Biomolecules Important Notes and Questions - NEET - CLASS XI

Biomolecules
BIOMOLECULES
Living system are made up of various complex molecules like carbohydrates, proteins, nucleic acids, lipids etc. Proteins and
carbohydrates are essential constituents of our food. Vitamins and mineral salts also play important role in functions of
organism.
Carbohydrates
 The carbohydrates are naturally occuring organic substances. They are present in both plants and animals.
 Carbohydrates are formed in plants by photosynthesis.
 Animals do not synthesise carbohydrates but rely on plants for their supply.
 Old definition
 Hydrates of carbon are called carbohydrates
 General formula - Cx(H2O)y, glucose, fructose, maltose, sucrose, lactose, fit into this formula.
 But all the compounds which fit into this formula may not be classified as carbohydrates
Ex. - Acetic acid, C2(H2O)2
Formaldehyde, CH2O
 There are a number of compounds which are carbohydrates but do not possess this formula
Ex. - Rhamnose (C6H12O5)
 New definition -
 Optically active polyhydroxy aldehydes or ketones or the compounds which produce such units on hydrolysis are
called carbohydrates.
 Carbohydrates may have aldehydic or ketonic function group either free or as hemiacetal or as hemiketal formula.
Carbohydrates
Sugars Non-sugars
or
polysaccharides
* Tasteless
* Amorphous solid
* Insoluble
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Biomolecules
 Reducing and non-reducing sugars
 Those saccharides which reduce Fehling’s solution and Tollen’s reagent called reducing sugar and those which do
not, non reducing sugars.
 Reducing sugars contain either -hydroxy aldehyde or -hydroxy ketone or they contain cyclic hemiacetal/hemiketal
structures in equilibrium with open chain forms having a free –CHO or >C=O group.
 All monosaccharides whether aldose or ketose are reducing sugars.
 In disaccharides, if the reducing group of monosaccharides are bonded there are non reducing sugars.
Ex. -Sucrose., If these functional groups are free, these are called reducing sugars. Ex. - Maltose, lactose
 Starch and cellulose are non-reducing because there are no free reducing groups.
 Although fructose has ketonic group but may reduce Fehling and tollen reagent because it may covers in the
aldehydic group in presence of alkali used in these reagent.
CH2OH HC OH CHO
| |
C=O C OH CH – OH
| | |
 Monosaccharides -
 Aldose  having aldehyde group
Ketose  having ketonic group
 Number of carbon atoms constituiting the monosaccharides is also involved in the name
Different Types of Monosaccharides

Carbon atoms General term Aldehyde Ketone
3 Triose Aldotriose Ketotriose
4 Tetrose Aldotetrose Ketotetrose
5 Pentose Aldopentose Ketopentose
6 Hexose Aldohexose Ketohexose
7 Heptose Aldoheptose Ketoheptose
Biomolecules
 Pair of diastereomers having differ configuration at a chiral center called epimers.
Ex. - Glucose and manose (C2 epimers)
Glucose and galactose (C4 epimers)
CHO CHO CHO

H OH HO H H * OH
* *
HO H HO H HO H
* * *
H OH H * OH HO H
* *
H OH H OH
H OH * *
*
CH2OH CH2OH CH2OH
D-glucose D-manose D-galactose
(1) Glucose
 Molecular formula - C6H12O6 (aldohexose)
 It is known as dextrose.
 It is also called grape sugar.
 It is colourless, crystalline solid, water soluble.
 Glucose is correctly named as D(+) glucose.
• Preparation of glucose
(i) From sucrose -
H+
C12H22O11 + H2O C6H12O6 + C6H12O6
Glucose Fructose
 Glucose is much less soluble in alcohol than fructose so separates out by crystallising on cooling.
(ii) From starch -
H+
(C6H10O5)n + nH2O nC6H12O6
Starch Glucose
Biomolecules
• Chemical reactions of glucose -
Glucose oxime
(CHCl)4
CH2Cl
Biomolecules
• Structure of glucose -
(A) Open chain structure -
H
C= O
H OH
*
HO H
*
H OH
*
H OH
*
CH2OH
D-glucose
 This structure was assigned on the basis of the following evidences -
(i) Its molecular formula was found to be C6H12O6.
(ii) Glucose on complete reduction with HI gives n-hexane
(iii) It react with acetic anhydride and forms penta acetate derivatives.
(iv) Glucose combines with NH2OH to form a mono oxime.
(v) Mild oxidation of glucose gives gluconic acid.
• Evidences against open chain structure -
(i) It does not react with NaHSO3, NH3, DNP reagent (No free CHO group)
(ii) It does not give the Schiff’s test (No free CHO group)
(iii) It does not react with GR (No free CHO group)
(iv) Glucose penta acetate does not react with hydroxy amine.
(v) Glucose is found to exist in two different crystalline forms which are named  and .
(vi) An aqueous solution of glucose shows mutarotation.

