No.

of
S. N. Topic
lectures
1. Importance of Biochemistry. 9 1
2. Properties of Water, pH and Buffer. 2
3. Carbohydrate: Importance and classification. Structures of Monosaccharides, 3
Reducing and oxidizing properties of Monosaccharides, Mutarotation;
Structure of Disaccharides and Polysaccharides.

4. Lipid: Importance and classification; Structures and properties of fatty acids; 2

storage lipids and membrane lipids.

5. Proteins: Importance of proteins and classification; Structures, titration and 2

zwitterions nature of amino acids; Structural organization of proteins.

6. Enzymes: General properties; Classification; Mechanism of action; Michaelis 2

& Menten and Line Weaver Burk equation & plots; Introduction to allosteric
enzymes

7. Nucleic acids: Importance and classification; Structure of Nucleotides, A, B & 2

Z DNA; RNA: Types and Secondary & Tertiary structure.

8. Metabolism of carbohydrates: Glycolysis, TCA cycle, Glyoxylate cycle, 3

Electron transport chain.
9. Metabolism of lipids: Beta oxidation, Biosynthesis of fatty acids. 2
10. Concepts and applications of plant biotechnology: 1
11. Scope, organ culture, embryo culture, cell suspension culture, callus culture, 2
anther culture, pollen culture and ovule culture and their applications;

12. Micro-propagation methods; organogenesis and embryogenesis, Synthetic 2

seeds and their significance; Embryo rescue and its significance; somatic
hybridization and cybrids;
13. Somaclonal variation and its use in crop improvement; cryo-preservation; 1

14. Introduction to recombinant DNA methods: physical (Gene gun method), 2

chemical (PEG mediated) and Agrobacterium mediated gene transfer methods;

15. Transgenics and its importance in crop improvement; 1

16. PCR techniques and its applications; 1
17. RFLP, RAPD, SSR; 1
18. Marker Assisted Breeding in crop improvement; 1
19. Biotechnology regulations 1
Proteins: Importance of proteins and
classification;
Structural organization of proteins.
 Protein
Greek word

proteios

holding the first place

Berzelius suggested the name proteins to the group of organic

compounds that are utmost important to life.
Mulder in 1838 used the term proteins for the high molecular
weight nitrogen-rich and most abundant substances present in
animals and plants.
 Importance of Protein
1. Nutritional role: with essential AA, nitrogen and sulfur.
2. Catalytic role: reaction catalyzing enzymes
3. Hormonal role: mostly hormones and receptors are protein in
nature.
4. Defensive role: providing defense against damage caused by
physical or biological factors.
5. Stress mitigation: mitigate the stress eg: Osmotins, dehydrins,
HSPs
6. Structural role: main structural components in cell membranes of
plants.
7. Gene expression :most factors required for DNA replication,
transcription and mRNA translation are protein in nature.
 Elemental composition of Proteins

• Carbon: 50 - 55%
• Hydrogen: 6 - 7.3%
• Oxygen: 19 - 24%
• Nitrogen: 13 - 19%
• Sulfur: 0 – 4%
• Besides the above, proteins may also contain
other elements such as P, Fe, Cu, l, Mg, Mn, Zn
etc
 Proteins are polymers of amino acids

Protein

Complete hydrolysis with HCL

yield L-ᾳ-amino acid

Peptide bond
Amino end
N-terminus
Carboxyl end-
A.A A.A A.A A.A A.A A.A A.A C-terminus

Protein
 Classification
Based on function
Based on chemical Based on nutrition
nature and solubility

1. Structural Proteins: Keratin,

Collagen
2. Enzymes or catalytic proteins: 1. Simple
1. Complete: protein have
Hexokinase 2. Conjugated all 10 essential AA. Eg
3. Transport proteins: Haemoglobin 3. Derivative albumin, milk casein
4. Hormonal proteins: Insulin and 2. Partially incomplete
growth hormone protein: partially lacking
5. Contractile proteins: Actin and one or more essential
myosin
amino acid (AA). Eg
6. Storage proteins: Ovalbumin
7. Genetic proteins: Nucleoproteins
wheat and rice proteins
8. Defensive proteins: 3. Incomplete proteins:
Immunoglobulins completely lack one or
9. Receptor proteins: for hormones more essential amino
and viruses acid. gelatin
 Proteins based on chemical nature and solubility: it is based on the amino acid
composition, structure, shape and solubility properties.

1. Simple: 2. Conjugated: 3. Derivative: obtained by

Composed by only (Amino acid+ non hydrolysis of simple and
amino acid amino acid group conjugated proteins with
(prosthetic group) acids, alkalis or enzymes.

