BIOMOLECULES

Living beings contain a wide variety of organic compounds, besides the ubiquitous water, and
other inorganic compounds. Major organic molecules present in the living beings are:
Carbohydrates, proteins, lipids and nucleic acids. The biomolecules are these unique compounds,
which are responsible for the origin, evolution and maintenance of life. These compounds are
synthesized by the cell machinery through pathways that are unique to living beings.
MAJOR COMPOUNDS IN LIVING BEINGS

Major
Organic compound Building block Examples
functions

Glucose,
Monosaccharide -
fructose
Energy
Lactose,
Oligosaccharide Monosaccharide storage,
CARBOHYDRATES sucrose
physical
Starch,
structure
Polysaccharide Monosaccharide chitin,
cellulose
Enzymes,
toxins, Antibodies,
PROTEIN Amino acid
physical pili, fimbriae
structure
Energy
storage,
LIPID Fatty acids & alcohol Fat, oil
thermal
insulation
Ribonucleotide Membrane
NUCLEIC ACID DNA, RNA
Deoxyribonucleotide stability
 CARBOHYDRATES
 Carbohydrates are aldehyde/ketone derivatives of polyhydroxy alcohols.
 Carbohydrates are also known as saccharides since many of the small molecular weight
carbohydrates have a sweet taste.
 Etymologically meaning hydrates of carbon, carbohydrates are principally composed of
carbon, hydrogen and oxygen. Some of the carbohydrates contain nitrogen and sulphur also in
addition to carbon, hydrogen and oxygen.
 They are the most abundant class of biomolecules and are widely distributed in plant and
animal tissues.
 Carbohydrates are represented by the formula: Cx(H2O)y i.e. H &O are in 2:1 ratio.
 They constitute only 1 to 2 percent of cell mass.

Functions of Carbohydrates:
1. Carbohydrates provide the body with a source of fuel and energy that is required to
carry out daily activities and exercise.
2. Carbohydrates spare protein so that protein can concentrate on building, repairing, and
maintaining body tissues instead of being used up as an energy source.
3. Carbohydrate is necessary for the regulation of nerve tissue and is the ONLY source of
energy for the brain.
4. Fibre, which is also a form of carbohydrate, is essential for the elimination of waste
materials and toxins from the body and helps to keep the intestines disease-free and
clean.
5. They occur as food reserves in plants (starch) & in liver and muscles of animals
(glycogen)
6. They serve as skeletal structures in plants (cellulose), insects & crustaceans (chitin).
Monosaccharides are important constituents of nucleic acids, coenzymes, flavoproteins
etc.
7. They are important in regulation of fat metabolism for normal oxidation of fats.
 How do carbohydrates give us energy?
As carbohydrates are digested and broken down by the body, they are converted into glucose
(blood sugar), which is then used or stored as energy.
If the glucose is not needed immediately, it will be stored in a person's liver and muscles as
glycogen, which is the storage form of glucose. When the body then needs some extra
energy, it will turn to the glycogen reserves and convert them into energy.

Classification of Carbohydrates

Carbohydrates are classified according to molecular size and solubility. In general, the smaller
molecules are more soluble than the larger ones. Carbohydrates are usually classified as:
1. Monosaccharides
2. Oligosaccharides
3. Polysaccharides
Monosaccharides
 Called as simple sugars as they cannot be further hydrolysed into smaller units
 General formula: Cn(H2O)n
 They may have 2-8 carbon atoms
 They can be classified as aldoses or ketoses, depending on whether they contain
aldehyde or ketone group respectively e.g: glucose is an aldose and fructose is a ketose
sugar.
 Based on the number of carbon atoms they possess, the carbohydrates can be divided as:
 Except for fructose, ketoses are not as common as aldoses. The most abundant
monosaccharide in nature is D-glucose.