(B) Cyclic structure of glucose -
 To overcome all objections against the open chain structure of glucose.
 It was given that two cyclic forms exist in equilibrium with open chain structure.
 Two cyclic hemiacetal forms of glucose differ only in the configuration of the hydroxyl group at C1 called anomeric
carbon. Such isomers i.e. -form and -form are called anomers.
 The six membered cyclic structure of glucose is called pyranose structure, in analog with pyran. The cyclic structure
of glucose is more correctly represented by Hawarth structure.
 A fresh aqueous solution of -glucose having specific rotation 110º and it is 19.7° for -glucose. On keeping the
solution of -glucose or -glucose, on equilibrium mixture is obtained having 36% -glucose and 64% -glucose
and mixture has specific rotation +52.5º. A change in the value of specific rotation is called mutarotation.
Biomolecules
• Structure of glucose -
H OH HO H
H 1 1
C= O *
*
2 2
H OH H OH H OH
* * *
3 3
HO H HO H HO H
* * *
4 4
H OH H OH H OH
* * *
5 5
H OH H O H O
* *
6 *6
CH2OH CH2OH CH2OH
D-glucose -D-glucose -D-glucose
6 6
CH2OH CH2OH
O 5 O 5 O
H H H OH
H H
4 1 4 1
OH H OH H
HO OH HO H
3 2 3 2
H OH H OH
Pyran -D-glucopyranose -D-glucopyranose
• Test of glucose
Heated in
(i) Glucose dry test tube
black mass
(ii) Silver mirror test  give silver mirror
(iii) Molisch test -

2-3 drops of alcoholic solution -Nephthanol
Glucose Formation of violet ring at
+ conc. H2 SO4 along the sides of test tube the junction of two liquids
(iv) Osazone formation test - Glucose on heating with excess of phenyl hydrazine in acetic acid gives a yellow
crystallinecompound
CHO CH = N–NH–C 6 H5 CH = NNHC6H5 CH = N–NHC6H5

| | | |
CHOH C6H 5 NH-NH2 CHOH C 6H 5 NH-NH2 C =O C6H5NHNH2 C =N–NHC6H5
| | | |
(CHOH)3 –H2O (CHOH)3 –C6H5NH2+NH3 (CHOH)3 –H2O (CHOH)3
| | | |
CH2OH CH2OH adjacent CHOH CH2OH CH2OH
glucose phenyl groups oxidised by
hydrazone second molecule
glucosazone
Biomolecules
(2) Fructore, fruit sugar, C6H12O6, Ketohexose
 It is written as D(–) fructose
 It also exists in the cyclic forms (Hemiketal).
 The ring formed is five membered ring and is named as furanose with analog to the compound furane.
1 1
CH2OH HOCH2 OH HO CH2 HO
2* 2*
C= O
3* 3*
HO H HO H HO H
*
4* 4*
H OH H OH H OH
*
5* 5*
H OH H O H O
*
6 6
CH2OH CH2OH CH2OH
D-fructose -D-fructose -D-fructose
6 1 6
OHCH2 CH2OH OHCH2 OH
5 2 5 2
H H HO OH H H HO CH2 OH
1
4 3 4 3
OH H OH H
-D-fructofuranose -D-fructofuranose
Comparison of Glucose and fructose
Property Glucose Fructose

