Unit 14: Biomolecules: Mahendra Kalra . 9462305605
Unit 14: Biomolecules: Mahendra Kalra . 9462305605
Unit 14: Biomolecules: Mahendra Kalra . 9462305605
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(vi) Reaction with nitric acid HNO3 : On oxidation with nitric acid,
glucose yield a dicarboxylic acid, saccharic acid. This indicates the
presence of a primary alcoholic (–OH) group in glucose.
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PYRANOSE STRUCTURE OF GLUCOSE: The six membered cyclic structure of glucose is called pyranose structure
(α– or β–), in analogy with pyran. Pyran is a cyclic organic compound with one oxygen atom and five carbon
atoms in the ring. The cyclic structure of glucose is more correctly represented by Haworth structure as given
below.
6. Fructose Fructose is an important ketohexose. It is obtained along with glucose by the hydrolysis of
disaccharide, sucrose. Fructose also has the molecular formula C6H12O6 and 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. It belongs to D-series and is a laevorotatory compound. It is appropriately written as
D-(–)-fructose.
Structure of Fructose
7. DISACCHARIDES & GLYCOSIDIC LINKAGE Disaccharides on hydrolysis with dilute acids or enzymes yield
two molecules of either the same or different monosaccharides.The two monosaccharides are joined
together by an oxide linkage formed by the loss of a water molecule. Such a linkage between two
monosaccharide units through oxygen atom is called Glycosidic Linkage
8. SUCROSE: sucrose on hydrolysis gives equimolar mixture of D-(+)-glucose and D-(-) fructose.
These two monosaccharides are held together by a glycosidic linkage between C1 of α-glucose and C2 of
β-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 after hydrolysis gives dextrorotatory glucose and laevorotatory fructose.
Since the laevorotation of fructose (–92.4°) is more than dextrorotation of glucose (+ 52.5°), the mixture is
laevorotatory. 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.
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7. How do you explain the presence of five —OH groups in glucose molecule?
8. Under what conditions glucose is converted to gluconic and saccharic acid?
9. Explain Pyranose structure of glucose.
10. Write such reactions & facts of Glucose which cannot be explained by its open chain structure.
11. What is the basic structural difference Glucose and Fructose?
12. Despite having an aldehyde group glucose does not give 2, 4 - DNP test. What does this indicate?
13. What is the significance of D and (+) in D(+)-glucose ?
14. Explain the structure of Sucrose.
15. Classify the following into monosaccharides and disaccharides.Ribose,2 deoxyribose, maltose, galactose,
fructose and lactose.
16. Monosaccharides contain carbonyl group hence are classified, as aldose or ketose. The number of carbon
atoms present in the monosaccharide molecule are also considered for classification. In which class of
monosaccharide will you place fructose?
17. What are the hydrolysis products of (a) Sucrose. (b) Lactose (c)Maltose.
18. Name the sugar present in milk. How many monosaccharide units are present in it? What are such
oligosaccharides called?
19. Glucose or sucrose are soluble in water but cyclohexane or benzene are insoluble in water. Explain
20. How do you explain the absence of aldehyde group in the pentaacetate of D-glucose?
21. Write two main functions of carbohydrates in plants.
22. What do you understand by the term glycosidic linkage?
23. Name the linkage connecting monosaccharide units in polysaccharides.
24. Which sugar is called invert sugar?
25. What is meant by Invert Sugar.
26. Sucrose is dextrorotatory but the mixture obtained after hydrolysis is laevorotatory. Explain.
27. What is glycogen? How is it different from starch?
28. What is the basic structural difference starch and cellulose?
29. Name the carbohydrates that are used as storage molecules in plants
30. Name the carbohydrates that are used as storage molecules in animals,
31. name the carbohydrate which is present in wood or in the fibre of cotton cloth.
32. Define the term Anomers.
33. What is essentially the difference between the α- form of glucose & β- form of glucose?
34. ●An optically active compound having molecular formula C6H12O6 is found in two isomeric forms (A)
and (B) in nature. When (A) and (B) are dissolved in water they show the following equilibrium.
(A) ↔ Equilibrium mixture ↔ (B)
1110 52.20 19.20
(i) What are such isomers called? (ii) Can they be called enantiomers? Justify your answer
(iii) Draw the cyclic structure of isomer (A)
35. Name the two components of starch. How do they differ from each other structurally?
36. Which of the two components of starch is water soluble?
TOPIC: PROTEINS
1. PROTEINS: are the most abundant biomolecules of the living system. Chief sources of proteins are milk,
cheese, pulses, peanuts, fish, meat, etc. They occur in every part of the body and form the fundamental
basis of structure and functions of life. They are also required for growth and maintenance of body. The
word protein is derived from Greek word, “proteios” which means primary or of prime importance. All
proteins are polymers of α-amino acids.
