NOTE FOR THE CHAPTER ----BIOMOLECULES---XII

The various types of compounds which are found to be essential for animal for animal life:Carbohydrates: e.g. starch and sugar
Lipids: e.g. ghee and butter
Proteins: e.g. complex molecules present in meat and pulses
Vitamins: e.g. present in food in traces
Hormones: present in food or synthesized by the body
The molecules of the above listed compounds form the basis of the life. Such molecules of organic compounds which
build up life system and required for the growth and the maintenance are called BIOMLECULES.
CELLULAR ENERGETICS: FREE ENERGY CHANGES IN BIOLOGICAL REACTIONSCellular reactions follow the basic principles of thermodynamics. Only those reactions should be spontaneous
for which G negative. All the carbolic reactions proceed with decrease of energy(G<0)but some important cellular
reactions proceed even G is positive.e.g. Photosynthesis in plants for which G>0. Many anabolic reactions
proceed with increase of free energy i.e. G>0.
A very common reaction which provides energy in many cellular reactions is the hydrolysis of adenosine
triphosphate (ATP). The biochemical unit of energy is ATP. The cell obtains energy for the synthesis of ATP through
photosynthesis / catabolism of nutrients such as carbohydrates and lipids, this all occurs through coupled reaction.
WHY ATP MOLECULE IS ENERGY RICH MOLECULE?
The ATP molecule is consists of four negatively charged oxygen atoms which are close to each other; the repulsive
forces between them are very high. These forces makes them high energy molecules, actually this energy is stored in
oxygen-phosphorous bonds. The oxygen bonds between the two phosphoric acid residues are high energy phosphate
bonds. During hydrolysis these bond break, this reduces the number of oxygen atoms in the molecules and the
repulsive forces between o-atoms decreases, and as a result large amount of energy is released. The energy released
during this process depends upon the products formed and the Ph of the solution. AMP and ADP molecules get
converted to ATP molecules during this process.
CARBOHYDRATES:
The polyhydroxy aldehydes, polyhydroxy ketones, or large polymeric molecules which on hydrolysis produce
polyhydroxy aldehydes, polyhydroxy ketones, are called CARBOHYDRATES.
STARCH AND THE SUGARS ARE THE MOST COMMON CARBOHYDRATES .
The sugar is stored in the body as glycogen (C6H1005)
CALSSIFICATION OF CARBOHYDRATES:
Carbohydrates can be classified on the basis of I) Behaviour on hydrolysis ii) taste
ON BEHAVIOUR they are classified into Monosaccharide, Oligosaccharides, and Polysaccharides.
MONOSACCHRIDES: These are simple carbohydrate molecules which can not be hydrolysed into many simpler
molecules. Each molecule represents a complete carbohydrate molecule unit. They contain 3 to 7 carbon atoms
therefore their general formula (CH20) n.
Examples: - glucose, fructose, galactose, and ribose.

OLIGOSACCHRIDES:- The carbohydrates whose molecules on hydrolysis give 2 to 9 molecules of

