1. History
Protein
Represented by Habib Ur
Rahman
Major
Classes
definition
Sources
Amino
Acid
Different
Bonds
Protein
Structure
Typesof
Protein
Functio
n
3. Historydefinition
Sources
Amino
Acid
Protein is a substance that has amino
acids as basic building block
compounds and carbon, hydrogen,
oxygen, nitrogen and sometimes
sulfur and is found in many foods. An
example of a protein is the type of
nutrient found in meats
4. HistorydefinitionSourcesAmino
Different
Bonds
Protein
Structure
Protein
General Structure
Amino acids are
molecules used to
build proteins due to
which the Amino acid
are called the building
block of protein.
All amino acids have a central carbon atom surrounded by a
hydrogen atom, a carboxyl group (COOH), an amino group (NH2),
and an R-group. It is the R-group or side chain that differs
between the 20 amino acids.
5. HistorydefinitionSourcesAmino
Different
Bonds
Protein
Structure
Protein
Types of Amino Acid
Essential Amino Acids Non-Essential Amino Acids
Essential amino
acids cannot be made by
the body so you must get
them from your diet.
Non-Essential amino
acids can be made by the
body
e.g. e.g.
Histidine
Isoleucine
Valine
Methionine
Alanine
Arginine
Glutamic
Glycine
6. HistoryMajor
Sources
Amino
Acid
7 Major Classes of Proteins
• Structural e.g. hair.
• Contractile e.g. Actin(muscle cells)
• Storage e.g. egg whites.
• Defense e.g. antibodies.
• Transport e.g. hemoglobin.
• Signaling e.g. hormones
• Enzymes e.g. lactose
11. HistorydefinitionSourcesAmino
Different
Protein
Structure
Typesof
Protein
Functio
n
Hydrogen bonds
• The hydrogen-bond also play a
very important roles in proteins'
structure because it stabilizes the
secondary, tertiary and quaternary
structure of proteins which formed
by alpha helix, beta sheets, turns
and loops.
• The hydrogen-bond connected the
amino acids between different
polypeptide chains in proteins
structure.
13. HistorydefinitionSourcesAmino
Different
Protein
Structure
Typesof
Protein
Functio
n
Ionic Bonds
Electrostatic interactions
occur between two
oppositely charged
molecules.
Disulfide Bridges
A disulfide bond can be form
between two cysteines
( C3H7NO2S)through
oxidation. These are also the
strongest covalent bonds within
a protein's tertiary structure.
Hydrophobic Interaction
• The hydrophobic
interaction originates
from the tendency of
non-polar molecules to
minimize their
interactions with water.
• When non-polar
molecules interact with
water, these molecules
tend to cluster together
in the center to form a
micelle.
15. HistorydefinitionSourcesAmino
DifferentProtein
Typesof
Protein
Functio
n
Primary structure
• Describe the number and sequence of Amino acid in the
protein molecule
• F.Sanger first describe the sequence and the number of the
amino acids in the protein molecule
• He concluded that
• Insulin is made up of 51 amino acid in two chain
• These two chains are held together by Disulphide Bond
• Hemoglobin is made up of four chains two alpha and two
beta
• Alpha chains contain 141 amino acid and each beta chains
contains 146
17. HistorydefinitionSourcesAmino
DifferentProtein
Typesof
Protein
Functio
n
Secondary structure
• Within the long protein chains there are regions in which
the chains are organized into regular structures known as
alpha-helixes ,beta-pleated sheets
• These are the secondary structures in proteins.
• It forms the spiral formation of the basic polypeptide chain
• The helix is uniform throughout the structure containing
3.6 amino acid in each turn
• These secondary structures are held together by hydrogen
bonds.
• The beta plated sheet is formed by the folding back of the
polypeptide
19. HistorydefinitionSourcesAmino
DifferentProtein
Typesof
Protein
Functio
n
Tertiary structure
• Polypeptide chain bends and folds upon its-
self forming globular protein
• Structure is maintained by the different types
of the bonds
• Ionic, covalent, and disulphide bond
• The three-dimensional structure of a protein
or nucleic acid
• Amino acids form secondary structures such as
alpha helices, beta sheets, and random coils,
which in turn fold on themselves to form the
tertiary structure of the protein
23. HistorydefinitionSourcesAmino
DifferentProteinTypesof
Functio
n
Fibrous protein
• Contain one or more
polypeptide in the form of
fibrils
• Insoluble in water
• Secondary structure is the
main component
• They are elastic in nature
• Play vital role in the
maintenance of structure of
the cell and cell organelles
Example
• Silk fiber (from the silk
warm and spider web)
• Myosin (in muscle cells)
• Fibrin (of blood cells)
• Keratin (nail and hair)
24. HistorydefinitionSourcesAmino
DifferentProteinTypesof
Functio
n
Globular protein
• These are spherical or elliptical in structure this is
because of the multiple folding of the
polypeptide chain
• A variety of bonding interactions including
hydrogen bonding, salt bridges, and disulfide
bonds hold the various chains into a particular
geometry.
• Tertiary structure is most important
• Globular proteins are somewhat soluble in the
aqueous solution of acids, salt and aqueous
alcohol
• They change their structure when structure or
physical or physiological changes takes place
Example
• Enzyme
• antibodies
• hormones
• hemoglobin
25. HistorydefinitionSourcesAmino
DifferentProteinTypesofFunctio
Important Functions of Protein in Your Body
• Growth and Maintenance. Your body needs protein for growth and
maintenance of tissues. ...
• Causes Biochemical Reactions. ...
• Acts as a Messenger. ...
• Provides Structure. ...
• Maintains Proper pH. ...
• Balances Fluids. ...(Across the membrane)
• Bolsters Immune Health. ...
• Transports and Stores Nutrients.