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Introduction and Properties of
protein
S.Sabarinathan
Research scholar
SRM university
Proteins
• The molecules which yields amino acids upon
hydrolysis are called proteins.
• Proteins are natural polymer of amino acids.
The number of amino acids in a protein
molecule may range from two to several
thousands.
• Protein molecules contain nitrogen, carbon
hydrogen and oxygen.
Cont...
• Proteins are the basis for the major structural
components of animal and human tissue.
• They act as biological catalysts (Enzymes),
form structural parts of organisms. Participate
in deferent cell reaction,. Act as molecules of
immunity and also provide fuel.
General structure of protein
General properties of protein
• Found in all living organisms.
• Involved in processes such a digestion of food,
cell structure, Catalysis, Movement, Energy
manipulation etc.
• Complex molecules.
• Polymers of amino acids. Long chains of
amino acids are called polypeptides.
Physical and chemical properties
• Proteins are cololourless and usually tasteless.
These are homogenous and crystalline.
• The proteins range in shape form simple
crystalloid spherical structure to long febrile
structures. Tow distinct patterns of shape have
been recognised – Globular proteins and
Fibrillar proteins .
Cont...
• The globular proteins are spherical in shape and
occur mainly in pants. Esp.. In seeds and in leaf
cells. These are bundles formed by folding and
crumpling of proteins chains, eg., pepsin , edestin,
Insulin, Ribonuclesase etc..
• The fibrillar proteins are thread- like or
ellipsoidal in shape and occur generally in animal
muscles. Most of the studies regarding protein
structure have been conducted using these protein
structure have been conducted using this proteins.
Eg., fibrinogen. Myosin etc.
Cont..
• Proteins generally have large molecular weights
ranging between 5*103 and 1*106. it might be
noted that the values of molecular weights of
many proteins lie close to re multiples of 35,000
and 70,000.
• Because of their giant size. The proteins exhibit
many colloidal properties, such as; their diffusion
rates are extremely slow and they may produce
considerable light – scattering in solution, this
resulting in visible turbidity ( Tyndall effect ).
Cont...
• Denaturation – it is the changes in the
properties of a protein. In other words. It is
the loss of biologic activity. In many instances
the process of denaturation is followed by
coagulation – a process were denatured
protein molecules tend to form large
aggregates and to precipitate from solution.
• Amphoteric nature- like amino acids, thee
proteins are amphoteric, therefore they act as
acids and alkalies both, these migrate in an
electric field and direction of migration
depends upon the net chare possessed by the
molecule, the net charge is influenced by the
pH value. Each protein has a fixed value of
isolectric point (pl) at which it will move in an
electric field.
Cont...
• The solubility of proteins is influenced by pH
• Solubility is lowest at isoelectric point and
increases with increasing acidity or
alkalinity. Thus they will be more soluble than
in the isoelectric state.
• All protein solutions rotate the plane of
polarized light to the left therefore these are
levotatotary.
• It also posses some chemical properties such
as hydrolysis
Thank you

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Introduction and properties of protein

  • 1. Introduction and Properties of protein S.Sabarinathan Research scholar SRM university
  • 2. Proteins • The molecules which yields amino acids upon hydrolysis are called proteins. • Proteins are natural polymer of amino acids. The number of amino acids in a protein molecule may range from two to several thousands. • Protein molecules contain nitrogen, carbon hydrogen and oxygen.
  • 3. Cont... • Proteins are the basis for the major structural components of animal and human tissue. • They act as biological catalysts (Enzymes), form structural parts of organisms. Participate in deferent cell reaction,. Act as molecules of immunity and also provide fuel.
  • 5. General properties of protein • Found in all living organisms. • Involved in processes such a digestion of food, cell structure, Catalysis, Movement, Energy manipulation etc. • Complex molecules. • Polymers of amino acids. Long chains of amino acids are called polypeptides.
  • 6. Physical and chemical properties • Proteins are cololourless and usually tasteless. These are homogenous and crystalline. • The proteins range in shape form simple crystalloid spherical structure to long febrile structures. Tow distinct patterns of shape have been recognised – Globular proteins and Fibrillar proteins .
  • 7. Cont... • The globular proteins are spherical in shape and occur mainly in pants. Esp.. In seeds and in leaf cells. These are bundles formed by folding and crumpling of proteins chains, eg., pepsin , edestin, Insulin, Ribonuclesase etc.. • The fibrillar proteins are thread- like or ellipsoidal in shape and occur generally in animal muscles. Most of the studies regarding protein structure have been conducted using these protein structure have been conducted using this proteins. Eg., fibrinogen. Myosin etc.
  • 8. Cont.. • Proteins generally have large molecular weights ranging between 5*103 and 1*106. it might be noted that the values of molecular weights of many proteins lie close to re multiples of 35,000 and 70,000. • Because of their giant size. The proteins exhibit many colloidal properties, such as; their diffusion rates are extremely slow and they may produce considerable light – scattering in solution, this resulting in visible turbidity ( Tyndall effect ).
  • 9. Cont... • Denaturation – it is the changes in the properties of a protein. In other words. It is the loss of biologic activity. In many instances the process of denaturation is followed by coagulation – a process were denatured protein molecules tend to form large aggregates and to precipitate from solution.
  • 10. • Amphoteric nature- like amino acids, thee proteins are amphoteric, therefore they act as acids and alkalies both, these migrate in an electric field and direction of migration depends upon the net chare possessed by the molecule, the net charge is influenced by the pH value. Each protein has a fixed value of isolectric point (pl) at which it will move in an electric field.
  • 11. Cont... • The solubility of proteins is influenced by pH • Solubility is lowest at isoelectric point and increases with increasing acidity or alkalinity. Thus they will be more soluble than in the isoelectric state. • All protein solutions rotate the plane of polarized light to the left therefore these are levotatotary. • It also posses some chemical properties such as hydrolysis