monosaccharides either same or different are called oligosaccharides. They are divided into di, tri, tetra and
polysaccharides further.
Examples: Disaccharides ( C12H22011) such as Sucrose, maltose, Lactose, they produce two molecules of
monosaccharides on hydrolysis.
Trisaccharides: - Carbohydrates which upon hydrolysis produce three molecules of monosaccharides. The gen.
formula is (C18H32016). Example:- Raffinose which on hydrolysis give one molecule of each glucose, fructose and
galactose.
Tetrasaccharides: - They give four molecules of monosaccharides on hydrolysis having gen. formula (C 24H42021).
Example: - Stachyrose which upon hydrolysis give each of glucose, fructose and two molecules of galactose.
Polysaccharides :- Carbohydrates which upon hydrolysis produce large number of monosaccharides having gen.
formula (C6H1005) n. where n = 100 3000. such as Starch, Cellulose, and glycogens.
CALSSIFICATION OF CARBOHYDRATES ON THE BASIS OF TASTE:- They are classified as Sugars and nonSugars
Sugars: - which are sweet in taste and dissolve in water are called sugars. All mono and disaccharides are sweet in
taste.
Examples: - Glucose, fructose, Sucrose, Lactose are sugars.
Non-Sugars:- Tasteless polysaccharides which are insoluble in water. They are generally amorphous in nature.
Examples: - Cellulose and Starch.
ADDITIONAL INFORMATION --- MONOSACCHARIDES
In addition to hydroxyl group they either contain aldehydic or ketonic group. The aldehydic being monovalent is either
present at the end of the carbon chain. Hence such monosaccharides are called ALDOSE. On the other hand ketonic
group being divalent can be present anywhere on the carbon chain. In natural monosaccharides this group is present
normally at the second carbon atom. Hence they are also termed as KETOSE. Depending upon the no. of c-atoms these
molecules are termed as trios, tetrose, pentose, and hexose. Ketose and aldose are added to the prefixes to the no. of catoms.
CHARACTERISTICS: - They are sweet and water soluble and when heated they get charred. Due to the presence of
0H-group they can be easily acetylated. They can be reduced to sugar alcohols. They can be oxidized at the aldehydic
carbon to aldonic acid. Two molecules of monosaccharides combine with an elimination of water (H 20) molecule to
give a disaccharide.
They undergo oxidation, reduction, acetylation, react with hydroxylamine, phenyl hydrazine and fermentation.
ADDITIONAL INFORMATION ------ DISACCHARIDES.
Its main source is sugarcane and beet. These include Sucrose, Maltose, and Lactose. Sucrose is hydrolysed by both
enzymes maltase and invertase.Sucrose is both a -glucoside and -fructoside. Hence it can be concluded that Sucrose
consists of -glucose and -fructose. They are held together by , -glycosidic linkage.
INVERT SUGAR: - Cane sugar is dextrorotatory. On hydrolysis it gives dextrorotatory glucose and laevorotatory
fructose. Therefore a equimolar mixture of glucose and fructose with opposite signs are called inversion of sugar or
invert Sugar.

POLYSACCHARIDES: - There can be linear or branched chain polysaccharides. Polysaccharides are amorphous,
tasteless and mostly insoluble in water. These include starch, dextrin, cellulose, and glycogens. Their main functions
are storage of food.
They can further be classified as Homopolysaccharides and Hetropolysaccharides.
Homopolysaccharides contain same type of monosaccharides. Example: - glycogen, starch, and cellulose are polymers
of glucose.
Hetropolysaccharides: - they contain two or more different monosaccharides. Example: - Gums.
STARCH: - It is odourless, tasteless, and insoluble in water. It is amorphous and white substance. When boiled its
granules swells and burst to form a colloidal solution called starch paste. It is a polymer of -glucose and composed of
two components amylase(20%) and amylopectin(80%). Amylose is water soluble whereas amylopectin is water
insoluble. The structure of glucose is similar as that of amylopectin. Amylose is linear polymer whereas amylopectin is
a branched one.
AMINO ACIDS: - The carboxylic acids containing amino (-NH 2) group attached to any carbon atoms other than
carboxylic carbon are called amino acids. An amino acid always contains one H-atom, one R group, one C00H group
and one NH2 group and they are attached to single carbon atom. In aqueous solution the C00H group looses a proton to
form carboxalate ion and the NH2 group gains this proton to form +NH3 ion. Hence in aqueous solution amino and
carboxyl groups are in the ionized form and amino acid molecule exists as a dipolar ion. This dipolar ion is called
Zwitter-ion. Amino acids in dipolar form are amphoteric in nature.
Therefore in acidic solution, an amino acid exists as a positive ion, and therefore it migrates to the negative electrode
(cathode) when placed in an electrical field.
In a basic solution, an amino acid it exists negative ion and therefore it migrates towards the positive electrode when
placed in electrical field.
The pH at which the amino acid molecule does not migrate to either of the electrodes is called the ISO-ELECTRIC
POINT.
D- L- CONFIGURATIONS OF AMINO ACIDS: - The - carbon atom in all the amino acids (except glycine) is
asymmetric (chiral). Therefore amino acids can exist in two stereo isomeric forms, i.e. D and L forms. These two
forms are the mirror images of each other but are non-superimposable on each other. Thy are drawn with the reference
of glyceraldehydes, in which the NH2-group lies on the left hand side of the c- atom in L- configuration and the NH 2group lies on the right side of the c- atom in D- configuration. All natural occurring amino acids are L-isomers.
Proteins consist of only L-amino acids.
The essential amino acids which must be present in our food are: - Isoleucine, Leucine, Lysine, Methionine,
Phenylalanine Threonine, Tryptophan, Valine, Arginine and Histidine.
PEPTIDES: - The compounds formed by the condensation of two or more, or same or different amino acids are called
peptides. During the formation of peptide, the amino (NH2) - group of one of the -amino acid and the carboxylic
(C00H) group of another molecule of the same or the different -amino acid get condensed with the elimination of
the water molecule. During this process a bond of the type C0NH- is formed between the two amino acids. This
amide linkage is called peptide linkage.
The peptide formed due to the condensation of only two, three or four molecules of the same or different amino acids
is called dipeptide; tripeptide and tetrapeptide bonds respectively.
All the peptides contain a free amino (NH 2) - group at one end and a free carboxylic (C00H) - group at the other end.
These are called end-groups or the terminal groups.
Some important biological peptides are Oxytocin-nanopeptide, Vasopressin- nanopeptide, Angiotensin-octapeptide.
PROTIENS: - Proteins are complex nitrogenous organic compounds and are essential for the growth and development
of the body. Proteins are macromolecules in which large numbers of amino acids are linked with peptide-bonds. On
hydrolysis they give amino-acids, in other words they are polypeptides of very high molecular mass, (10 4 106g/mol).
Egg, meat, fish, pulses, and milk are the good source of proteins. Normally there are 20 amino-acids are present in
proteins, and another six are found in the special tissues. The amino- acids differ in the side chain groups (R). the