TYPE FORMULA EXAMPLE

Diose C2H4O2 Glycolic aldehyde
Triose C3H6O3 Glyceraldehyde (aldose) & dihydroxyacetone(ketose)
Tetrose C4H8O4 Erythrose(aldose) & erythrulose (ketose)
Pentose C5H10O5 Ribose (aldose) & Ribulose (ketose)
Hexose C6H12O6 Glucose (aldose) & Fructose (ketose)
Heptose C7H14O7 Glucoheptose (aldose) & Sedoheptulose (ketose)
Glucose, a 6-carbon sugar (hexose) is the sugar in our blood. Fructose, the sugar that
sweetens fruit, and galactose, the sugar found in milk, have the same chemical formula as
glucose and are therefore isomers of glucose.

D- Glucose

The common monosaccharides have cyclic structures: in aqueous solutions all monosaccharides
with 5 or more carbon atoms in the backbone occur more predominantly in a cyclic form in
which carbonyl group has formed covalent bond with oxygen of hydroxyl group along the chain.
The formation of these ring structures is the result of a general reaction between alcohols and
aldehydes or ketones to form derivatives called hemiacetals or hemiketals.

Reaction between the

aldehyde group at C-l and
Formation of the two
the hydroxyl group at C-5 cyclic forms of D-glucose
forms a hemiacetal linkage
producing either of two
stereo isomers the
Alpha and beta anomers
which differ only in this
stereo chemistry around the
hemiacetal carbon, These
six-membered ring
compounds are called
pyranoses because they
resemble the six-membered ring compound pyran. The systematic names for the two ring forms
D-Glucose are α-D-glucopyranose and β-D-glucopyranose. Aldoses also exist in cyclic forms
having five membered rings,which, because they resemble the five membered ring compound
furan, are called furanoses. However, the six-membered aldopyranose ring is much more stable
than the aldofuranose ring and predominates in aldohexose and aldopentose solutions. Only
aldoses having five or more carbon atoms can form pyranose rings (The interconversion of alpha
and beta anomers is called mutarotation).

Isomeric forms of monosaccharides that differ only in their configuration about the
hemiacetal or hemiketal carbon atom are called anomers.

Two monosaccharides are linked together by glycosidic bond which is formed by the loss of
one molecule of water.

Oligosaccharides
 They are compound sugars that yield 2-10 molecules of monosaccharides on hydrolysis.
 Oligosaccharides yielding 2 molecules of monosaccharide are designated as disaccharide
and the one yielding 3 molecules of monosaccharide as trisaccharide and so on.
 General formula of disaccharides: Cn(H2O)n-1, trisaccharides: Cn(H2O)n-2 ,
tetrasaccharides: Cn(H2O)n-3 and so on.

TYPE EXAMPLE
Disaccharide Sucrose (glucose+fructose), lactose (glucose+galactose), maltose, trehalose
Trisaccharide Raffinose(glucose+galactose+fructose), rabinose
Tetrasaccharide Stachyose(2 galactose+1 glucose+ 1 fructose)
Pentasaccharide Verbascose

Raffinose, stachyose, verbascose can be found in beans, cabbage, brussels sprouts, broccoli,
asparagus, other vegetables, and whole grains. They can be hydrolyzed to D-galactose and sucrose by
the enzyme α-galactosidase, an enzyme not found in the human digestive tract. In the lower intestine,
they are fermented by gas-producing bacteria which make carbon dioxide, methane, and/or hydrogen
-- leading to the flatulence commonly associated with eating beans and other vegetables
Polysaccharides
 These are also compound sugars and yield more than 10 molecules of monosaccharides
on hydrolysis.
 They can be further classified as:
o Homopolysaccharides
1. Made up of same type of monosaccharides.
2. E.g: glycogen, inulin, cellulose, pectin, chitin, starch
Starch has 2 components- amylose and amylopectin
Amylose is made of linear chains of D-glucose linked by α- 1,4 glycosidic bonds
Amylopectin is composed of linear chains of D-glucose linked by α- 1, 4 glycosidic bonds.
These chains are inturn joined by α- 1, 6 bonds.

