Biomolecules

Chemistry of Carbohydrates:: Carbohydrates are polyhydroxy aldehydes or polyhydroxy ketones, or large

polymeric molecules which on hydrolysis yield polyhydroxy aldehydes and polyhydroxy ketones.
 On the basis of hydrolysis, carbohydrates may be classified as monosaccharides, oligasaccharides and
polysaccharides.
 On the basis of taste they can be classified as sugars and non-sugars, sugars are sweet in taste and soluble in water.
Non sugars are tasteless and water insoluble
 On the basis of reducing behaviour they can be classified as reducing sugars and non-reducing sugars.
Carbohydrates which reduce Fehling’s solution are called Reducing sugars. While others are non reducing
sugars.
Monosaccharides ; Monosaccharides possessing an aldehyde group are called aldoses, whereas those containing a
keto group are termed as ketoses. They can be divided in D &L families. When -OH group on the carbon atom
adjacent to -CH20H group lies on the right hand side in the Fischer projection, the monosaccharide is said to have D-
configuration & if it lies to the left hand side,it is said to have L-configuration.
Glucose: It is prepared either by the hydrolysis of sucrose or the starch. It exhibits chemical reactions characteristic of —
CHO group, primary —OH group, secondary —OH group and cyclic structure. Glucose shows mutarotation which can be
represented as follows :

 Glucose on reduction forms sorbitol.

 On oxidation with bromine water forms Gluconic acid & with HNO 3 glucaric acid .
 It forms peta- acetate indicating 5 OH groups
 Glucose does not restore pink color of Schiffs reagent,does not react with 2,4-DNP and sodium bisulphite. Two
isomeric monomethyl derivatives known as -D-glucoside and -D-glucoside are formed, on reaction of glucose
with methanol in presence of dry HCl gas. This indicates that glucose has a cyclic structure
 In glucose, the —CHO group interacts with the —OH group at C5 leading to the formation of a six-membered ring.
This makes C1 asymmetric and the stereoisomers—-D-glucose and -D-glucose are obtained. These are
anomers.
 In fructose, the —OH group present at C6 interacts with the ketogroups at C2 to form a hemiketal resulting in the
formation of a six-membered ring. Now C: becomes asymmetric and we have two anomers--D-fructose and -D-
fructose.
 On treating with dil sodium hydroxide solution, glucose is converted into a mixture of D-glucose, D-mannose and
D-fructose. This reaction is known as Lobry de Bruyn-van Ekenstein rearrangement. Mannose and fructose also
undergo this type of change. Because of this reason fructose also gives Tollen’s Reagent and Fehling’s Solution
test although it doesn’t have aldehyde group.
Disaccharides: Disaccharides may be supposed to be formed by a condensation reaction between two
monosaccharides, one acing as a hemiacetal and the other as an alcohol. The new linkage thus, formed is called
glycosidic linage.
Maltose is a reducing sugar. Its molecule is composed of two units of -D-glucose joined together by an -glycosidic
linkage between C1 of the first unit and C4 of the second unit.
Sucrose is a non-reducing sugar. Its molecule is composed of a six-membered -D-glucose and a five-membered -D-
fructose unit joined together by an a, -glycosidic linkage between C 1 of glucose unit and C, of fructose unit. Sucrose is
dextrorotatory (D = 66.5o). Upon hydrolysis it gives an equimolar mixture of D-glucose (+52.5°) and D-fructose (-92.4°)
and the entire solution becomes laevorotatory. This process is called inversion of cane sugar.
Lactose is a reducing sugar & is found only in animals & not in plants. Its molecule is composed of -D-galactose & -D-
glucose units held together by -glycosidic linkage between C1 of galactose & C4 of glucose units.
Polysaccharides: Polysaccharides are condensation polymers and have the general formula (C6H10O5)n.
Starch is a polymer of -glucose and consists of two components—amylose (20%) and amylopection (80%).
 Amylose is the water soluble component and is a linear polymer of -glucose consisting of -D-glucose units
linked together through -glycosidic linkages involving C1 of one glucose unit and C4 of the next glucose unit.
 Amylopectin is the water insoluble component and is composed of chains of 25 to 30 -D-glucose units joined
together through -glycosidic linkage involving C1 of one glucose unit and C4 of the next glucose unit. These
chains in turn are connected to each other by 1,6-linkages.