properties of amino-acids depend upon the nature of side chain. The human can synthesize 10 out of 20 amino-acids
found in proteins. The other 10 must be supplied in the diet. Therefore they are called essential amino-acids. Lack of
proteins can cause a disease called Kwashiorkar. The elements present in most of the proteins are carbon, hydrogen,
oxygen, nitrogen and sulphur, iron, magnesium, phosphorous, etc.
CLASSIFICATION OF PROTIENS: - They are classified on the basis of chemical composition. Therefore there are
mainly three classes of proteins. A) Simple proteins B ) Conjugated proteins C) Derived proteins.
Simple proteins------ these are made up of only -amino-acids and they upon hydrolysis give -amino-acids.
Example ---------- Albumin,(in white of egg) Glutinin, (in wheat) Keratin, (in hairs & nails) are simple proteins.
Conjugated proteins: ------- the proteins which contain organic and inorganic compounds along with amino-acids are
called Conjugated proteins. The non-amino-acid group of the protein is called prothestic group. This group controls the
biological functions of the proteins. Conjugated proteins are further classified into
----------------------------------------------------Lipoproteins ------these contain lipids and amino-acids. The prothestic group in them is lipids.
Nucleoproteins ----- these contain nucleic acids and amino-acids. The prothestic groups in them are nucleic acids.
Glycoprotein ------- these contain carbohydrates and an amino-acids.The prothestic group in them is
carbohydrates/sugar.
Chromoproteins ------ they contain amino-acids and colored pigments.Haemoglobin, Myoglobin, Haemocynin,
Cytochrome, and Riboflavin.
Phosphoproteins------- they contain amino-acids and phosphate group.
Derived-Proteins: - The degradation products obtained from the partial hydrolysis of simple and conjugated proteins
are called Derived proteins.
CLASSIFICATION ON THE BASIS OF MOLECULAR STRUCTURE.
On the basis of structure they are classified as Fibrous Proteins and Globular Proteins:Fibrous Proteins:- They are consists of linear, thread-like polypeptide chain which are arranged and twisted to form
long strands (fibers) and they are held together by hydrogen bonds therefore the intermolecular forces of attractions are
very strong. They are insoluble in water and quite stable.
Example: - collagen of tendons, Keratin in skin, hairs and nails, Fibroin in silk, Myosin in muscles are Fibrous
Proteins.
Globular Proteins:- The proteins in which polypeptides are tightly folded into a compact form are called Globular
Proteins. In these proteins the hydrocarbon (lipohillic) ends are pushed inwards while the polar hydrophilic part is
oriented outwards therefore these proteins are water soluble and very sensitive towards temperature and pH.
Examples: - All the enzymes, many hormones such as insulin, thryoglobins, antibodies, Haemoglobin, fibrinogen,
albumin, and venoms of snakes, scorpion, wasp, and bees are globular proteins.
CLASSIFICATION ON THE BASIS OF FUNCTION: On the basis of their function these are classified into the following types: 1 Structural Proteins
2 Contractile Proteins
3 Hormones
4 Enzymes
5 Blood proteins
ROLE OF PROTEINS:-

