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PROTEINS
CONTENT
•Introduction
•Source
•Classificatio
n
•Structure
•General
properties
•Importance
of protein
SOURCE OF PROTEINS
 PLANT SOURCE:

grains,cereals,legumens,nuts ,seeds,
fruits,roots and tubers like
yams,cassava,and sweet potato.
 ANIMAL SOURCE:
meat,egg,fish and milk and milk derived
food
INTRODUCTION
 Proteins are polymers of

amino acids

bonded by peptide linkages.
 Their molecular weights range from 5000
to many millions.
 They occur in all living cells.
 They are present in muscle, skin, hair and
other tissues that make up the body’s nonbony structure.
 As enzymes they catalyze

biochemical reactions.
 As hormones they regulate
metabolic processes.
CLASSIFICATION
Proteins

chemical

molecular
Classification by
chemical composition
Chemical
composition

simple
proteins
Conjugated
proteins
According to this system, proteins
are divided into two classes;
1. SIMPLE PROTEINS:
The simple proteins are those
which are made of chains of
amino acid units only, joined by
amide linkages.
Upon hydrolysis, they yield
mixtures of amino acids and
nothing else.
Example;
 Albumin
 Globulin
 Glutenin
2.CONJUGATED PROTEINS:
These molecules are made of a simple
protein united covalently or noncovalently with a non-protein factor.
The non-protein portion is called
prosthetic group or cofactor.
Examples:
 Glyco-protein
 Phospho-proteins
 Chromo-proteins
CLASSIFICATION BY
MOLECULAR SHAPES
Molecular
shape

Fibrous
proteins
Globular
proteins
This shape-classification divides protein
into two types depending on their molecular
shape:
1.
FIBROUS PROTEIN:
In these proteins the poly-peptide
chains coil about one another and are
held together by strong inter-chain
hydrogen bond.
Thus their molecules assume the shape
of large linear fibers which are used
for connections, support, and the
structure in living organisms.
They are insoluble in water.
Examples:
Keratin
Myosin
Collagen
2.GLOBULAR PROTEINS
 Their molecules are globular or

roughly spherical in shape.
 They are made of poly-peptide
chains coiled back and forth on
themselves so as to make compact
spheroid molecules.
 The poly-peptide chains are held
together firmly by inter chain
hydrogen bonds.
 Globular proteins are generally soluble in
water or solution of acids, bases and salts.
 The function of globular proteins is to
maintain and regulate life processes in the
living organism.
 Examples:
 Enzymes
 Insulin
 Hemoglobin
 Antibodies
 Cytochromes
STRUCTURE OF PROTEINS
The proteins are made up of polymers of amino
acid by peptide bonding, hence its basic structure
will be:
Proteins have a complex 3-dimensional structure.
It is studied step by step at four different
levels, rather than as a whole.
1. Primary structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure
PRIMARY STRUCTURE
 The primary structure of a protein refers to the

sequence of amino acid.
 The amino acid sequence in many proteins have been
determined and following observations are made:
1. A protein may contain more than one amino acid
chain.
2. Sequence of amino acids in the protein chain is
essentially random.
3. Small variation in the sequence of amino acid have
pronounced effects on the properties of protein.
SECONDARY STRUCTURE
 The secondary structure of a protein

refers to the shape in which long amino
acid chains exist.
 Many proteins consist of amino acid chain
coiled into a spiral known as an -helix.
 The spiral is held together by hydrogen
bonds between N-H and C=O groups
vertically adjacent to one another in the
helix.
TERTIARY STRUCTURE
 An

-helix may be considered to be a
piece of rope which is free to bend twist
and fold.
 The tertiary structure of a protein
refers to the final 3-dimensional shape
that results from twisting, bending and
folding of protein helix.
QUATERNARY STRUCTURE
 Complex proteins are often form from two

or more amino acid chains rather then a
single amino acid chain.
 Each chain is a complete protein with a
characteristic primary, secondary and
tertiary structure.
 The quaternary structure refers to the
way in which these amino acid chains of a
complex protein are associated with each
other.
GENERAL PROPERTIES
Most proteins are colorless amorphous solid.
They have no definite melting point.
Proteins like amino acids, exists as
zwitterions.
 Most proteins are optically active.
 Proteins, like amino acid, have isoelectric
points.
 Proteins form colloidal dispersion in
water.They can pass through a filter paper but
not through a membrane.