o Heteropolysaccharides
1. Yield different types of monosaccharides on hydrolysis
2. E.g.: hyaluronic acid- found in tissues such as eye, joints, umbilical cord,
chondroitin- found in cartilage, heparin- found in liver
Carbohydrates are also found in the following forms:
 Amino sugars – one hydroxyl group is replaced by amino group e.g: glucosamine
 Sugar acids – e.g. D-gluconic acid, galacturonic acid
 Sugar phosphates – e.g. glucose-6-phosphate, fructose-6-phosphate

Starch Found in grains, roots, vegetables and legumes. It is made up of many (up to 1000)
glucose units. Humans can digest it. One only needs to cook
and chew the plant cells to break open the cellulose walls. Enzymes release the individual
glucose units, which are absorbed into the blood stream.

Glycogen The storage form of carbohydrates in man and animals and is the primary source of
glucose and energy. Muscle glycogen is used directly as
energy. Liver glycogen may be converted to glucose and carried by the blood to the tissues for
their use.

Cellulose Made up of many glucose molecules and is the supportive framework of plants.
Cellulose cannot be digested by humans. Therefore, it provides bulk to the stool. Cellulose is a
type of fiber.
 PROTEINS

The name protein (Gk: first rank) was first suggested by Berzelius (1838)
They are complex organic nitrogenous molecules found in the cells of
living beings, consisting of one or more chains of amino acids. The
constituent elements of proteins are; carbon, hydrogen, oxygen, nitrogen
and rarely sulphur.

Amino acids
 Building blocks of proteins
 Each amino acid has an acidic carboxyl group(-
COOH) and a basic amino group (-NH2)
 Amino acid units are linked together by peptide
bond to from a peptide chain
 If a peptide chain is made up of more than 10 amino acids, it is a
polypeptide

Properties

1. Amino acids are usually colourless

2. Taste –Amino acids have a range of tastes varying from tasteless
(tyrosine), sweet (glycine) to bitter (arginine)
3. They are Crystalline solids. Shape of crystals – slender(tyrosine),
hexagonal(cysteine) able to etc.
4. Soluble in water meanwhile, they only dissolve sparingly in organic
solvents, and the extent of their solubility depends on the size and
nature of the side chain.
5. Amino acids feature very high melting points - up to 200-300°C.
6. Zwitterions
The amine and carboxylic acid functional groups found in amino
acids allow them to have amphiprotic properties. Carboxylic acid
groups can be deprotonated to become negative carboxylates
(−COO− ), and α-amino groups can be protonated to become
 positive α-ammonium groups (+NH3−). At pH between 2.2 and 9.4,
the α-amino acids contain a negative carboxylate and a positive α-
ammonium group, so has net zero charge. This molecular state is
known as a zwitterion. Amino acids also exist as zwitterions in the
solid phase.
7. Proteins have a very large size measured in
Daltons(Da).
8. Colloidal
9. Amphoteric
10. Denaturation
Refers to the loss of biological activity in
protein which is brought about by physical
agents (shaking, heat treatment, high
pressure) or chemical agents (X rays,
alcohol, acetone, sodium dodecyl sulphate
etc.)
It is a process in which proteins lose the
quaternary, tertiary and secondary structure which is present in
their native state. If proteins in a living cell are
denatured, this results in disruption of cell activity
and possibly cell death.

Structure of proteins
Various types of chemical bonds are involved in a protein:
1. Peptide bond
Principal linkage found in all proteins
2. Disulphide bond
Covalent bond formed between sulphahydryl groups of two
cysteine residues
3. Hydrogen bond
Interaction in which hydrogen (H) bound to a
highly electronegative atom, such as nitrogen (N), oxygen (O)
or fluorine(F) shares electrons with another electronegative atom
4. Hydrophobic bond
Some R groups attached to amino acids are hydrophobic. These
hydrocarbon sidechains form close association to resulting in a
relatively strong bond.
5. Ionic bond
Interaction between ions having dissimilar charge.

