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Structure of Proteins - Primary, Secondary, Tertiary Structures, Examples
Structure of Proteins - Primary, Secondary, Tertiary Structures, Examples
Biomolecule
Structure of Proteins
Did you know, other than water, protein is the most abundant substance in your body? In fact, every single
cell of the human body consists of proteins. Proteins have a unique three-dimensional structure, which
allows it to perform its various functions. We shall now study the structure of proteins.
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Classi cation of
Introduction to Monosaccharides Aldoses Introduction to Vitamins,
Biomolecules Hin and Ketoses Hin Classi cation Hin
Structure of Proteins
Proteins are what we call biological polymers (i.e. they occur naturally in nature). Now we previously learnt
that amino acids are the building blocks of proteins. What this actually entails is that proteins are long
chain-like structure, with amino acids being the main ingredient. These amino acids are connected together
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with peptide bonds, and a few such bonds linking together form a polypeptide chain. Now one or more of
these polypeptide chains twist or fold spontaneously and a protein is formed.
The size of the proteins varies greatly. It actually depends on the number of polypeptide molecules it
contains. One of the smallest protein molecules is insulin, and the largest being Titin which consist of 34,350
amino acids. Let us now look at the four types of protein structure that make up a protein molecule.
Carbohydrates
Monosaccharides
Disaccharides
Polysaccharides
Amino Acids
Enzymes
Vitamins
Nucleic Acids
The primary structure is the unique formation and order in which the amino acids (the building blocks)
combine and link to give us a protein molecule. Protein gets all its properties from its primary structure.
There are in all twenty amino acids in the human body. All of these have a carboxyl group and an amino
group. But each has a different variable group known as the “R” group. It is this R group that lends a
particular protein its unique structure.
Every protein is determined by the sequencing of the amino acids. The formation and ordering of these
amino acids in proteins are extremely specific. If we alter even one amino acid in the chain it results in a
non-functioning protein or what we call a gene mutation.
After the sequencing of amino acids, we now move on to the secondary structure. This is when the peptide
backbone of the protein structure will fold onto itself, to give proteins their unique shape. This folding of the
polypeptide chains happens due to the interaction between the carboxyl groups along with the amine
groups of the peptide chains.
There are two kinds of shapes formed in the secondary structure. These are
α-helix: The backbone follows a helical structure. The hydrogen bonds with the oxygen between the
different layers of the helix, giving it this helical structure.
β-pleated sheet: here the polypeptide chains are stacked next to each other and their outer hydrogen
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3] Tertiary Structures
This is the structure that gives protein the 3-D shape and formation. After the amino acids form bonds
(secondary structure) and shapes like helices and sheets, the structure can coil or fold at random. This is
what we call the tertiary structure of proteins. If this structure is disrupted or disturbed a protein is said to
be denatured which means it is chemically affected and its structure is distorted.
a. Dehydration
b. deamination
c. denaturation
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Sol: The correct answer is option “C”. Denaturation of proteins is the disruption and even possibly the
destruction of both secondary and also tertiary structures of proteins.
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Biomolecule
Vitamins Structure of Nucleic Acids Nucleic Acids Structure of Proteins Enzymes Amino Acids
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