Cellulose is a linear polymer of -glucose. The -glucose unit are linked together through -glycosidic linkages between CI
of one glucose unit &C4 of the next glucose unit.Other polysaccharides are glycogen, gums & pectins.
Functions of carbohydrates: Carbohydrates act as the major source of energy for animals and human beings. They act
as food reserve in plants (starch) and animals (glycogen) and are the structrual material for the cell walls.
Chemistry of -Amino acids and Peptides
-Amino acids : -Amino acids are the basic building units of proteins. The -carbon in all aminoacids (except glycine) is
asymmetric and hence all amino acids exist in two stereoisomeric forms. All amino acids are are optically active
having L-configuration. These are of three types—neutral, acidic and basic.
There are 20 commonly occurring amino acids in proteins. Out of these, only 10 are synthesised by the human body. They
are not essential to be supplied in the diet and are called non-essential amino acids. However, the remaining 10 are not
synthesized by the human, body and must be supplied in the diet. They are termed as essential amino acids. Deficiency
of these amino acids leads to a disease called Kwashiorkor.
 In aqueous solution, amino acids form a dipolar ion called zwitter ion H3N+—CH(R) —COO-. As a result, amino
acids show amphoteric behaviour. In acidic solution they exist as positive ion s (H3N+-CH(R)-COOH), while
in basic solution they exist as negative ions (NH2 -CH(R)—C00- ). The acidic functional group in amino acid is
H3N+ and basic function group is COO-
 On passing electric current, the amino acid ion moves towards cathode in acidic solution and towards anode in
basic solution. The pH at which amino acid molecule does not migrate to either electrode is called isoelectric
point.
Peptides and peptide bond: The compounds obtained by the condensation of two or more, same or different -
amino acids are called peptides. Polypeptides are obtained by the condensation of a large number of same or different a-
amino acid molecules.When two -amino acids combine together, the —COOH group of one amino acids condenses with
the —NH2 group of the other amino acid to form a new linkage —CO—NH--, called the peptide bond.
Chemistry of Proteins: Proteins are polypeptides having at least 100 or more amino acid units and possess
molecular mass greater than 10,000.
 On the basis of molecular structure, proteins may be classified as, fibrous proteins and globular proteins, whereas
on the basis of composition they may be classified as simple proteins, conjugated proteins and derived proteins.
Structure of proteins:
 The primary structure of proteins refers to the sequence of amino acids held together by peptide linkages.
 The secondary structure refers to the shape in which polypeptide chains are arranged. Two types of secondary
structures -helix structure and -conformation or pleated sheet structure have been suggested for proteins. The -
helix is also known as 3.613 helix because each turn of the helix has about 3.6 amino acids and a 13 member ring
is formed by hydrogen bonding.
 The tertiary structure refers to the three dimensional shape of the protein molecule which results from the twisting,
bending and folding of the -helix.
 Quaternary structures represents the spatial orientation of multiple subunits. For example, quarternary structure of
hemoglobin consists of 4 polypeptide chain.Two -chain of 141 -amino acid & 2 -chain of 146 -amino acids.
Denaturation of proteins: The process which leads to a change in the physical and biological properties of a protein
without affecting its chemical composition is called denaturation.
 It may be effected by the action of heat, alcohol. conc. acids, radiation etc.
 Denaturation changes only the secondary and tertiary structures of protein, the primary structure remains
unchanged.
 This process is irreversible in most cases. However, in some cases,it may be reversed & termed as renaturation.
 Denaturation leads to increase in entropy.
Biological functions of proteins: Proteins are essential for life. They serve as basic building materials for tissues of
animals (structural materials) and act as delivery vans in the body. As enzymes, they catalyse biological reactions, as
hormones they regulate metabolic processes and as antibodies they protect the body against toxic substances. They also
act as food reserve.
Enzymes: Enzymes are an important class of globular proteins which act as biocatalysts in the living systems and are
produced by the living cells.
 They are highly specific in their action and are highly efficient.
 Some enzymes are associated with a non-protein component called prosthetic group. When the prosthetic group is
a metal ion, it is called a cofactor. If it is a small organic molecule, it is called coenzyme.