1. Molecular formula C6H12O6 C6H12O6
2. Nature Polyhydroxy aldehyde Polyhydroxy ketone
3. Melting point 146oC 102oC

4. Optical activity of natural form Dextrorotatory Lavevorotatory
5. With ethyl alcohol Almost insoluble More soluble
6. Reduction with NaBH4 D-Sorbitol Mixture of D-sorbitol and

D-mannitol
7. Molisch's reagent Forms a violet ring Forms a violet ring
8. Fehling's reagent Gives red precipitate gives red precipitate

9. Tollen's reagent Forms silver mirror Forms silver mirror
10. Phenylhydrazine Forms osazone Forms osazone
11. Mutarotation Show Show
Biomolecules
 Disaccharides
 The disaccharides yield on hydrolysis two monosaccharides -
H+
Sucrose + H2O invertase enzyme Glucose + Fructose
H+
Lactose + H2O lactase
Glucose + Galactose
H+
Maltose + H2O maltase
Glucose + Glucose
 In disaccharides, the two monosaccharides are joined together by glycoside linkage (oxide linkage) formed by the
loss of water molecule. A glycoside bond is formed when hydroxyl group of the hemiacetal carbon of one monosac
charide condenses with a hydroxy group of another monosaccharide.
(1) Sucrose
 It is also called cane sugar.
 It is composed of -D-glucopyronose unit and -D-fructofuranose unit. These units are joined by - glycosidic
linkage between C-1 of the glucose unit and C-2 of the fructose unit.
6
CH2OH
5 O
H H
H
4 1
OH H
HO
2  -link
3
H OH
6 O
OHCH2  -link
5 2
H H HO CH2OH
1
4 3
OH H
 Since the reducing groups of glucose and fructose are involved in glycosidic bond formation, sucrose is a non
reducing sugar.
 Sucrose is dextrorotatory but often hydrolysis gives dextrorotatory glucose and laevoratory fructose.
 Since the laevorotatory of fructose (–92.4º) is more than dextrorotatory. Thus hydrolysis of sucrose brings about a
change in the sign of rotation from dextro to laevo and the product is named as invert sugar, process is called
inversion of sugar.
Biomolecules
(2) Maltose (Malt sugar)–C12H22O11
 It is composed of two -D-glucose units in which C-1 of one glucose unit is linked C-4 of another glucose unit.
6 6
CH2OH CH2OH
5 O 5 O
H H H H
H H
4 1 4 1
OH H OH H
HO OH
3 2 O 3 2
H OH H OH
( -1,4 - glycosidic linkage)
 Since a reducing group is free in maltose so it is reducing sugar.

(3) Lactose (Milk sugar)- C12H22O11
 It is composed of -D-galactose and -D-glucose.
 The linkage is between C-1 of galactose and C-4 of glucose.
6 6
CH2OH CH2OH
5 O 5 O
HO H OH
H H
4 1 4 1
OH H O OH H
H H H
3 2 3 2
H OH H OH
Galactose unit Glucose unit
( -1,4 - glycosidic linkage)
 Since a reducing group is free at C-1 so it is reducing sugar.

 Polysaccharides –
 Polysaccharides contain a large number of monosaccharides units joined together by glycosidic linkage.
 General formula - (C6H10O5)n
 These are non reducing sugar.
(1) Starch –
 It is polymer of -glucose
 Starch consists of two components -amylose and amylopectin.
 Amylose is water soluble component which constitutes about 15-20% starch. Chemically amylose is a long un
branched chain with 200-100 -D-glucose units held by C1–C4 glycosidic bond.
 Amylopectin is insoluble in water and constitutes about 80-85% of starch. It is branched chain polymer of -D-
glucose units in which chain is formed by C1-C4 glycosidic linkage whereas branching occurs by C1-C6 glycosidic
linkage.
Biomolecules
 Glycogen is also known as animal starch.
(2) Cellulose –
 It is a straight chain polymer of -D-glucose
 C1 of one glucose unit is joined with C4 of next glucose unit.
HOH2C
O
O
HOH2C OH
O O
OH
HOH2 C OH
O O
OH
OH -links
O
OH
Biomolecules
Amino acids
The compound containing –NH2 and –COOH functional groups are known as amino acid, depending upon the relative
position of –NH2 group with respect to –COOH group, amino acids are classified into , , , , and so on amino acid.
Hydrolysis of protein gives only -amino acids represented as :
R CH COOH
NH2
Protein may contain other functional groups also.