Enzymes: - All the enzymes found in the cells are proteins which catalyse large number of biological reactions in the
body.
Hormones: - Many hormones are proteins in our body. Hormones are chemical regulators therefore regulate blood
pressure. Glycoprotein and thryoglobins help in the synthesis of hormone thyroxin whereas nucleoproteins carry the
genetic information from the parents to off-springs.
Haemoglobin: - It contains the protein called globin and is present in the blood, transfer the oxygen from lungs to
tissues.
Blood proteins: - thrombin and fibrinogen are involved in blood clotting
DENATURATION OF PROTEINS:Energetically the most stable state of a protein is called as its native state or native form. The native state of a protein is
dictated by the amino acid sequence in the protein. Proteins are very sensitive to heat, acids, alkalies and even to the
electrolytes. Properties of globular proteins change altogether on heating or on treatment with acids/alkalies or
electrolytes. On heating, water-soluble globular proteins precipitate out due to formation of water-insoluble fibrous
proteins.The coagulated protein is called as denatured protein.
The process which leads to change in physical and biological properties of proteins without affecting its chemical
composition is called as denaturation of proteins. Denaturation causes changes only in secondary, and tertiary
structures of proteins. The primary structure of any protein does not change due to denaturation. Denaturation may be
reversible in some cases. Denaturation is caused by following factors
Change in the pH
Increase in temperature
Presence of acids, alkalies, or salts
Exposure to ultraviolet rays or x- rays
The most common examples are
Boiling of egg
Preparation of cheese from milk.
CHARACTERISTICS OF ENZYMES:EFFECT OF TEMPERATURE The activity of enzymes is highest at near point temperatures. Above this temperature
the enzymes get denatured and lose their activity. At lower temperature, the rates of enzyme catalyst reactions are slow
because of kinetic effects. In general, the rate of all chemical reactions increase on increasing the temperature. But the
rate of enzyme-catalyst reaction first increases shows a maximum at about 35- 37 oC and then decreases at high
temperature.
EFFECT OF pH The rate of pH on enzyme reaction is complex. The rate of an enzyme-catalyst reaction usually
passes through the maximum at an optimum pH. At higher or lower pH than this optimum pH, the enzymes tend to get
denatured and therefore lose their activity.
PRESENCE OF ELECTROLYTES AND ULTRAVIOLET RAYS- Enzymes lose their activity in the presence of
electrolytes or when exposed to ultraviolet radiations. This is because enzymes get denatures in the presence of
electrolytes or when exposed to ultraviolet rays.
ENZYME INHIBITORS Enzymes are very sensitive to catalytic poisons. Some typical poisons are HCN, H 2S, CS2.
Enzymes lose their activity in the presence of these substances because these molecules tend to get absorb on the
surface of enzyme strongly.
EFFECT OF METAL IONS AND SIMPLE ORGANIC MOLECULES- most enzymes are associated with some nonprotein compounds required for their activity. These non-protein compounds are called as prosthetic groups. Prosthetic
groups may be metal ions or smaller organic molecules called coenzymes. Some of the metal ions involved are those