2. α-AMINO ACIDS :
All proteins are polymers of α-amino acids. Amino acids contain amino (–NH2) and carboxyl (–COOH)
functional groups. Amino acids are generally represented by a three letter symbol, sometimes one
letter symbol is also used. For example :
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5. ISOELECTRIC POINT: The pH at which the amino acid molecule has no net charge & do not migrate
towards any electrode is called its Isoelectric point.
6. PEPTIDE BOND OR PEPTIDE LINKAGE.: peptide linkage is an
amide formed between –COOH group and –NH2 group. The
bond formed between two amino acids by the elimination of a
water molecule is called a peptide linkage or bond(–CO–NH–.)
For example, when carboxyl group of glycine combines with the
amino group of alanine we get a dipeptide, glycylalanine.
A dipeptide contains two amino acids linked by one peptide
Linkages , A tripeptide contains three amino acids linked by two
peptide linkages.When the number of such amino acids is more than ten, then the products are called
polypeptides. A polypeptide with more than hundred amino acid residues, having molecular mass higher
than 10,000u is called a protein.
7. GLOBULAR PROTEINS & FIBROUS PROTEINS : Proteins can be classified into two types (Globular Proteins
& fibrous proteins) on the basis of their molecular shape.
Globular proteins Fibrous proteins
This structure results when the When the polypeptide chains run parallel and are held together
chains of polypeptides coil by hydrogen and disulphide bonds, then fibre– like structure is
around to give a spherical shape. formed They can be stretched and contracted like a thread
usually soluble in water Insoluble in water
Example : Insulin Examples are
and albumins keratin (present in hair, wool, silk) and myosin (present in
muscles)
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8. Primary structure of proteins: Proteins may have one or more polypeptide chains. Each polypeptide in a
protein has amino acids linked with each other in a specific sequence and it is this sequence of amino
acids that is said to be the primary structure of that protein. The primary structure of a protein refers to
the number and sequence of the amino acids in its polypeptide chains. Any change in this primary
structure i.e., the sequence of amino acids creates a different protein.
9. Secondary structure of proteins:( α-helix and β-pleated sheet structure): The secondary structure of
protein refers to the shape in which a long polypeptide chain can exist. It gives information: (a) about the
manner in which the protein chain is folded and bent;(b) about the nature of the bonds which stabilise
this structure. They are found to exist in two different types of structures viz. α-helix and β-pleated sheet
structure.
α-Helix : This structure is formed when the chain of α -amino acids coils as a right handed screw
(called α -helix) because of the formation of hydrogen bonds between amide groups of the same
peptide chain, i.e., NH group in one unit is linked to carbonyl oxygen of the third unit by hydrogen
bonding. This hydrogen bonding between different units is responsible for holding helix in a
position. It is stablised by intramolecular hydrogen bonding. Wool and hair have α -helix
structure.
In β-structure all peptide chains are stretched out to nearly maximum extension and then laid side
by side which are held together by intermolecular hydrogen bonds. The structure resembles the
pleated folds of drapery and therefore is known as β-pleated sheet. Silk has a beta pleated
structure.
10. TERTIARY STRUCTURE OF PROTEINS: The tertiary structure of proteins represents overall folding of the
polypeptide chains i.e., further folding of the secondary structure. It gives rise to two major molecular
shapes viz. fibrous and globular. The main forces which stabilise the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction.
11. QUATERNARY STRUCTURE OF PROTEINS: 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
12. DENATURATION OF PROTEINS: Protein found in a biological system with a unique three-dimensional
structure and biological activity is called a native protein. When a protein in its native form, is subjected to
physical change like change in temperature or chemical change like change in pH, the hydrogen bonds are
disturbed. Due to this, globules unfold and helix get uncoiled and protein loses its biological activity. This
is called denaturation of protein. During denaturation 2° and 3° structures are destroyed but 1º
structure remains intact. For example : the heating of white of an egg (water soluble) gives a hard and
rubbery insoluble mass (coagulation of egg white on boiling) ,curdling of milk which is caused due to the
formation of lactic acid by the bacteria present in milk.
QUESTIONS RELATED TO PROTEINS
1. Draw the structure of Glycine, Alanine, and Phenylalanine.
2. Amino acids may be acidic ,alkaline or neutral.How does this happen.
3. ●What are essential and non essential amino acids? Give two examples of each type.
4. ●Write a note on zwitter ion and isoelectric point.
5. Amino acids behave like salts rather than simple amines or carboxylic acids. Explain
6. What do you understand by the term Peptide linkage&Poly Peptide linkage?
7. Write the name of linkage joining two amino acids.
8. ●Distinguish between the following: (a)Essential &Nonessential amino acids (b) Fibrous &Globular
proteins(c) -helix and -pleated sheet proteins
9. Write a note on: (a)Primary structure of proteins (b) secondary structure of proteins
10. What are the common types of secondary structure of proteins?
11. ●What type of bonding helps in stabilizing the -helix structure of proteins
12. ●How do you explain the amphoteric behaviour of amino acids?