 Nomenclature of -Amino acids:
 All -amino acids have their trival names which generally reflect the property of the amino acids or their sources. For
example, glycine is so named since it has sweet taste.
 Amino acids are generally represented by a three letter symbol, sometimes one letter symbol is also used. The structures
of the some commonly occuring amino acids along with their three-leter and one-letter symbols are given in the following
table:
S.N. Name of the Characteristic feature Three letter One letter code
amino acids of sides chain, R symbol
1. Glycine Gly G
2. Alanine Ala A
3. Valine* Val V
4. Leucine* Leu L
5. Isoleucine* IIe I
6. Arginine* Arg R
7. Lysine* Lys K
8. Glutamic acid Glu E
9. Aspartic acid Asp D
10. Glutamine Gln Q
11. Asparagine Asn N
12. Threonine* Thr T

13. Serine Ser S
14. Cysteine Cys C
15. Methionine* Met M
16. Phenylalanine* Phe F
Biomolecules
17. Tryosine Tyr Y
18. Tryptophan* Trp W
19. Histidine* His H
20. Proline Pro P
*Essential amino acid

 Classification of Amino acids:
Depending upon the relative number of amino and carboxyl groups in the molecules amino acids are classified as acidic,
basic or neutral, depending upon the relative number of amino and carboxyl groups.
 Equal number of –NH2 and –COOH groups make the amino acid neutral.
 More –NH2 group than –COOH group make the amino acid basic
 More –COOH group than –NH2 group make the amino acid acidic.
 Essential and non-essential amino acids:
The amino acids which cannot be synthesized in the body are known as essential amino acids which must be taken
through diet. The amino acids, which can be synthesized in the body are known as non-essential amino acids.
 Physical Properties of -Amino acids:
Amino acids are generally colourless, crystalline, water-soluble, high melting solids. They behave like salts rather than
simple amines or carboxylic acids due to the presence of both COOH and –NH2 groups.
In aqueous solution amino acids can exist as a dipolar ion known as zwitter ion –COOH group losses H  ion and –NH2
groups H  ion.
In zwitter ionic form, amino acids show amphoteric behaviour.
In acidic solution, the accepts a proton and gets converted to –COOH, while in basic solution the ammonium
substituent losses a proton and gets converted to –NH2.
Biomolecules
 Isoelectric Point:
The pH at which the amino acid shows no tendency to migrate when placed in an electric field is known as its isoelectric
point.
Protein
 This term is called by Mulder.
 They are made up of C, H, N, O some protein also contain sulphur, phosphorus and mineral elements [Cu++, Zn++, Fe++
etc]
 They have molecular weight higher than 10000 u.

 It is most abundant organic substance of the cell.
 It is polymer of amino acid.
R R
| |
NH2  C  CO– OH  H –NH  C  COOH
| H2 O |
H H
 CO  NH 
 In protein various amino acids remain attach through peptide bond or amide bond.
 Peptide bond formation is an example of dehydration synthesis.
 Simplest peptide is dipeptide. For example, when carboxyl group of glycine combines with amino group of alanine, we
get glycylalanine (dipeptide).
 Protein has various peptide bonds, so it is called polypeptide or polyamide structure.