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There are four basic structural levels of organization of proteins based
on the degree of complexity of the molecule

 Primary Structure
Refers to the sequence of amino acids in the polypeptide chain. The main
mode of linkage in the polypeptide chain is the peptide bond which links
the α - carboxyl group of one amino acid to α - amino group of the other.

 Secondary Structure
Secondary structure refers to particularly stable
Arrangements of amino acid residues giving rise to recurring
structural patterns. Two main types of secondary structures
are present depending on the nature of H
bonding:The alpha helix (intramolecular) and the beta
strand or beta pleated sheet (intermolecular).

α - Helix
 Polypeptide chain is wound around
an imaginary axis to form a right-
handed coiled or spiral conformation
 The "backbone" of the peptide forms
the inner part of the coil while the
side chains extend outward from the
coil.
 Depends on intramolecular H bonding
 Eg: keratin
β - pleated sheet
 In this structure, individual protein chains are aligned side-by-side
into a zig zag structure.
 The protein chains are held together by intermolecular hydrogen
bonding
o Parallel
All the N-terminals of successive
strands are oriented in the same
direction; this orientation may be
slightly less stable
Eg: pectate lyase enzyme

o Antiparallel

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 The successive β strands alternate so that the N-terminus of
one strand is adjacent to the C-terminus of the next. This is
the arrangement that produces the strongest inter-strand
stability
Eg: silk fibroin protein

 Tertiary Structure
Refers to three-dimensional structure of a single protein
molecule.Involves folding of alpha-helices and beta-sheets. This structure
is stabilised by a variety of bonds – disulphide linkages, hydrogen bonds,
hydrophobic interactions, ionic interactions

 Quaternary Structure
Quaternary structure is the three-dimensional structure of a multi-
subunit protein (multimer) and how the subunits interact with each
other. It is stabilized by the same non-covalent interactions and disulfide
bonds as the tertiary structure. Complexes of two or more polypeptides
(i.e. multiple subunits) are called multimers.
Eg: hemoglobin is the oxygen carrying protein in blood which is made of
4 polypeptide chains and four heme prosthetic groups.

 Other secondary structures : Triple helix

Found in collagen which is an important part of connective tissues. It contains three
helical polypeptide chains which wind around each other to form a superhelix. The
superhelical twisting is right handed though each chain is left handed.

 α keratin is found in the skin and appendages such as hair, nails, feathers. The
polypeptide chain is a right handed helix. Three helical strands wrap together into a
superhelix called protofibril, which is left handed.

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CLASSIFICATION OF PROTEINS

I. Based on chemical composition

(1) Simple proteins:
When hydrolysed, simple proteins yield only amino acids. They include
the following groups:
(a) Albumins:
 Examples are lacto albumin found in milk and serum albumin
found in blood.
(b) Globulins:
 Examples are lactoglobulin found in milk, serum globulin, legumin
(c) Glutelins:
 Glutenin from wheat, oryzenin from rice are examples.
(d) Prolamines:
 They include gliadin from wheat and zein from corn.
(e) Scleroproteins:
 Examples are keratin found in hair and nails, collagen which is
found in connective tissue and fibroin in silk.
(f) Histones:
 Occur in association with nucleic acids
(g) Protamines:
 Examples of protamines are salmine (in salmon) and sturine (in
sturgeons)

(2) Conjugated proteins:

These consist of simple proteins in combination with non-protein
component. called prosthetic groups. Conjugated protein includes the
following groups:
(a) Nucleoproteins:(Protein + nucleic acid).
 Nucleoproteins are proteins in combination with nucleic acids.
 Some Nucleoproteins are combinations of nucleic acids with
protamine. Nuclehistones are combinations of nucleic acids with
histones.
(b) Glycoproteins/ Mucoproteins: (Protein+Carbohydrate)
 Glycoproteins are proteins linked to mucopolysaccharides
(carbohydrate) like hyaluronic acid, chondroitin.
 Examples: Follicle Stimulating Hormone (FSH)
(c) Phosphoproteins (Protein+phosphate):
 Phosphoproteins are proteins in combination with phosphoric acid.

