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Question
Proteins are found to have two different types of secondary structures viz α− helix and β− pleated sheet structure. α− helix structure of protein is stabilised by
(a) peptide bonds (b) van der Waals, forces
(c) hydrogen bonds (d) dipole-dipole interactions
Proteins are found to have two different types of secondary structures viz α− helix and β− pleated sheet structure. α− helix structure of protein is stabilised by
(a) peptide bonds (b) van der Waals, forces
(c) hydrogen bonds (d) dipole-dipole interactions
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Solution
(c) Secondary structures of protein denote the shape in which a long polypeptide chain exists. The secondary structure exists in two type of structure α− helix and β− pleated structure.
In α− helix structure, a polypeptide chain forms all possible hydrogen bonds by twisting into a right-handed screw with -NH group of each amino acid rest hydrogen bonded to>C=O of adjacent amino acid, which forms a helix.
(c) Secondary structures of protein denote the shape in which a long polypeptide chain exists. The secondary structure exists in two type of structure α− helix and β− pleated structure.
In α− helix structure, a polypeptide chain forms all possible hydrogen bonds by twisting into a right-handed screw with -NH group of each amino acid rest hydrogen bonded to>C=O of adjacent amino acid, which forms a helix.
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