 About 20 types of amino acid takes part in protein synthesis. For example insuline which countains 51 amino acids.
 Protein show maximum biodiversity.
 Protein show functional diversity.
 Classification of Protein: On the basis of molecular shape, proteins are classified into two types:
(1) Fibrous protein (2) Globular protein
Biomolecules
(1) Fibrous proteins: When the polypeptide chains run parallel and are held together by hydrogen and disulphide
bonds, then fibre-like structure is formed, known as fibrous proteins. Such protein are insoluble in water.
For example: Keratine, Myosin etc.
(2) Globular proteins: When the polypeptide chains coil around to give a spherical shape, the formatino of globular
protein takes place. Such protein are usually soluble in water.
For example: Insulin, Albumins etc.
 Primary, Secondary, Tertiary and Quaternary Structures of Proteins:
(1) Primary structure: Proteins may have one or more polypeptide chains. Each polypeptide in a protein has amino
acids linked with each in a specific sequence and it is this sequence of amino acids that is said to be the primary structure
of that protein. Any change in this primary structure i.e., the sequence of amino acids creates a different proteins.
(2) Secondary structure: The secondary structure of proteins refer to the shape in which a long polypeptide chain
can exist. They are found to exist in two different types of structure namely -helix and -pleated sheet structure. These
structures arise due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between
C and –HN– groups of the peptide bond.
O
-Helix Structure of Proteins -Pleated Sheet Structure of Proteins

 -Helix is one of the most common ways in which a polypeptide chain forms all possible hydrogen bonds by twisting into
a right-handed screw (Helix) with the –NH group of each amino acid residue hydrogen bonded to C =O of an adjacent
turn of the helix as shown above figure.
Biomolecules
 In -structure all peptide chains are stretched out to nearly maximum extension and then laid side by side which are held
together by intermolecular H-bonds. The structure resembles the pleated folds of drapery and therefore is known as -
pleated sheet.
(3) Tertiary Structure: The tertiary structure of proteins represents overall folding of the polypeptide chains i.e.,
further folding of secondary structure. It gives rise to two major molecular shapes namely fibrous and globular. The main
forces which stabilizes the 2° and 3° structures of proteins are hydrogen bonds, disulphide linkages, vander Waals and
electrostatic forces of attraction.
(4) Quaternary Structure: Some of the proteins are composed of two or more polypeptide chains referred to as sub
units. The spatial arrangement of these subunits with respect to each other is known as quaternary structure.
Diagrammatic representation of protein structure

(two bus-units of two types in quaternary structure)
 Denaturation of Proteins : The loss in biological activity of protein due to unfolding of globules and uncoiling of helix
is called denaturation of protein. During denaturation secondary and tertiary structures are destroyed but primary
sturcture remains intact. The coagulation of egg white on boiling is a common example of denaturation. Another
example is curing of milk which is caused due to the formation of lactic acid by the bacteria present in milk.
 Test of protein
(a) Ninhydrin - Protein when treated with a pyridine solution of ninhydrin give colour ranging from deep blue to violet pink
or even red in some cases.
(b) Biuret Test - When an alkaline solution of protein is treated with a drop of aqueous copper sulphate, a bluish violet
colour is obtained.
(c) Million’s Reaction - This test is characteristic of phenol and of only those proteins having this group (e.g. tryosine unit). A
white precipitate is obtained when such protein is heated with Million’s reagent (HgNO3 in HNO3 containing little HNO2).
Biomolecules
Enzyme
 Colloidal solution of protein which works as biological catalyst is known as enzyme.
 All enzymes are globular proteins.
 Some enzymes are associated with some non-protein component, called the cofactor of their activity. These cofactors
are of two types:
(i) Inorganic ions such as Zn++, Mg++, K+, Na+, Fe++, Cu++, Mo++ etc.
(ii) Organic Molecules : They are of two types:
(a) Coenzymes : They are small organic molecules cofactor is held with protein by very weak bond. In most of the cases
these cofactors are derived from vitamins such as, thiamine, riboflavin, niacin etc.
(b) Prosthetic Groups : These are also organic molecules (mainly vitamins) and are bonded to protein by covalent bond.
 Thus all enzymes are conjugated proteins:
Name of Enzyme Reaction Catalysed
(i) Zymase Glucose and Fructose  C2H5OH
(ii) Invertase Sucrose  Glucose + Fructose
(iii) Maltase Maltose  Glucose + Glucose
(iv) Lactase Lactose  Glucose + Galactose
(v) Emulsin Cellulose  Glucose
(vi) Urease Urea  CO2 + NH3
(vii) Pepsin Proteins  -amino acids
(viii) Trypsin Proteins  -L-Amino acids
(ix) -Amylase Starch  Glucose
 Temperature Dependence of Enzyme Activity:
 The enzymes work best at an optimum temperature range of 298 K to 313 K. Their activity decreases with decrease or
increase in temperature and stops at 273 K.
 Efficiency : Even a small amount of enzymes are highly efficient. This is because their molecules are regenerated during
their catalytic activity.
 Those chemical substances which tend to reduce activity of a particular enzyme are called enzyme inhibitors.
Biomolecules
Vitamins (Vital minerals)
The organic compounds which are required in very small amounts and are necessary to maintain normal health, growth
and nutrition are called vitamins. It should be noted that vitamins are not utilized in cell building or as energy source
but they act as catalysts (co-enzymes) in biological processes. Their deficiency causes serious diseases. Vitamins
are not synthesized in the body and hence should be supplied in diet i.e. they are essential dietary factors.
 Classification of Vitamins
(i) Fat soluble vitamins – These are vitamin A, D, E and K.
(ii) Water soluble vitamins – Vitamin B complex and vitamin C.
SR. Name of Sources Deficiency diseases

