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प्रश्न
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:
पर्याय
Peptide bonds
van der Waals forces
Hydrogen bonds
Dipole-dipole interactions
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उत्तर
Hydrogen bonds
Explanation:
These structures arise due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between > C – O and N – H – group of the peptide bond.
α-helix is one of the most common ways in which a polypeptide chain forms all possible hydrogen bonds by twisting into a right-handed screw (helix) with the –NH group of each amino acid residue hydrogen-bonded to > C = O of an adjacent turn of helix.
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संबंधित प्रश्न
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Peptide linkage and Glycosidic linkage
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| (I) | ![]() |
| (II) | ![]() |
| (III) | ![]() |
α-Helix is a secondary structure of proteins formed by twisting of polypeptide chain into right-handed screw like structures. Which type of interactions are responsible for making the α-helix structure stable?
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