Globular protein Fibrous protein

Spherical in shape •Fiber like in shape

Mostly water soluble •Tough and water insoluble.
and easily digestible. •Used to build a variety of materials that support and
protect specific tissues eg skin, hair, nails.
Example: Enzymes,
Example: Collagen and Keratin
hormones and antibodies
 2. Conjugated or compound
(Amino acid + non amino acid components –prosthetic group)
These proteins are classified into six major groups based on
nature of prosthetic group as decribed below:
1. Nucleoproteins: Protein+Nucleic acid, found in nucleus. Eg:
Histone
2. Lipoproteins: Conjugates of lipid+protein, eg lecithin,
cephaline
3. Phosphoproteins: Phosphoric acid+protein, eg Casein in milk
4. Glycoproteins: Carbohydrates covalently attached to
polypeptide chain. Eg Fibrinogen
5. Chromoproteins: colored proteins, pigment+protein.
Chlorophyll, carotenoids
6. Metalloproteins: these proteins represent the group of
enzymes which require metal as prosthetic group.eg: Enzymes
involved in kreb cycle.
 C. Derived proteins

Hydrolysis
By acids, alkalis or enzymes

Denatured or degraded proteins

Types: Derived Proteins

Primary derived proteins Secondary derived proteins

1. Metaproteins 1. Proteoses: produced by hydrolysis of
2. Coagulated proteins metaproteins. Eg: albuminose from albumin
2. Peptones: produced by hydrolysis of proteoses.
3. Peptides: produced by hydrolysis of natural
proteins
Structural Organization of Proteins

• The structure of proteins is rather complex which can be divided

into 4 levels of organization:
1. Primary structure : The linear sequence of amino acids
forming the backbone of proteins (polypeptides).
2. Secondary structure: The spatial arrangement of protein by
twisting of the polypeptide chain.
3. Tertiary structure: The three dimensional structure of a
functional protein.
4. Quaternary structure : Some of the proteins are composed of
two or more polypeptide chains referred to as subunits. The
spatial arrangement of these subunits is known as quaternary
structure.
 1. Primary structure of protein
• The sequence in which amino acids are
arranged in a polypeptide chain of a
protein is called as primary structure.
• The primary structure is held together
by peptide bonds that are made during
the process of protein biosynthesis.
• In the chain of amino acids which
constitute protein, the amino acid
present at the left end is the first AA
(called N-terminal amino acid), here as
at the right end is the last amino acid
known as C-terminal amino acid.

C-terminal amino
acid
Example of primary structure of protein: Structure of
insulin
The simplest protein is Insulin. Insulin consists of 51 amino
acid residues.
It is the first protein to have its primary structure determined.
Insulin is a protein hormone composed of two polypeptide
chains: A chain (21 amino acids) and B chain (30 amino acids).
 SECONDARY PROTEIN STRUCTURE

• Two basic forms: alpha-helices and beta-sheets

• Hydrogen bond interactions within the alpha-helix and beta-
sheet provide the stability of secondary structure of proteins.
• Alpha-helices
• Low energy conformations that enable higher-order packing of
proteins.
• Large or charged amino acid groups (such as proline) can
disable the alpha helix conformation by manually disrupting
the hydrogen bond interactions.
 Beta-pleated sheets

• More structurally diverse than alpha helices and thus facilitate

more diverse protein functions.
• Create stable, diverse structures within a protein to allow
higher order functions.
• There are two notable ways in which the beta-pleated sheet
can exist:
-Parallel — the peptide chain advances in a single direction.
-Anti-parallel — the peptide chain advances in two opposite
directions.
More stale because
the hydrogen
bonding pattern is
more optimal
 TERTIARY PROTEIN STRUCTURE

• Peptide chain with its secondary structure may be further

folded & twisted about itself forming 3D arrangement of a
functional protein.
• Tertiary structure is the complete three dimensional structure
of a polypeptide chain.
• It is a compact structure. Hydrophobic side chains held interior
and hydrophilic groups are on the surface of the protein
molecule.
• The function of a protein depends on its tertiary structure. If
this is disrupted, it loses its activity
• Primarily comprises alpha helices and beta sheets
 QUATERNARY PROTEIN STRUCTURE

• Proteins having single polypeptide chains: Monomeric

proteins
• Proteins having more than one polypeptide
chains: Oligomeric proteins
• A multi subunit protein is also referred to as
a multimer. Multimeric proteins can have from two to
hundreds of subunits.
• Each polypeptide chain in the oligomeric protein is
called subunits or monomers.
• Dimer – 2 polypeptide chains,
• Tetramer – 4 polypeptide chains.
TERTIARY & QUATERNARY PROTEIN BONDING

• The most significant stabilizer of tertiary and quaternary

protein structures are hydrophobic interactions.
• The following additional forces stabilize these structures:
-Hydrophilic interactions.
-Electrostatic interactions.
-Hydrogen bonds between side chains.
-Strong disulfide bonds.