BIOMOLECULES

T Raghuveer
XII
ORGANIC CHEMISTRY
 BIOMOLECULES INTRODUCTION
Biomolecules are the organic molecules that are involved in the maintenance
and metabolic processes of living organisms. Thus, they build up the living
system and are responsible for their growth and maintenance.

Some of the common biomolecules are:

•• Carbohydrates
•• Proteins
•• Lipids
•• Nucleic acids
•• ATP molecules
 TYPES OF METABOLLITES

Primary metabolites Secondary metabolites

• Key role in growth, development & reproduction • No role in growth, development & reproduction
• Formed during growth phase as a result of energy • Formed towards end of growth phase
metabolism • Ecological importance (drugs, toxins, pigments etc)
• Amino acids, nucleotides, acetic acid, lactic acid, • Rubber, gums, cellulose, carotenoids, morphine,
vitamins erythromycin

Biomolecules are termed as Metabolites.

These Metabolites are converted into each other in a series of linked reactions called metabolic pathways.
There are 2 types of metabolic pathways:
Anabolic pathways Catabolic pathways
• Formation of complex structures from simpler ones • Formation of simpler structures from complex ones
• Biosynthetic pathways • Degradation pathways
• Consume energy • Release energy
 MICRO - MACRO MOLECULES
[Biomolecules can be categorized into two types depending upon their molecular weights]

Biomicromolecules Biomacromolecules

[Molecular weights less than 1000 Dalton] [Higher molecular weights]

• Amino acids • Proteins
• Sugars • Carbohydrates
• Nucleotides • Nucleic acids
• Lipids
• Water
• Minerals
 • Polyhydroxy aldehydes [or] polyhydroxyketones [or]
compounds on hydrolysis give carbohydrates.
CARBOHYDRATES • They are optically active due to the presence of chiral ‘C’.
• They are also called saccharides (From Latin word Saccharum = sugar) due
to sweet taste.

CLASSIFICATION OF CARBOHYDRATES

1. Monosaccharides 2. Oligosaccharides
(a) Simplest carbohydrates (a) Carbohydrates which gives 2 to 10 monosaccharide
(b) It cannot be hydrolysed into simpler units on hydrolysis
compounds (b) Examples – Sucrose, Lactose, Maltose
(c) Examples – Glucose, mannose

3. Polysaccharides
(a) Carbohydrates which on hydrolysis give large number of
monosaccharide units.
(b) Examples – Cellulose, starch
 SUGAR :
Monosaccharides & oligosaccharides are crystalline solids, soluble in water and sweet in taste.

NON SUGAR :
Polysaccharides are amorphous, insoluble in water and tasteless. .

Based upon reducing and non-reducing properties, carbohydrates can be divided

into the following two categories:
F
REDUCING SUGARS
These are the carbohydrates which contain free aldehydic or ketonic group and reduces Fehling's solution or
Tollen's reagent.
example: Maltose, lactose.

NON REDUCING SUGARS

These are the carbohydrates which do not contain free functional group and do not reduce Fehling’s or
Tollen’s reagent.
example: Sucrose.
 ANOMERS
Pair of optical isomers which differ in configuration only around C1 atom
are called anomers.
Examples D-glucopyranose and D-glucopyranose.

EPIMERS
Pair of optical isomers which differ in configurationaround any other C
atom other than C1 atom are called epimers.
Examples D-glucose and D- mannose are C2epimers.

MONOSACCHARIDE • GLUCOSE
S • FRUCTOSE

• SUCROSE
DISACCHARIDES • MALTOSE
• LACTOSE

• STARCH
POLYSACCHARIDES • CELLULOSE
• GLYCOGEN
 MO NOSACC HARIDES GLUCOSE
It is a monosaccharide’s with molecular formula C6H12O6. It is present in sweet
fruits and in honey.
PREPARATION OF GLUCOSE (also called dextrose, grape sugar): STRUCTURE OF GLUCOSE
• Cyclic structure :
FROM SUCROSE :

FROM STARCH :

STRUCTURE OF GLUCOSE
• Open chain structure (Fisher model):

These two optical isomers differ in configuration around any other C atom other than C1 atom.
In D-Glucose, −OH group on first chiral `C’ from the bottom is on right hand.

In L-Glucose, −OH group points to the left of chiral carbon.

