of the desirable properties
of saturated fats, such as solidity at room temperature, but an unintended consequence is that some of the cis double
bonds change configuration and become trans double bonds. Trans-unsaturated fatty acids can pack more tightly and are
more likely to be solid at room temperature. Some types of shortening, for example, contain a high fraction of trans fats.
• Partial hydrogenation and trans fats might seem like a good way to get a butter-like substance at oil-like prices.
Unfortunately, trans fats have turned out to have very negative effects on human health. Because of a strong link
between trans fats and coronary heart disease, the U.S. Food and Drug Administration (FDA) recently issued a ban
on trans fats in foods, with a three-year deadline for companies to remove trans fats from their products.
 Omega-3 and omega-6 fatty acids
• Omega fatty acids
• Another class of fatty acids that deserves mention includes the omega-
3 and omega-6 fatty acids. There are different types of omega-3 and
omega-6 fatty acids, but all of them are made from two basic precursor
forms: alpha-linolenic acid (ALA) for omega-3s and linoleic acid (LA) for
omega-6s.
• The human body needs these molecules (and their derivatives), but
can't synthesize either ALA or LA itself.
• Accordingly, ALA and LA are classified as essential fatty acids and must
be obtained from a person’s diet. Some fish, such as salmon, and some
seeds, such as chia and flax, are good sources of omega-3 fatty acids.
• Omega-3 and omega-6 fatty acids play a number of different roles in the
body. They are precursors (starting material) for the synthesis of a
number of important signaling molecules, including ones that regulate
inflammation and mood.
• They are involved in the synthesis of the prostaglandin hormones that
are necessary in controlling cell growth and specialization.
• Omega-3 fatty acids in particular may reduce the risk of sudden death
from heart attacks, decrease triglycerides in the blood, lower blood
pressure, and prevent the formation of blood clots.
Functions and sources of omega-3 and omega-6 fatty acids
 Significance of fats
Roles of fats
• Fats have received a lot of bad publicity, and it’s true Functions of lipids
that eating large amounts of fried foods and other
“fatty” foods can lead to weight gain and cause health
problems. However, fats are essential to the body and
have a number of important functions.
• For instance, many vitamins are fat-soluble, meaning
that they must be associated with fat molecules in order
to be effectively absorbed by the body. Fats also provide
an efficient way to store energy over long time periods,
since they contain over twice as much energy per gram
as carbohydrates(9 calories versus 4 calories).
• Fats in animals provide protection from heat loss, they
additionally provide insulation for the body.
• Fat around some organs (eyes , heart and kidneys )
cushion the organs from physical damage.
• Like all the other large biological molecules, fats in the
right amounts are necessary to keep your body (and the
bodies of other organisms) functioning correctly.
 Phospholipids
• Cells are surrounded by a structure called the plasma membrane,
which serves as a barrier between the inside of the cell and its
surroundings.
• Specialized lipids called phospholipids are major components of the
plasma membrane. Like fats, they are typically composed of fatty acid
chains attached to a backbone of glycerol. Instead having three fatty
acid tails, however, phospholipids generally have just two, and the third
carbon of the glycerol backbone is occupied by a modified phosphate
group.
• Different phospholipids have different modifiers on the phosphate
group, with choline (a nitrogen-containing compound) and serine (an
amino acid) being common examples. Different modifiers give
phospholipids different properties and roles in a cell.
• A phospholipid is an amphipathic molecule, meaning it has a Formation of the phospholipids
hydrophobic part and a hydrophilic part. The fatty acid chains are
hydrophobic and do not interact with water, whereas the phosphate-
containing group is hydrophilic (because of its charge) and interacts If a drop of phospholipids is placed in water, it
readily with water. may spontaneously form a sphere-shaped
structure known as a micelle, in which the
• In a membrane, phospholipids are arranged into a structure called a hydrophilic phosphate heads face the outside
bilayer, with their phosphate heads facing the water and their tails and the fatty acids face the interior of this
pointing towards the inside. This organization prevents the structure. Formation of micelle is energetically
hydrophobic tails from coming into contact with the water, making it a favored.
low-energy, stable arrangement.
 Steroids
• Steroids are another class of lipid molecules, identifiable by their
structure of four fused rings. Although they do not resemble the
other lipids structurally, steroids are included in lipid category
because they are also hydrophobic and insoluble in water.
• All steroids have four linked carbon rings and several of them, like
cholesterol, also have a short tail. Many steroids also have an –OH
functional group attached at a particular site (cholesterol) ; such
steroids are also classified as alcohols, and are thus called sterols.
• Cholesterol, the most common steroid, is mainly synthesized in
the liver and is the precursor to many steroid hormones. These
include the sex hormones testosterone and estradiol, which are
secreted by the gonads (testes and ovaries). Cholesterol also
serves as the starting material for other important molecules in
the body, including vitamin D and bile acids, which aid in the
digestion and absorption of fats from dietary sources. It’s also a
key component of cell membranes, altering their fluidity and
dynamics.

cholesterol is also found in the bloodstream, and blood levels of

cholesterol are what we often hear about at the doctor’s office or in
news reports. Cholesterol in the blood can have both protective
effects (in its high-density, or HDL, form) and negative effects (in its
low-density, or LDL, form) on cardiovascular health.
Progesterone
Classification of lipids based on their chemical composition

Examples of each type of lipids

Thank you for your attention and cooperation.