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  Examples are casein of milk and vitelline in eggs.
(d) Chromoproteins:
 These are proteins in combination with a proshetic group that is a
pigment.
 Examples are haemoglobin, rhodopsin, flavoproteins and
cytochromes.
(e) Lipoproteins:
 These are proteins conjugated with lipids.
 Examples: lecithin.
(f) Metalloproteins:
 These are proteins conjugated to metal ion like Fe, Co, Mn, Zn.
 Examples: enzymes

(3) Derived proteins:

These proteins are formed by degradation of simple & conjugated
proteins. It includes primary derived proteins – obtained by slight change
in properties and secondary derived proteins – formed by progressive
hydrolysis.
Examples – peptones, proteose

II. Based on shape

a. Globular proteins – consist of polypeptide chains which are
tightly folded into compact spherical or globular shape. They
are soluble in water. Eg: enzymes, hormones
b. Fibrous proteins – consist of polypeptide chains arranged in
long strands. They are insoluble in water. Eg: keratin,
fibroin, collagen, elastin

FUNCTIONS
1) Structural proteins: these are major structural components in the
cell. Eg: keratin – found in hair, nails, feathers; fibroin – in silk
fibres

2) Transport proteins: these proteins bind to specific molecules &

transport them from one tissue to another. Eg: hemoglobin,
cytochromes

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3) Storage proteins: These proteins act as storage or reserves for
amino acids or metal ions. Eg: casein, ovalbumin – reserve for
amino acid; ferritin – reserve for iron

4) Motile/ Contractile proteins: These proteins enable cells to

contract and move about. Eg: actin & myosin help in muscle
contraction

5) Catalytic proteins: These proteins possess catalytic activity and

catalyse reactions in the cell. Eg: enzymes

6) Protective proteins: These proteins defend organisms against

invasion. Eg: antibodies (immunoglobulins), fibrinogen, proteins in
snake venom

7) Regulatory proteins: These proteins help in regulation of cellular

activities. Eg: hormones (ACTH, TSH)

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 LIPIDS

 The term lipid refers to a group of compounds that are esters of

long chain fatty acids.
 These result from the combination of a
fatty acid with an alcohol.
 They are soluble in organic solvents such
as chloroform, ether, benzene etc. and
insoluble in water and polar solvents.
 As lipids are insoluble in aqueous
medium, they are transported in blood as
lipoprotein complexes which form water soluble micelles.
 This group includes waxes, terpenes, steroids, acyl glycerols etc.

CLASSIFICATION OF LIPIDS
1. Simple Lipids
 Also called as homolipids
 They are esters of fatty acids with alcohols
 Includes fats, oils and waxes
o FATS : these are esters of fatty acids with glycerol
They are generally solids at room temperature
Example – butter, tallow, lard

o OILS : these are esters of fatty acids with glycerol

They are generally liquids at room temperature
Example – Olive oil, peanut oil, sunflower oil

o WAXES : these are esters of fatty acids with long chain

alcohols (24 – 36 carbon atoms). Waxes are of common
occurrence in both plants and animals.

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 Example – beeswax, spermaceti, paraffin wax, suberin in
the endodermis of root, sebum in the hairs of mammals,
cerumin in the wax glands of ear

2. Conjugated lipids
 Also known as heterolipids
 These are lipids, which contain an inorganic or organic
group in addition to fatty acids and alcohol.
 They are of following types:
o Phospholipids - These are lipids containing a phosphate
group.
A phospholipid molecule has a strongly nonpolar and
hydrophobic (water insoluble) tail region represented by
fatty acid chains and a strongly polar or hydrophilic
(water soluble) head region represented by the phosphate
group. Due to this property, a phospho-lipid placed in
water forms a lipid bilayer in a characteristic manner.
Example–phosphatidylcholine, phosphatidylethanolamine

o Glycolipids
These are lipids containing a carbohydrate group,

15
 usually galactose. They are found in the nerve cell
membranes especially in the myelin sheath.
Example – gangliosides, cerebrosides
o Sphingolipids are lipids containing a core of an amino
alcohol called
sphingosine.
Example –
Ceramides,
Phytoceramide,
Sphingomyelins