CHEMICAL REACTIONS OF GLUCOSE
Reaction with HI : Reaction with hydroxylamine, NH4OH:

j
Reaction with bromine water:
Acetylation reaction :

Oxidation:
Reaction with Fehling’s solution :

f
Reaction with Phenylhydrazine, C6H5NHNH2

Reaction with Tollen’s reagent:

 C HARIDES FRUCTOSE
MO NOSAC
Fructose also has the molecular formula as Glucose C6H12O6
On the basis of its reactions it was found to contain a ketonic functional group at carbon number 2 and six carbons
in straight chain as in the case of glucose.
STRUCTURE OF GLUCOSE STRUCTURE OF GLUCOSE
• Cyclic structure :
2.
1. E

Sucrose (glucose + fructose) present in sugarcane is hydrolysed in presence of enzyme, Sucrase to get one
unit of glucose and one unit of Fructose
 C HARIDES SUCROSE
DISAC
It is one of the common disaccharides, which on hydrolysis gives equimolar
mixture of D (+) -glucose and D (−) fructose.

• Sucrose is a non-reducing sugar, because

the two monosaccharide units are held
together by a glycosidic linkage between C1
of -glucose and C2 of – fructose.
• Since the reducing groups of glucose and
fructose are involved in glycosidic bond
formation, sucrose is a non-reducing sugar.
• Sucrose is dextrorotatory but on hydrolysis it gives dextrorotatory & laevorotatory and
the mixture is laevorotatory.

Haworth Projection of Sucrose

 C HARIDES MALTOSE
DISAC
Maltose is composed of two α-D-glucose units in which C1 of one glucose (I) is
linked to C4 of another glucose unit (II).
The free aldehyde group can be produced at C1 of second glucose in solution and
it shows reducing properties so it is a reducing sugar.

Haworth Projection of Maltrose

 C HARIDES LACTOSE
DISAC
Lactose morecommonly known as MILK SUGAR, as it is found in milk.
It is composed of β-D-galactose and β-D-glucose.
The linkage is between C1 of galactose and C4 of glucose
It shows reducing properties so it is a reducing sugar.
 CC HARI D ES STARCH
POLYSA
It is a polymer of -glucose and consists of two components —
Amylose and Amylopectin
Main sources of starch are wheat, maize, rice, potatoes and barley.
It is a white amorphous powder, in-soluble in cold water.
o AMYLOSE:
• It is a linear polymer of α‒ glucose. It is water soluble and gives blue colour with iodine solution.
• It is a water soluble component
• It is a long unbranched chain polymer
• It contains 200 – 1000 -D-(+)- glucose units held by – glycosidic linkages involving C1 – C4glycosidic
linkage
• It constitutes about 15-20% of starch
o AMYLOPECTIN:
• It is a branched chain polymer of α‒ glucose. It is water in-soluble and does not give blue colour with
iodine solution.It is a water insoluble component
• It is branched chain polymer
• It forms chain by C1 – C4glycosidic linkage whereas branching occurs by C1 – C6glycosidic linkage
• It constitutes about 80-85% of starch
 D ES
CELLULOS
HARI
CC
POLYSA E
Cellulose is a linear polymer of β-glucose. It consists of bundles of polymeric chains which are
held together by hydrogen-bonding.
Main sources of starch are wheat, maize, rice, potatoes and barley.
It is a white amorphous powder, in-soluble in cold water.
• It occurs exclusively in plants.
• It is a straight chain polysaccharide composed only of -D-glucose units which are joined by glycosidic
linkage between C1 of one glucose unit and C4 of the next glucose unit.
• Main sources are wood (45 –50%), cotton (90 – 95%). It is the main constituent of cell walls.
• It is colourless amorphous solid that decomposes on heating.
• It does not reduce Tollen's reagent or Fehling's solution.
• It cannot be digested by human stomach.
• Cell wall of bacteria and plants is made up of cellulose
• Cellulose forms a number of important products, such as:
o Cellotape used for packaging.
o Viscose rayon used in textile industry.
o Gun cotton used as an explosive.
 POLYSA
CC HARI D ES GLYCOGEN

• The carbohydrates are stored in animal body as glycogen.

• It is also known as animal starch because its structure is similar to Amylopectin.
• It is present in liver, muscles and brain.
• When the body needs glucose, enzymes break the glycogen down to glucose.
 AMINO
PROTIENS ACID
All protiens are protiens of α - amino acids
Amino acids contain amino (–NH2) and carboxyl (–COOH) functional groups.