No. Vitamins
1. Vitamin A Fish liver oil, carrots, butter and milk Xerophthalmia (hardening of cornea of eye)
Night blindness
2. Vitamin B1 Yeast, milk, green vegetables and Beri beri (loss of appetite, retarded growth)
(Thiamine) cereals
3. Vitamin B2 Milk, eggwhite, liver, kidney Cheilosis (fissuring at corners of mouth and lips),
(Riboflavin) digestive disorders and burning sensation of the skin.
4. Vitamin B6 Yeast, milk, egg yolk, cereals and Convulsions

(Pyridoxine) grams
5. Vitamin B12 Meat, fish, egg and curd Pernicious anaemia (RBC deficient in haemoglobin)
6. Vitamin C Citrus fruits, amla andgreen leafy Scurvy (bleeding gums)
(Ascorbic acid) vegetables
7. Vitamin D Exposure to sunlight, fish and egg yolk Rickets (bone deformities in children) and
osteomalacia (soft bones and joint pain in adults
8. Vitamin E Vegetable oils like wheat germ oil, Increased fragility of RBCs and muscular
sunflower oil, etc. weakness
9. Vitamin K Green leafy vegetables Increased blood clotting time
Biomolecules
Nucleic Acid
The particles in nucleus of the cell, responsible for heredity are called chromosomes which are made up of proteins and
other type of biomolecules called nucleic acid. These are natural biopolymers made of nucleotide units i.e., polynucleotides.
Nucleic acid contain the elements carbn, oxygen, nitrogen and phosphorous.
 Friedrich Miescher in 1869 isolated it from pus cell and called it Nuclein.
 Altmann give nucleic acid name
 Nucleic acid act as genetic material in living being.
 Nucleic acid has three components -
(1) Nitrogenous base (2) Pentose sugar (3) Phosphate group
[1] Nitrogeneous base :-
There are two types of nitrogenous bases:
(a) Pyrimidine :- (b) Purines