3. Derived lipids
 These are products of
hydrolysis of simple &
conjugated lipids
 Eg: fatty acids, steroids, terpenes etc.
 Important steroids include cholesterol & ergosterol

FATTY ACIDS
 A fatty acid is an organic acid with a long hydrocarbon chain
ending in a carboxyl (COOH) group.
 They contain a carboxyl group (hydrophilic) and long nonpolar
hydrocarbon tail (hydrophobic).
 Most naturally occurring fatty acids have an even number of
carbon atoms ranging between 14 to 22
 The hydrocarbon tail may be saturated or unsaturated.
 A fatty acid is described as SATURATED if there are no double
bonds between carbons of the molecular chain, i.e. the carbon
atoms are filled/ saturated with hydrogens.

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 For example, lauric acid (12 carbon)Palmitic acid (16 carbon) and
stearic acid (18 carbon).
They are found more in fats & are solid at room temperature.
 A fatty acid is described as UNSATURATED if one or more double
bonds occur between the carbon atoms of the chain.

Example - oleic acid, linoleic acid, linolenic acid (18 carbon)

They are found more in oils & are liquids at room temperature.
 Unsaturated fatty acids are of different types based on the number
of double bonds:
o Monoethenoid – oleic acid
o Diethenoid – linoleic acid
o Triethenoid – linolenic acid
o Tetraethenoid – arachidonic acid

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Essential fatty acids, or EFAs, are fatty acids that humans
and other animals must ingest because the body requires them
for good health but cannot synthesize them.
Polyunsaturated fatty acids (PUFAs) are fatty acids that
contain more than one double bond in their
backbone. This class includes many important
compounds, such as essential fatty acids.
Examples of PUFA - linoleic acid, linolenic acid,
arachidonic acid Monoacylglycerol
.
ACYL GLYCEROLS / GLYCERIDES
 Glycerides or acylglycerols, are esters formed from glycerol and
fatty acids.
 Glycerol has three hydroxyl functional groups, which can be
esterified with one, two, or three fatty acids to form
monoglycerides, diglycerides, and triglycerides respectively.
 Vegetable oils and animal fats contain mostly triglycerides
 Mono & diglycerides do not occur in nature and are formed as
intermediates in the metabolism of lipids. Diacylglycerol

BIOLOGICAL IMPORTANCE OF LIPIDS

1. Major source of energy; 1g of fat yields 9 kcal of energy which is
twice the energy available from oxidation of 1g of carbohydrate.
2. On oxidation, triacyl glycerols yield more water which is useful for
hibernating animals and camels.
3. It is used as stored food in the adipose tissue, abdominal cavity
and mammary glands.

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 4. It serves as insulation against low temperatures. Warm blooded
polar animals such as seals, walruses, penguins are padded with
triacyl glycerols.
5. Lipoproteins form structural components of cell membranes and
mitochondria.
6. Lipids act as vitamin carriers for fat soluble vitamins.
7. Squalamine is a lipid from sharks which is antibiotic in nature.
8. Fats are usually found deposited around vital organs like heart,
lungs etc. which protects them from mechanical pressure.

PROPERTIES OF LIPIDS
1. Physical State: saturated fatty acids are solid at room
temperature whereas unsaturated fatty acids are liquid at
room temperature.
2. They are colourless, odourless, and have a bland taste.
3. Sparingly soluble/ insoluble in water.
4. Saponification - a process by which triglycerides are reacted
with an alkali (usually sodium or potassium hydroxide) to
produce glycerol and a fatty acid salt
5. Rancidity - Rancidification, the product of which can be
described as rancidity, is the chemical decomposition of fats,
oils and other lipids leading to the development of
unpleasant odour & taste.

Oxidative rancidity is associated with the degradation by

oxygen in the air.

Microbial rancidity - refers to a process in which

microorganisms, such as bacteria, use their enzymes such
as lipases to break down fat.

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