Where R – Any side chain

Most naturally occurring amino acids have L – Config.
• GLYCINE : sweet smell
• TRYOSINE : cheese
ZWITTER FORM OF AMINO ACIDS :
• Amino acids behave like salts rather than simple amines or carboxylic acids.
• This behaviour is due to the presence of both acidic (carboxyl group) and basic (amino group) groups in the same
molecule.
• In aqueous solution, the carboxyl group can lose a proton and amino group can accept a proton, giving rise to a
dipolar ion known as zwitter ion.
• This is neutral but contains both positive and negative charges.
• In zwitter ionic form, amino acids show amphoteric behaviour as they react both with acids and bases.

ISOELCTRONIC POINT :
• The pH at which the dipolar ion exists as neutral ion and does not migrate to either electrode cathode or anode is
called isoelectronic point.
 Types of AMINO ACID
ESSENTIAL AMINO ACID:
The amino acids which cannot be synthesised in the body and must be obtained through diet, are known as essential amino
acids.
Examples: Valine, Leucine

NON- ESSENTIAL AMINO ACID:

The amino acids, which can be synthesised in the body, are known as non-essential amino acids.
Examples: Glycine, Alanine
 α– Helix:

SECODAR
Y It refers to the shape in which
long polypeptide chain can
β– pleated sheet: exist. Two different types of
structures:

PROTEIN TERTIA It represents the overall folding

PRIMARY
STRUCTURE RY of the polypeptide chain i.e.,
further folding of the 2°
structure.
The sequence of amino
acids is said to be the
primary structure of a • Some of the proteins are composedof two or more
protein. polypeptide chains referred to as sub-units.
QUATERNARY
• The spatial arrangement of these subunits with
respect to each other is known as quaternary
structure of proteins.
 Types of bonding which stabilize the 3° structure:

• Disulphide bridge (-S – S-)

• H – bonding – (C = O … H – N)
• Salt bridge (COO– … + )
• Hydrophobic interactions
• van der Waals forces
Protein Folding:
Primary → Secondary → Tertiary

Quaternary Structure of a Protein

Secondary Structure – Alpha Helices versus Beta Pleated Sheets
α– Helix sheet β– pleated sheet
• It was given by Linus Pauling in 1951 • It exists when R group is small.
• It exists when R- group is large. • In this conformation, all peptide
• Right handed screw with the NH chains are stretched out to nearly
group of each amino acid residue H – maximum extension and then laid
bonded to – C = O of adjacent turn of side by side which are held together
the helix. by hydrogen bonds.
• Also known as 3.613 helix since each
turn of the helix hasapproximately
3.6 amino acids and a 13 –
membered ring is formed by H –
bonding.
• C = O and N – H group of the peptide
bonds are trans to each other.
• Ramchandran angles (and) – angle
which makes with N – H and angle
which makes
with C = O.
 ENZYMES
• These are biocatalysts.
• Most of them are globular protein
• Enzyme and substrate together form the ES complex
• Enzyme changes its shape slightly as the substrate binds
• EP complex is formed
• Products leave the active site of enzyme
• Enzyme is free again to bind to another substrates
• hey facilitate biochemical reactions inside the body of living organisms
• They lower the activation energy for a reaction
• Their shapes determine their functions
• They are highly selective in nature
• Mostly, enzymes are proteins; however some nucleic acids behave like
enzymes, called Ribozymes
• Enzymes are named after compounds/ class on which they act
• Names end with ‘ase’
• Example: The enzyme ‘Maltase’ acts on Maltose sugar to convert it to
Glucose
 Different types of Enzymes

• Oxidoreductases Catalyse oxidation reduction between 2 substrates

• Transferases Transfer group from one substrate to another

• Hydrolases
• Cause hydrolysis, breaking larger molecules into smaller ones
• Most digestive enzymes are Hydrolases
• Lyases
Maltose à Glucose + Glucose
Break covalent bonds

• Isomerases Catalyse rearrangement of molecular structures to form isomers

• Ligases Linking covalent bond between substrates to form a large molecule
 Alanine Arginine Asparagene Glycene
• Non-essential • Semiessential amino acid • Non-Essential Amino • Non-Essential Amino Acid
amino acid • Iinfants are unable to Acid • This is the smallest amino acid
• Symbol: Ala synthesize it , therefore are • This was the first • Name is derived from the
• Non-polar, neutral externally provided to them amino acid to be term ‘Glyco’ meaning sweet,
• CH3CH(NH2)COOH through Fish, chocolates isolated. Since it was as it tastes sweet
• Good for heart diseases and isolated from • Symbol: Gly
speedy recovery of wound Asparagus, hence • Non-polar, neutral
named Asparagene • NH2CH2COOH
• Symbol: Asn
• Polar, neutral
• C 4H 8N 2O 3
 RNA DNA COMPOSITION OF NUCLEIC ACID
Single stranded structure Double stranded structure
S