of Zn, Mg, Mn, Fe, Cu, K and Na.Many of the coenzymes are derived from vitamins, such as thiamine, niacin,
riboflavin, etc.
NUCLEIC ACIDNucleic acids are another important macromolecules present in the cells of all living organisms.Nucleic acids are long
thread like macromolecules of high molecular masses. Nucleic acids are responsible for transmission of hereditary
characters and for the bio-synthesis of proteins. Therefore they govern the metabolic activities in living organisms.
They are present in the form of nucleoproteins.
CONSTITUENTS OF NUCLEIC ACIDS
Nucleic acid contains following three contents
A pentose sugar ( ribose or deoxyribose)
A nitrogen containing heterocyclic base; a purine or pyridimine base
A phosphate group
Nucleosides The base sugar unit in any nucleic acid chain is called as nucleoside.The nucleosides are named after
the names of the base, attached at the carbon atom number 1 of the sugar unit.
Eg. Ribose ribonucleoside, deoxyribose deoxyribonucleosides
Nucleotides The base- sugar- phosphate is called as a nucleotide. Nucleotides are the phosphate esters of
nucleosides.
For eg. Ribose- ribonucleotide, deoxyribose- deoxyribonucleotides
TYPES OF NUCLEIC ACIDSDeoxyribonucleic acid (DNA)- DNA is the genetic material and is responsible for heredity character of the cell. DNA
is present in the nucleus of the cell. DNA is the most stable molecule of the biological world. DNA molecule may be
consuderd immortal.
COMPOSITION OF DNADNA contains the following four nitrogen bases- PURINES- adenine and guanine, PYRIDAMINES- thymine and
cytosine
Each unit of DNA strand has only four bases.
- the number of purine nucleotides is equal to the number of pyridimine nucleotides.
- the ratio of adenine(A) to thymine (T) . and guanine (G) to cytosine(C) is one
-

BIOLOGICAL SIGNIFICANCE OF DNADNA acts as a carrier of genetic information from parents to their offsprings
- DNA guides the process of protein synthesis in cells
- DNA is involved in the synthesis of RNA.

RIBONUCLEIC ACID (RNA)

The RNA is found to be genetic material in some plants and animal viruses.RNA is found in nucleolus, cytoplasm and
on the membrane in ribosomes. Each ribonucleotide contains
A pentose sugar-ribose
Purines- adenine and guanine
Pyridimines- cytosine and Uracyl
And phosphate groups.
Structure of RNA
Nucleotide of RNA consist of pentose sugar ribose. These ribonucleotides are linked to each other by 3-5
phosphodiester bonds. In this respect RNA resembles DNA. The polymeric chain of ribonucleotides forms RNA
polynucleotide strands.
RNA is single stranded except in certain viruses.RNA doesnt form helix. The primary structure of RNA differs from
DNA in the following ways:
In RNA, the sugar residue is ribose, whine in DNA it is 2deoxyribose
RNA consists of pyridimine base Uracyl(U) in the place of Thymine (T) in DNA.

Classification of RNA
The organisms which have RNA only as nucleic acid use this RNA in genetic mechanism. Such type of RNA is called
as genetic RNA.
The organisms which have RNA along with some DNA , use their RNA in carrying out the orders of DNA.Such type
of RNA is called as non genetic RNA.
The non genetic RNA is heterogeneous and is classified by cellular location
MESSENGER RNA- Messenger RNA (m-RNA) is short-lived molecule that carries genetic information from DNA
to ribosomes where protein synthesis occurs.
RIBOSOMAL RNA- Ribosomal RNA(R-RNA) is an integral part of ribosome that also takes part in protein
synthesis.
About 75% of cellular component of RNA is ribosomal RNA ts molecular mass varies from 40,000 to 1.5 million.
TRANSFER RNA- Transfer RNA (T-RNA) acts as a carrier of amino acids. Its molecules contains 75-78 nucleotides
and their molecular mass varies from 23000 to 25000.Near the middle of its molecule there is a sequence of three
bases called anticodon. These three bases are hydrogen bonded to a complimentary sequence in m-RNA during protein
synthesis.All t-RNA molecules have a L- shaped tertiary structure. The hydrophobic interactions are a major
stabilizing force in the tertiary structure of t-RNA.
FUNCTION OF NUCLEIC ACIDS: - They have two important functions to perform---Replication The genetic information for the cell is contained in the sequence of the bases A, T, G, and C in the DNA
molecule.
When the cell divides, DNA molecule replicates and makes exact copies of themselves so that daughter cell will have
DNA identical to that of the parent cell, in this process the two strands of DNA helix- unwinds and each strands serves
as atemplate for the synthesis for a new stand.
Synthesis of proteins. This process involves Transcription and Translation
Translation :- In this step the double helix of DNA opens up and two strands of DNA acts as template for the synthesis
of complementary DNA molecule called messenger RNA (m-RNA)
The following sequences of bases in m-RNA formed and that of uncoiled strand of DNA takes place
Uncoiled strand of DNA : C G A C T T A C C G T A A
Tanscripted m-RNA
: G C U G A A U G G C AU U
Translation:- During translation, m-RNA directs the protein synthesis in the cytoplasm of cell with the involvement of
another type of RNA molecule namely , transfer-RNA (t-RNA) and the ribosomal particle.
LIPIDS:- Lipids are waxy or oily substances which are present in all living organisms. Lipids are the constituents of
all cell membranes. Lipids are esters of long chain fatty acids and alcohols. Lipids show some common characteristics
Lipids are soluble in the organic solvents but insoluble in water
All lipids on hydrolysis give monocarboxylic acids ( saturated or unsaturated)
Lipids may be broadly classified as
SIMPLE LIPIDS( triglicerides)- Fats and oils
Waxes
COMPLEX (compound) lipids-Phospholipids
Glycolipids
Functions of lipids
To form a part of structure of biological membranes. Phospholipids serve as structural component of cell membrane
To store energy for the cell. Simple lipids serve as energy reservoirs for animals
Simple lipids act as shock absorbers and heat insulators for the bodies of many organisms including humans.
HARMONES- chemical compounds secreted by ductless glands which meditate communication between the cells and
control various cellular activities are called as hormones.