 They are single ring containing nitrogeneous base.  They are double ring containing nitrogeneous base.
 They have nitrogen on 1’ & 3’ positions and 4-carbons.  Nitrogen is present on 1’, 3’, 7’, & 9’ positions.
 It is 6 membered ring.  Purine is formed by the attachement of imidazole ring on
4’ and 5’ positions of pyrimidine
H H
7
C6 5 C6 5 N
1N C H 1N C 8
C H
2
2
C C H C C N9
4 H N 4
H N
3 3
H
Ex. Cytosine, Uracil , Thymine Ex. Adenine, Guanine
Thymine Cytosine Uracil Adenine Guanine
Note:
 Cytosine is common for both DNA and RNA and Thymine is present in DNA. Uracil is present in RNA at the place of
Thymine.
Biomolecules
[2] Pentose sugar :
 Nucleic acid has two type of pentose sugar:-
Ribose sugar Deoxyribose
(C5H10O5) (C5H10O4)
It is present in RNA It is present in DNA
5’ 5’
HOCH2 O OH HOCH2 O OH
4’ 1’ 4’ 1’
H H H H
H H H H
3’ 2’ 3’ 2’
HO OH HO H
-D-ribose  -D-2-Deoxyribose
 Deoxyribose sugar lack a oxygen at 2’ C.

 These sugars are present in -furanose form.
[3] Phosphate group :-
OH O
| |
3 H   3
OH  P  O   O  P  O (PO 4 )
| |
OH O
 Nucleoside & Nucleotide

 Nitrogeneous base + Sugar = Nucleoside or base sugar combination.
 Nucleoside + Phosphate = Nucleotide or Nucleoside monophosphate.
Nitrogenous base + Sugar
Nucleoside
Phosphate group
Nucleotide
Polymerisation
(By the formation of phosphodiaster bond)
Polynucleotide chain (DNA or RNA)
Biomolecules
Note :
 RNA has ribonucleotides while DNA has deoxyribonucleotide.
 Sugar of ribonucleoside has three hydroxyl group on 2’, 3’, 5’ positions. So phosphate can attach on 3’ or 5’ position.
 Sugar of dioxyribonucleoside has free hydroxyl group on 3’ & 5’ positions only.
Phosphodiester
bond
Glycosidic
bond
Phosphate
Deoxyribose
Nucleoside
Nucleotide
 Different type of nucleotide and nucleoside are following:
Bases
Purines Pyrimidines
Adenine (A) Guanine (G) Cytosine (C) Uracil (U)/Thymine (T)
In RNA Adenosine Guanosine Cytidine Uridine
Nucleosides
In DNA Deoxyadenosine Deoxyguanosine Deoxycytidine Deoxythymidine
In RNA Adenylate Guanylate Cytidylate Uridylate
Nucleotides
In DNA Deoxyadenylate Deoxyuanylate Deoxycytidylate Deoxythymidine
Note :
 Nitrogen base and sugar attach through N-glycosidic bond.
 This bond is formed between first carbon (1’-C) of sugar and 3’-N of pyrimidine or 9’-N of purine.
 Phosphate attach with fifth carbon (5’-C) of sugar through ester bond.
Biomolecules
 Structure of Nucleic Acid
A simplified version of nucleic acid chain is as shown below.
 Information regarding the sequence of nucleotides in the chain
of a nucleic acid is called its primary structure.
 Nucleic acids have a secondary structure also. James Watson
and Francis Crick gave a double strand helix structure for DNA.
 Two nucleic acid chains are wound about each other and held
together by hydrogen bonds between pairs of bases.
 The two strands are complementary to each other because the

hydrogen bonds are formed between specific pairs of bases. Ad-
enine forms hydrogen bonds with thymine whereas cytosine forms
hydrogen bonds with guanine.
 In secondary structure of RNA, helices are present which are only

single stranded. Sometimes they fold back on themselves to form
a double helix structure.
 RNA molecules are of three types and they perform different func-
tions. They are named as messenger RNA (m-RNA), ribosomal
RNA (r-RNA) and transfer RNA (t-RNA).
Diagram of the DNA double helix showing complementary

base pairing. The arros indicate the 3’5’ direction
Biomolecules
5' end
3' end
A segment of one DNA chain showing how phosphate ester