Proteins are easily precipitated :
By heat
By ethyl alcohol
By conc. inorganic acid
By silver nitrate
By picric acid or tannic acid
By uv rays and x-rays
Simple proteins can be hydrolysed with acids
(HCl),alkalies (NaOH),or enzymes to give
component amino acid.
 Proteins are oxidized on burning and
putrification.The product include N,CO2 and

1.
2.
3.
4.
5.
6.


water.
IMPORTANCE
Protein Structure and Classification Guide

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Protein Structure and Classification Guide

  • 3. SOURCE OF PROTEINS  PLANT SOURCE: grains,cereals,legumens,nuts ,seeds, fruits,roots and tubers like yams,cassava,and sweet potato.  ANIMAL SOURCE: meat,egg,fish and milk and milk derived food
  • 4. INTRODUCTION  Proteins are polymers of amino acids bonded by peptide linkages.  Their molecular weights range from 5000 to many millions.  They occur in all living cells.  They are present in muscle, skin, hair and other tissues that make up the body’s nonbony structure.
  • 5.  As enzymes they catalyze biochemical reactions.  As hormones they regulate metabolic processes.
  • 8. According to this system, proteins are divided into two classes; 1. SIMPLE PROTEINS: The simple proteins are those which are made of chains of amino acid units only, joined by amide linkages. Upon hydrolysis, they yield mixtures of amino acids and nothing else.
  • 10. 2.CONJUGATED PROTEINS: These molecules are made of a simple protein united covalently or noncovalently with a non-protein factor. The non-protein portion is called prosthetic group or cofactor. Examples:  Glyco-protein  Phospho-proteins  Chromo-proteins
  • 12. This shape-classification divides protein into two types depending on their molecular shape: 1. FIBROUS PROTEIN: In these proteins the poly-peptide chains coil about one another and are held together by strong inter-chain hydrogen bond. Thus their molecules assume the shape of large linear fibers which are used for connections, support, and the structure in living organisms.
  • 13. They are insoluble in water. Examples: Keratin Myosin Collagen
  • 14. 2.GLOBULAR PROTEINS  Their molecules are globular or roughly spherical in shape.  They are made of poly-peptide chains coiled back and forth on themselves so as to make compact spheroid molecules.  The poly-peptide chains are held together firmly by inter chain hydrogen bonds.
  • 15.  Globular proteins are generally soluble in water or solution of acids, bases and salts.  The function of globular proteins is to maintain and regulate life processes in the living organism.  Examples:  Enzymes  Insulin  Hemoglobin  Antibodies  Cytochromes
  • 16. STRUCTURE OF PROTEINS The proteins are made up of polymers of amino acid by peptide bonding, hence its basic structure will be:
  • 17. Proteins have a complex 3-dimensional structure. It is studied step by step at four different levels, rather than as a whole. 1. Primary structure 2. Secondary structure 3. Tertiary structure 4. Quaternary structure
  • 18. PRIMARY STRUCTURE  The primary structure of a protein refers to the sequence of amino acid.  The amino acid sequence in many proteins have been determined and following observations are made: 1. A protein may contain more than one amino acid chain. 2. Sequence of amino acids in the protein chain is essentially random. 3. Small variation in the sequence of amino acid have pronounced effects on the properties of protein.
  • 19.
  • 20. SECONDARY STRUCTURE  The secondary structure of a protein refers to the shape in which long amino acid chains exist.  Many proteins consist of amino acid chain coiled into a spiral known as an -helix.  The spiral is held together by hydrogen bonds between N-H and C=O groups vertically adjacent to one another in the helix.
  • 21.
  • 22. TERTIARY STRUCTURE  An -helix may be considered to be a piece of rope which is free to bend twist and fold.  The tertiary structure of a protein refers to the final 3-dimensional shape that results from twisting, bending and folding of protein helix.
  • 23.
  • 24. QUATERNARY STRUCTURE  Complex proteins are often form from two or more amino acid chains rather then a single amino acid chain.  Each chain is a complete protein with a characteristic primary, secondary and tertiary structure.  The quaternary structure refers to the way in which these amino acid chains of a complex protein are associated with each other.
  • 25.
  • 26.
  • 27.
  • 28. GENERAL PROPERTIES Most proteins are colorless amorphous solid. They have no definite melting point. Proteins like amino acids, exists as zwitterions.  Most proteins are optically active.  Proteins, like amino acid, have isoelectric points.  Proteins form colloidal dispersion in water.They can pass through a filter paper but not through a membrane.   
  • 29. Proteins are easily precipitated : By heat By ethyl alcohol By conc. inorganic acid By silver nitrate By picric acid or tannic acid By uv rays and x-rays Simple proteins can be hydrolysed with acids (HCl),alkalies (NaOH),or enzymes to give component amino acid.  Proteins are oxidized on burning and putrification.The product include N,CO2 and  1. 2. 3. 4. 5. 6.  water.