Polysaccharides: Glycosidic Bonds

CHAPTER 5
Disaccharides consist of two monosaccharide residues linked together by glycosidic

bonds
The polysaccharides are defined as the polymers of sugars and their various
derivatives, such as glucosamine and galactosamine linked together by glycosidic
bonds.
There are two types of glycosidic linkages depending on the types of anomers
-glycosidic Linkages and -glycosidic Linkages.
Starch is the main storage form of polysaccharides in plants and glycogen in animals
Cellulose, a structural polysaccharide, is the main component of the plant cell walls and
is the most abundant biopolymer in the biosphere.
Chitin, the material of the insect exoskeleton and peptidoglycan, the main components
of the bacterial cell walls
If the polysaccharides are composed of the same type of monomers or sugars, they are
called homopolysaccharides
if more than one type of sugar or sugar derivatives are involved in the formation of the
polysaccharides, they are called heteropolysaccharides.
Starch is the polymer of glucose units linked together by -1 > 4 linkages and/or -1 > 6
linkages.
starch is a mixture of two types of glucose chains—amylose and amylopectin
Glycogen is the storage form of carbohydrates in animals and is stored in liver and
muscles.
Cellulose: No branchings occur in cellulose, a linear molecule
Cellulose is the most important structural component of nearly all green plants’ cell walls.
The
glucose units are linked by -1 > 4-glycosidic linkages.
Peptidoglycan: This is a heteropolysaccharide present in the cell walls of bacteria
imparting rigidity and shape to the cells
Fructose-6-phosphate is an important intermediate of both photosynthesis and glycolysis.
Glucose-1-phosphate + ATP + H2O →ADP-glucose + 2 Pi

ADP-glucose + Glucose-1-phosphate →ADP-glucose-glucose + Pi
Proteins or polypeptides play an outstanding part in all cell activities. They act as
biological catalysts (= enzymes
-They are linear chains consisting of a sequence of 20 amino acids indifferent
combinations linked exclusively by peptide bonds.
*The peptide bonds are formed by the reaction of the primary amino group of one
amino acid with primary carboxyl group of another amino acid with the elimination of a
molecule of water (Figure 5.8). Thus, it is a condensation reaction.
This type of linkage causes a polarity for the polypeptide chain. One end has the
amino group and is called the N-terminus, while the other end is terminated by a
free carboxyl group and is called the C-terminus
(Nobel Laureate)Frederic Sanger, showed for the first time that proteins have a
definite amino acid sequence and a specific three-dimensional structure that is
determined by the amino acid sequence. He found out that certain reagents suchas
fluoro-dinitro-benzene (FDNB) known as Sanger’s reagent can react specifically with the
free NH2 group of the amino acid at the N-terminal of a polypeptide. Fluoro-DNB reacts
with the N-terminal amino acid and on acid hydrolysis it yields a yellow DNP derivative of
the amino acid, which can be separated and identified by ion-exchange chromatography.
The most popular direct protein-sequencing technique in use today is the Edman
degradation procedure
The whole method, including the reaction steps and the identification of PTHamino acid
derivative, is automated and the instrument that can carry out these reactions is known
as a sequenator
The sequence of R-groups along the chain is called the primary structure
Secondary structure refers to the local folding of the polypeptide chain.
Tertiary structure is the arrangement of secondary structure elements in three-
dimensions and quaternary structure describes the arrangement of a protein’s sub-units.
Professor G.N. Ramachandran, systematically studied the various possible and

angles via the computer to find stable conformations and predicted the different types
of secondary structures in protein molecules
One of the most common secondary structure patterns is called the alpha helix or
helix discovered by Pauling and Corey and published in the Proceedings of the
National Academy of Sciences (PNAS) in 1951
The -helix is the main structural component of the protein -keratinpresent in hair
Random coils are present along with -helices and -sheets in most of the globular
proteins
To combine helices and sheets in their various combinations, protein structuresmust
contain turns that allow the peptide backbone to fold back which are called beta turns or
-turns.
Enzymes are the biocatalysts that control almost all cellular reactions. A catalyst is a
compound, which accelerates a chemical reaction without undergoing any change in
quality or quantity.
Enzymes function as catalysts, which are substances that facilitate (speed up) reactions
without actually entering into the reaction
Rate of a reaction = quantity of product formed per minute
This is the energy of activation (Ea). The activation energy can be defined as the energy
needed by a molecule to take part in a reaction
This hypothesis that explains the mechanism of enzyme substrate interaction is known
as the Lock and Key hypothesis
Some enzymes change the shape of the active center slightly to accommodate the
substrate molecules, a process known as induced fit. This theory is known as the
induced fit theory
Enzymes typically work in chains called metabolic pathways in which the product of one
reaction is the substrate of the next.
The turnover number is the number of substrate molecules converted to product per
second by one molecule of enzyme
Cofactors
Proteins are often associated with other chemical groups known as cofactors or
prosthetic groups. Enzymes are no exception
In addition to enzymes some non-enzyme proteins also have prosthetic groups or the
non-protein parts. They are:
Nucleoproteins: have nucleic acid as the prosthetic group
Glycoproteins: have carbohydrate as the prosthetic group
Lipoproteins: have lipid as the prosthetic group
Friedrich Miescher discovered nucleic acids, the molecular substrate of the genetic
material. He also demonstrated that the regulation of breathing depends on CO2
concentration in the blood.
Nucleic acids are polymers consisting of nucleotides that are linked by

phosphodiester bonds (polynucleotides).
RNA is the non-genetical nucleic acids except in some viruses such as HIV, where
it is the genetic material
Deoxyribonucleic acid or DNA, forms the genetic material of almost all organisms
except some viruses, which have RNA as the genetic material and therefore are called
RNA viruses. DNA is a very long polymer and always exists as a doublestranded helical
molecule.
The ratio A + T/C + G is specific for every species. This is known as the Chargaff rule.
James Watson and Francis Crick proposed a model, the Watson-Crick model for
the structure of DNA. They published their findings in 1953 in the journal, Nature.
The Watson-Crick model (subsequently verified by additional data) explained almost all
the properties of DNA as the genetic material including the mechanism of its replication
by using both of the DNA strands as matrices.
Lipids are a class of hydrophobic molecules but very much miscible with organic solvents
such as hexane, chloroform, ethyl acetate, etc. They are a group of biologically-important
lipids that show amphipathic characteristics
The most common phospholipid is lecithin. Phospholipids also make excellent

emulsifiers and are used in a number of food and household products

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CHAPTER 5

Disaccharides consist of two monosaccharide residues linked together by glycosidic

Fructose-6-phosphate is an important intermediate of both photosynthesis and glycolysis.

Glucose-1-phosphate + ATP + H2O →ADP-glucose + 2 Pi

Professor G.N. Ramachandran, systematically studied the various possible and

Rate of a reaction = quantity of product formed per minute

Nucleic acids are polymers consisting of nucleotides that are linked by

The most common phospholipid is lecithin. Phospholipids also make excellent

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