Phosphate ribose forms the Phosphate deoxyribose

backbone forms the backbone
H

Bases involved are: Adenine, Bases involved are: Adenine,

Guanine, Cytosine, Uracil Guanine, Cytosine, Thymine
• Complete hydrolysis of DNA (or RNA) yields
Adenine (A) pairs with Uracil Adenine (A) pairs with
(U) Thymine (T) • A pentose sugar
H
• Phosphoric acid
Guanine (G) pairs with Guanine (G) pairs with
Cytosine (C) Cytosine (C) • Nitrogen containing heterocyclic compounds called
Y

Helps in Polypeptide Specify order of amino acids

bases
synthesis in a polypeptide • Nitrogenous bases exit in 2 forms:
YH

Purine – double ring

Convey genetic information, Store genetic information,
cannot self replicate has capacity to duplicate • 2 versions: Adenine, Guanine
Pyrimidine – single ring
• 3 versions: Cytosine, Thymine, Uracil
THYMINE ADENINE URACIL GUANINE

CYTOSINE
FIBROUS PROTEIN GLOBULAR PROTEIN
• Insoluble in water • This globular proteins generally have a more
• When polypeptide chain run parallel and are compact and rounded shape and have functional
held together by hydrogen and disulphide roles .
bonds, then fibre - like structure is formed.
• Exmples : keratin and myosin
 DENATURATION
• Denaturation is a structural change in a protein that results in the loss (usually permanent) of its biological
properties
• Because the way a protein folds determines its function, any change or abrogation of the tertiary structure will
alter its activity
• Denaturation of proteins can usually be caused by two key conditions – temperature and pH

Temperature
• High levels of thermal energy may disrupt the hydrogen bonds that hold the protein together
• As these bonds are broken, the protein will begin to unfold and lose its capacity to function as intended
• Temperatures at which proteins denature may vary, but most human proteins function optimally at body temperature (~37ºC)
pH
• Amino acids are zwitterions, neutral molecules possessing both negatively (COO–) and positively (NH3+) charged regions
• Changing the pH will alter the charge of the protein, which in turn will alter protein solubility and overall shape
• All proteins have an optimal pH which is dependent on the environment in which it functions (e.g. stomach proteins require an
acidic environment to operate, whereas blood proteins function best at a neutral pH)
 USES OF DNA TYPES OF RNA
• DNA sequence is unique for an individual and
RNA helps in protein synthesis.
cannot be altered.
Three types of RNA exist which together help in protein synthesis:
• Due to this, it can be used in:
1. Identifying dead bodies
2. Forensic lab
3. Determining paternity

Messenger RNA (m-RNA) Ribosomal RNA (r-RNA) Transfer RNA (t-RNA)

• Convey information Central component of Recognize sequence of
from DNA to ribosome amino acids, and based
ribosome on that proteins are
• Genetic information is formed
encoded in nucleotide
sequence arranged in
codon (sequence of three
DNA or RNA nucleotides like
CAG, AGC etc..)
• Each codon
represents an amino
acid
 NUCLEOTIDES BOND
Nucleotides are joined together by
phosphodiester linkage between 5′ and 3′
carbon atoms of the pentose sugar. The
formation of a typical dinucleotide

Nucleic acid chain

 • Lipids are Heterogeneous organic compounds.
LIPIDS • They contain Carbon, hydrogen, less amount of oxygen, phosphorus, nitrogen, sulphur
• These are Water insoluble; therefore they form part of membranes that divide water
components in the body

• Energy storage in the form of Oils & fats

• Structural roles in Cell membrane
FUNCTIONS PERFORMED • Messenger (steroid hormones)
BY LIPIDS
• Constituents of Plants pigments chlorophyll, carotene etc, Wax, rubber, Vitamins A, E, K
• Fat acts as an insulator that conserves body heat in animals
• Fat underneath the skin also act as shock absorber
• Sterides
1. Sterols (Cholesterol)
2. Steroid hormones (Progesterone, Testosterone)
SIMPLE LIPIDS • Waxes
• Fatty acids
LIPIDS • Triglycerides

COMPOUND LIPIDS • Phospholipids

• Glycolipids
• Lipoproteins
Example of Lipids
THANK YOU