Introduction What are functional proteins? Structures Primary structures Secondary structures Tertiary structures Myoglobin History Role in disease Bonding interaction Conclusion Reference

1. “ FUNCTIONAL PROTEIN“
By
KAUSHAL KUMAR SAHU
Assistant Professor (Ad Hoc)
Department of Biotechnology
Govt. Digvijay Autonomous P. G. College
Raj-Nandgaon ( C. G. )

2. Pt. RAVISHANKAR SHUKLA
UNIVERSITY
RAIPUR 2013
SYNOPSIS
Introduction
What are functional proteins?
Structures
Primary structures
Secondary structures
Tertiary structures
Myoglobin
History
Role in disease
Bonding interaction
Conclusion
Reference

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 Protein are the most abundant biological macromolecules, occurring in all cells
and all parts of cells.
 Proteins also occur in great variety; thousands of different kinds may be found
in a single cell.
 Proteins are polymers of amino acids, with each amino acid residue joined to its
neighbour by a specific type of covalent bond.
 Each protein has a specific chemical & structural function, strongly
suggesting that each has a unique three dimensional structure.
 Protein has many different types of structure present. They are primary,
secondary, super secondary, tertiary and quaternary structure.
INTRODUCTION

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WHAT ARE FUNCTIONAL PROTEIN?
The meaning of a functional protein is that it has the
ability to carry out metabolic processes. The tertiary
structure of a proteins is the functional protein. A functional
protein's metabolic functions are to breakdown (anabolic)
and build up (catabolic) tissues for structural integrity, and
also helps to build the cell walls (peptidoglycan) of plants
and some bacteria, as well as humans.

5. Pt. RAVISHANKAR SHUKLA
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RAIPUR 2013The primary structure refers to amino acid linear sequence of the
polypeptide chain, held together by covalent or peptide bond.
The α carbons of adjacent amino acid residues are separated by
three covalent bond arranged in Cα-C-N-Cα.
The peptide C-N bonds, because of their partial double-bond character,
cannot rotate freely Rotation is permitted about the N-C, and the Cα-C bonds.
Peptide conformation is defined by three dihedral angles
(also known as torsion angles) called φ (phi),ψ(psi), and ω (omega).
PRIMARY STRUCTURE

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SECONDARY STRUCTURE
The term secondary structure refers to any chosen segment
of a polypeptide chain and describes the local spital arrangement.
A regular secondary structure occurs when each dihedral angel,
φ and ψ remain the same or nearly the same throughout
the segment.
There are many types of secondary structure such as αhelix,
βsheet, βturn, loop and super secondary structures.

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αhelix
right handed (clockwise) or
left handed (anticlockwise).
The amino acid residues in a
α-helix have conformation
with φ = -57 and ψ = – 47 and
each helical turn includes 3.6
amino acid residue.

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βconformation
They are in a zigzag
structure.
They are of two types:
parallel & antiparallel.
Parallel:-
φ = -119 ͦ & ψ = +113 ͦ
Antiparallel:-
φ = -139 ͦ & ψ = +135 ͦ

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βturn
Position where
polypeptide chain
changes its direction.
They are very
common when it
connected to two
adjacent antiparallel
βsheet

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loop
loop are necessary to connect adjacent
regions of secondary structure.
It is connecting link between two structure.
It lies on surface of protein.

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TERTIARY PROTEIN
The overall three dimensional arrangement of all atoms
in a protein is referred to as protein’s tertiary structure.
Myoglobin is the best known example of tertiary protein.

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MYOGLOBIN
Myoglobin is an iron- and oxygen-binding protein found in
the muscle tissue of vertebrates in general and in almost all
mammals.
It is related to hemoglobin, which is the iron- and oxygen
binding protein in blood, specifically in the red blood cells.
History
In 1958, Max Perutz and John Kendrew determined the 3D
structure of myoglobin by X-ray crystallography.

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BONDING INTERACTIONS
Disulfide Bonds:
Disulfide bonds are formed by oxidation of the sulfhydryl groups on cystein.
Hydrogen Bonding:

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Salt Bridges
Salt bridges result from the
neutralization of an acid and
amine on side chains.
The final interaction is ionic
between the positive
ammonium group and the
negative acid group.
Any combination of the various
acidic or amine amino acid side
chains will have this effect.

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Non-Polar Hydrophobic Interactions

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BONDING INTERACTION IN MYOGLOBIN

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When muscle tissue is damaged, very large
concentrations of myoglobin enters the kidneys. When
this happens, myoglobin is then considered highly toxic
and may contribute to acute renal failure. Muscle injury
is commonly associated with the release of myoglobin,
and is known to be the cause of heart attacks.

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CONCLUSION
Tertiary structure refers to three-dimensional structure of a single
protein molecule.
Myoglobin is an iron- and oxygen-binding protein found in the muscle.
It is a single-chain globular protein of 153 or 154amino acids,
containing a heme (iron-containing porphyrin) prosthetic group.
There are four types of bonding interactions: hydrogen bonding, salt
bridges, disulfide bonds, and non-polar hydrophobic interactions.

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REFERENCES
Lehninger- PRINCIPLE OF BIOCHEMISTRY
By Nelson & Cox, fifth edition.
Millikan, G. A. (1939). Muscle hemoglobin. Physiol. Rev. 19,503 -523.
www.ncbi.nlm.nih.gov/pubmed/17177361