Hormones may be called as chemical messengers or chemical regulators.Hormones are produced in ductless glands
and transported by blood circulation to the target tissues for producing inhibitory or stimulatory effect.
Classification of hormones-Based on chemical structures hormones fall in three categoriesSteroid hormones, Polypeptide hormones, Amine hormones
VITAMINES- A group of bio molecules which are not produced by the body but required in very small quantities for
normal metabolic activities and healthy growth of human beings and animals are called as Vitamines.
On the basis of their solubility they can be classified intoWATER SOLUBLE VITAMINES- Vitamines which dissolve in water are called as water soluble vitamins. Eg.
Vitamin B and C
OIL OR FAT SOLUBLE VITAMINES- Vitamines which dissolve in oil or fat are called as fat or oil soluble vitamins.
Eg. A, D, E and K.
IMPORTANT NCERT QUESTIONS
Q1

What are reducing and non-reducing sugars? What is a structural feature characterizing reducing sugar?
Q2

Q3

Draw simple fischer projections of D and L glucose. Are these enantiomers?

Write down the structures and the names of the products obtained when D glucose is treated with (a) acetic
anhydride
(b) hydrocynic acid, (c) bromine (d) concentrated HNO 3, (e) HI.
Q4

Q5

Explain mutarotation. Explain its mechanism in D glucose.

What are essential and non essential amino acids? Give 2 eg. Of each. Give reasons for the following(a) amino acids have relatively higher melting point as compared to corresponding halo acids.
(b) On electrolysis in acidic solutions amino acids migrate toward cathode whereas in alkaline solution these
migrate towards anode.
Q6

Q7

What type of linkages are responsible for the formation of these

(a) - Helix formation
(b) - sheet structure

What forces are responsible for the stability of - helix? Why is it named as 3.6 13 helix?
Q8

Q9
Q10
Q11

What is denaturation and renaturation of proteins?

What products are obtained on complete hydrolysis of DNA? Write down the structures of purines and
pyridimine
bases present in DNA.
What are complementary bases? Draw structure to show hydrogen bonding between adenine and thymine
bases
present in DNA.
How does DNA replicate? Give the mechanism of replication. How is the process responsible for preservation
of
heredity?
Q12

Answer the following about protein synthesis(a) How do 64 codons code for only 20 amino acids
(b) During translation which one of the two-end functional groups of the polypeptide is formed first?
Q13

How are lipids classified? Give an example of each class.

Q14

Hormones are chemical messengers . Explain.

Q15

Name the deficiency diseases caused due to lack of Vitamin A , C, E , B 1, B12, B6, and K.
REDUCING ANS NON-REDUCING SUGARS :-

Those carbohydrates which contain a free aldehydic or a ketonic group and reduce Tollens reagent are called
Reducing sugars. E.g. Glucose, fructose, galactose. On the other hand which do not reduce Tollens reagent and do not
contain free aldehydic or a ketonic group are called non-reducing sugars. E.g. Maltose, Lactose, Sucrose.
Kindly practice all the structures also.

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