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DEPARTMENT OF MICROBIOLOGY BARKATULLAH UNIVERSITY BHOPAL
s presented by :- Harishchandra Ahirwar (M.Sc. I Sem.)
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STRUCTURE AND PROPERTIES OF PROTEINS
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CONTENTS1. Introduction2. History3. Structure
A. PrimaryB. SecondaryC. TertiaryD. Quaternary
4. Properties5. Function6. Summary
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INTRODUCTION Protiens are the most abundant organic
molecules of the living system.Proteins are the polymer of Amino Acids. The term protien is generally used for a
polypeptide containing more than 50 amino acids.
They are involved in most of our body’s function.
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HISTORYThe term ‘Protein’ is derived from a
Greek Word ‘Proteios’ meaning ‘holding the first place.
Berzelius (swedish chemist) suggested the name Protein.
Mulder (dutch chemist) in 1838 used the term Protein.
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STRUCTURE OF PROTEIN
1. Primary structure2. Secondary structure3. Tertiary structure 4. Quaternary structure
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Primary Structure of а Protein The primary structure of а protein is the sequence of
amino acids present in its peptide chain. The end with the free H3N+ group is called the N-
terminal end, and the end with the free СОО- group is called the С-terminal end...
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PRIMARY STRUCTURE
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Secondary structureThe secondary structure of a protein results from hydrogen bonds at regular intervals along the polypeptide backbone.– Typical shapes that
develop from secondary structure are coils (an alpha helix) or folds (beta pleated sheets).
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ALPHA HELIX
The alpha helix structure resembles а coiled helical spring, with the coil configuration maintained by hydrogen bonds between N – Н and С= О groups of every fourth amino acid.
Alpha Helix
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The beta pleated sheet secondary structure involves amino acid chains that are almost completely extended.
Beta pleated sheet
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• Tertiary structure is determined by a variety of interactions among R groups and the polypeptide backbone.– These interactions include hydrogen bonds ,
ionic bonds hydrophobic and van der waals interactions .
Tertiary structure
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TERTIARY STRUCTURE
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• Quaternary structure results from the aggregation of two or more polypeptide subunits.–Collagen is a fibrous protein of three
polypeptides that are supercoiled like a rope.• This provides the structural strength for their
role in connective tissue.–Haemoglobin is a globular protein with two
copies of two kinds of polypeptides.
Quaternary structure
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PROPERTIES OF PROTEINS1. Solubility:-Protein form colloidal solution instead
of true solutions in water.2. Molecular weight:-Proteins vary in their
molecular weight, dependent on no. of Amino acid residues.
3. Shape:-Wide variation in the protein shape, may be globular (insulin), oval (albumin), fibrous (fibrinogen).
4. Isoelectric pH:-At isoelectric pH, proteins exist as dipolar ions.
5. Acidic & basic proteins6. Precipitation of proteins
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FUNCTION OF PROTEINSProteins perform a great variety of specialized and essential function in the living cells
These functions are grouped as Static (Structural) Dynamic
Structural functions :- Certain protiens are primarily responsible for structure and strength of body. These include collagen and elastin found in bone matrix, vascular system and other organs.
Dynamic functions :- The dynamic functions of protiens are as acting like enzymes , hormones, blood clotting factors ,immunoglobins,
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REFRENCESBIOCHEMISTRY BY Dr. U. Satyanarayana
TEXTBOOK OF BIOCHEMISTRY BY Jain & Jain
Images from google
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THANK YOU