 The deficiency of enzymes in living beings causes certain diseases. Phenyl ketone urea is caused by the
deficiency of enzyme phenylamine hydroxylase. Disease albinism is caused by the deficiency of tryosinase.
Chemistry of Nucleic Acids: Nucleic acids constitute an important class of biomolecules which are present in the
nuclei of all living cells. These are biopolymers. The monomer unit present in them is called nucleotide. Thus, they are
polynucleotides. Nucleic acids are of two types—(a) deoxyribonucleic acid (DNA), and (b) ribonucleic and (RNA).
Consituents of nucleic acids: A nucleotide consists of a sugar, a nitrogen containing heterocyclic base, and a
phosphate group.
Base + Sugar = Nucleoside Base + Sugar + Phosphate = Nucleotide
 Two types of pentose sugar-ribose (in RNA) and 2-deoxyribose (in DNA) are present in nucleotides.
 The nitrogen base present is a derivative of either purine or pyrimidine.
 The commonly found purines are adenine (A) and guanine (G), whereas the commonly found pyrimidines are
thymine (T), cytosine (C) and uracil (U).
 The base residues present in DNA are A, G, C and T; while those present in RNA are A, G, C and U.
 Depending upon the nature of sugar unit present, nucleosides are of two types—ribonucleosides and
deoxyribonucleosides. Similarly, nucleotides are also of two types—ribonucleotides and deoxyribonucleotides.
Primary structure of nucleic acids: The sequence in which the four nitrogeneous bases (A, G, C,T or U) are attached to
sugar-phosphate backbone of a nucleotide chain in a nucleic acid is called the primary structure of those nucleic acids.
Structure of DNA and RNA: James Watson and Francis Crick (1953) proposed a double helix structure of DNA. The
DNA molecule consists of two right handed helical nucleotide strands coiled together in the form of a double helix.
 The two strands are held together by hydrogen bonds (A =T, G  C) between the bases present on their
back bones. The two strands are complementary because the base sequence of one polynucleotide chain fixes
the base sequence of the other chain.
 The two strands of DNA separate on heating and reunite on cooling. The temperature at which the two strands
separate completely is called melting temperature (Tm) which is specific for each specific sequence.
 In RNA, helices are present but they are only single stranded.
Replication: It is the process by which a single DNA molecule produces two identical copies of itself during cell division.
DNA replication follows the base pairing rules (i.e., A pairs with T and G with C) and is a direct consequence of the base
pair specificity.
Protein synthesis: The DNA molecules existing in the chromosomes hold the code for protein synthesis and act as
instruction mannual. The genetic information coded in DNA is in the form of specific base sequences. The synthesis of
specific proteins occurs in the following two steps :
(i) Transcription : This involves the copying of DNA sequences into a complementary RNA molecule called m-RNA. When
A strand is synthesised, the DNA-RNA double helix splits to form three types of RNA-m-RNA, t-RNA & r-RNA. These migrate
to the cytoplasm and perform specific functions in protein synthesis. DNA returns to its original double helix structure.
(ii) Translation : The sequence of three nucleotides on a polynucleotide chain is known as codon. The process of translation
involves the reading of triplet codes (codons) expressed in mRNA on the ribosomal particles by t-RNA. Each triplet of
t-RNA then transfers the specific amino acid and carries it to the proper position on the ribosomal particle. The protein thus
synthesised is then released from the ribosomal particle.
Gene and genetic code: The DNA sequence that codes for a specific protein is called a gene and the relationship
between the nucleotide triplets and the amino acids is called the genetic code,
Mutation: A chemical change in a DNA molecule which could lead to synthesis of proteins with a different amino acid
sequence is called mutation. The proteins thus produced may not have biological activity.
Vitamins: Vitamins constitute a group of organic compounds which are required in very small amounts for the healthy
growth and normal functioning of animal organisms. The important vitamins are A, B-complex, C, D, E, K and H.
 Vitamins A, D, E and K are fat soluble, whereas vitamins B-complex and vitamin C are water soluble. Vitamin H
(biotin) is neither fat soluble nor water soluble.
 Vitamins are biological catalysts and are daily needed but only in small amounts.
 A deficiency of one or more vitamins leads to characteristic deficiency symptoms and causes specific diseases.