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etc.
9 Vitamin K Green leafy vegetables Increased blood clotting ,time Haemorrhagic conditions
QUESTION RELATED TO VITAMIN
1. Define vitamins. How are vitamins classified?
2. Name the deficiency diseases caused due to lack of vitamin A, C, E, B1, B2, B6 , B12 E &K.
3. Give the main sources of vitamin A, C, E, B1, B2,, B6 , B12 E &K.
4. Write the chemical name of vitamin A, C, E, B1, B2,, B6 , B12 E &K.
5. Write the name of Vitamin responsible for the : (a) Pernicious anaemia (b) Increased blood clotting
time(c) Xerophthalmia(d) Rickets (e) Muscular weakness (f) Night blindness (g) Beri Beri(h) Bleeding
gums (i) Osteomalacia
6. Which of the following B group vitamins can be stored in our body? Vitamin B1, Vitamin B2 ,Vitamin B6
Vitamin B12
7. Except for vitamin B12, all other vitamins of group B, should be supplied regularly in diet. Why?
8. Why cannot Vitamin C be stored in our body?
9. Why Vitamin B & C essential for us.
TOPIC : ENZYMES &NUCLEIC ACIDS
1. Enzymes are Biocatalyst produced by living cells which catalysis the biological reactions. Enzymes are
mainly globular proteins. They are very specific in nature. They are needed in very small quantity.The
various steps involve in the enzyme catalyzed reaction are as follows:--
Binding of the enzymes (E) to substrate (S) to form a complex.
E + S ES (complex)
Product formation in the complex :E S E P
Release of product from the complex.: E P E + P
2. NUCLEIC ACIDS: Nucleus of a living cell is responsible for this transmission of inherent characters, also
called heredity.The particles in nucleus of the cell, responsible for heredity, are called chromosomes
which are made up of proteins and another type of biomolecules called nucleic acids. These are mainly of
two types, the deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). Since nucleic acids are long chain
polymers of nucleotides, so they are also called polynucleotides.
3. Complete hydrolysis of DNA (or RNA) yields a pentose sugar, phosphoric acid and nitrogen containing
heterocyclic compounds (called bases).
4. DNA (DEOXYRIBOSE NUCLEIC ACIDS) & RNA (RIBOSE NUCLEIC ACIDS)
DNA RNA
It contains β-D-2-deoxyribose sugar. It Contains β-D-ribose sugar.
It Contains adenine (A), guanine (G), cytosine It Contains adenine (A), guanine (G), cytosine (C), uracil
(C) and thymine (T) as bases. (U). as bases
It has double helix structure It has single helix structure
It Can replicate It Can not replicate
It is responsible for inheritance of character It is responsible for protein synthesis.
It is present in the nucleus cell. It is present in the cytoplasm of the cell.
STRUCTURE OF NUCLEIC ACIDS
5. NUCLEOSIDES: A unit formed by the attachment of a base to 1’ position of
sugar is known as nucleoside
Base + Sugar Nucleosides
7. PHOSPHODIESTER LINKAGE : Nucleotides are joined together by phosphodiester linkage between 5′ and
3′ carbon atoms of the pentose sugar.
10. PRIMARY STRUCTURE OF A NUCLEIC ACID : Information regarding the sequence of nucleotides in the
chain is of a nucleic acid is called its primary structure.
11. SECONDARY STRUCTURE OF A NUCLEIC ACID :
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. Adenine 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 functions.
12. DIFFERENT TYPES OF RNA : RNA molecules are of three types and they perform different functions. They
are named as messengerRNA (m-RNA), ribosomal RNA (r-RNA) and transfer RNA (t-RNA).
13. 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.
Questions related to Enzymes & Nucleic acids
1. ●Define Enzymes. Explain the mechanism of Enzyme action
2. What are biocatalysts? Give an example.
3. Define Nucleic acids. How are they classified? Mention their two important sources.
4. Write the full forms of DNA and RNA.
5. ●Write the important differences between DNA and RNA.
6. Name the four bases present in RNA.
7. Of the two bases named below which one is present in RNA and which one is present in DNA? (i) Thymine
(ii) Uracil
8. Out of the two bases Thymine & Uracil which one is present in DNA.
9. Out of the four bases name those which are common to both DNA
10. Which of the following are purine bases?Guanine,AdenineThymine & Uracil
11. What is the difference between a nucleoside and a nucleotide?
12. What is phosphodiester linkage.
13. Which moieties of nucleosides are involved in the formation of phosphodiester linkages present in
dinucleotides?
14. The two strands in DNA are not identical but are complementary. Explain
15. What are different types of RNA molecules which perform different functions.?
16. What products would be formed when a nucleotide from DNA containing thymine is hydrolysed?
17. When RNA is hydrolysed, there is no relationship among the quantities of different bases obtained. What
does this fact suggest about the structure of RNA?
18. ●Write a note on DNA fingerprinting.
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