Which level of protein organisation is exemplified by α-helices and β-sheets?
A
Primary structure
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B
Secondary structure
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C
Tertiary structure
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D
Quaternary structure
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Solution
The correct option is B Secondary structure The primary structure refers to the number and sequence of amino acids in a polypeptide.
The folding of the polypeptide chain in different ways gives rise to its secondary structure. ⍺-helix is the most common type of coil in which the polypeptide folds. Proteins such as keratin, myosin are present as ⍺-helices. Another type of secondary structure is represented by 𝛽-sheets. Here, the polypeptide chains are bonded with the help of hydrogen bonding through their backbone. The chains can occur in a parallel or antiparallel fashion.
Tertiary structure refers to the further coiling and folding of the secondary structure upon itself like a hollow woollen ball or mass.
The quaternary structure involves the aggregation of two or more polypeptide chains or subunits in their tertiary form together in a particular fashion. Each polypeptide develops its own tertiary structure. It includes the number and kinds of subunits in protein, together with their relative position with respect to each other.