groups link the 3’- and 5’-OH groups of deoxyribose units.
 DNA Fingerprinting
It is known that every individual has unique fingerprints. These occur at the tips of the fingers and have been used for
identification for a long time but these can be altered by surgery. A sequence of bases on DNA is also unique for a person
and information regarding this is called DNA fingerprinting. It is same for every cell and cannot be altered by any known
treatment. DNA fingerprinting is now used
(i) in forensic laboratories for identification of criminals.
(ii) to determine paternity of an individual.
(iii) to identify the dead bodies in any accident by comparing the DNA’s of parents or children.
(iv) to identify racial groups to rewrite biological evolution.
 Biological Functions of Nucleic Acids
DNA is the chemical basis of heredity and may be regarded as the reserve of genetic information. DNA is exclusively
responsible for maintaining the identity of different species of organisms over millions of years.
 A DNA molecule is capable of self duplication during cell division and identical DNA strands are transferred to daughter cells.
 Another important function of nucleic acids is the protein synthesis in the cell. Actually, the proteins are synthesised by
various RNA molecules in the cell but the message for the synthesis of a particular protein is present in DNA.

Biomolecules Important Notes and Questions - NEET - CLASS XI

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Biomolecules Important Notes and Questions - NEET - CLASS XI

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Biomolecules

 Carbohydrates are formed in plants by photosynthesis.

 Hydrates of carbon are called carbohydrates

Ex. - Acetic acid, C2(H2O)2

Ex. - Rhamnose (C6H12O5)

 All monosaccharides whether aldose or ketose are reducing sugars.

Ketose  having ketonic group

Different Types of Monosaccharides

CHO CHO CHO

D-glucose D-manose D-galactose

 This structure was assigned on the basis of the following evidences -

(i) Its molecular formula was found to be C6H12O6.

(ii) Glucose on complete reduction with HI gives n-hexane

(iv) Glucose combines with NH2OH to form a mono oxime.

(v) Mild oxidation of glucose gives gluconic acid.

• Evidences against open chain structure -

(iii) It does not react with GR (No free CHO group)

(vi) An aqueous solution of glucose shows mutarotation.

 To overcome all objections against the open chain structure of glucose.

Pyran -D-glucopyranose -D-glucopyranose

(ii) Silver mirror test  give silver mirror

(iii) Molisch test -

CHO CH = N–NH–C 6 H5 CH = NNHC6H5 CH = N–NHC6H5

Comparison of Glucose and fructose

Property Glucose Fructose

3. Melting point 146oC 102oC

6. Reduction with NaBH4 D-Sorbitol Mixture of D-sorbitol and

8. Fehling's reagent Gives red precipitate gives red precipitate

11. Mutarotation Show Show

 It is also called cane sugar.

 Since a reducing group is free in maltose so it is reducing sugar.

( -1,4 - glycosidic linkage)

 Since a reducing group is free at C-1 so it is reducing sugar.

Protein may contain other functional groups also.

10. Glutamine Gln Q

11. Asparagine Asn N

12. Threonine* Thr T

18. Tryptophan* Trp W

19. Histidine* His H

20. Proline Pro P

*Essential amino acid

In zwitter ionic form, amino acids show amphoteric behaviour.

substituent losses a proton and gets converted to –NH2.

 They have molecular weight higher than 10000 u.

 Protein has various peptide bonds, so it is called polypeptide or polyamide structure.

-Helix Structure of Proteins -Pleated Sheet Structure of Proteins

Diagrammatic representation of protein structure

 All enzymes are globular proteins.

(ii) Organic Molecules : They are of two types:

 Thus all enzymes are conjugated proteins:

Name of Enzyme Reaction Catalysed

(i) Zymase Glucose and Fructose  C2H5OH

(ii) Invertase Sucrose  Glucose + Fructose

(iii) Maltase Maltose  Glucose + Glucose

(iv) Lactase Lactose  Glucose + Galactose

(v) Emulsin Cellulose  Glucose

(vi) Urease Urea  CO2 + NH3

(vii) Pepsin Proteins  -amino acids

(viii) Trypsin Proteins  -L-Amino acids

(ix) -Amylase Starch  Glucose

 Temperature Dependence of Enzyme Activity:

SR. Name of Sources Deficiency diseases