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प्रश्न
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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उत्तर
In α-helix structure of protein, a polypeptide chain is stabilize by the formation of intramolecular H – bonding between – NH – group of amino acids in one turn with the >C = O groups of amino acids belonging to adjacent turn.
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संबंधित प्रश्न
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Discuss the optical activity of lactic acid.
Define the following as related to proteins:
Peptide linkage
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(i) Guanine
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\[\ce{\underset{(Glycine)}{H2N - CH2 - COOH}}\];
\[\begin{array}{cc}
\ce{H2N - CH2 - COOH}\\
|\phantom{......}\\
\ce{\underset{(Alanine)}{CH3}\phantom{...}}
\end{array}\]
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The main structural feature of proteins is
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Assertion (A): Proteins are found to have two different types of secondary structures viz alpha-helix and beta-pleated sheet structure.
Reason (R): The secondary structure of proteins is stabilized by hydrogen bonding.
Select the most appropriate answer from the options given below:
Out of the following, which type of interaction is responsible for the stabilisation of the α-helix structure of proteins?
The total number of negative charge in the tetrapeptide, Gly-Glu-Asp-Tyr at pH 12.5 will be ______. (Integer answers)
Assertion (A): Proteins are polymers of α-amino acids connected by a peptide bond.
Reason (R): A tetrapeptide contains 4 amino acids linked by 4 peptide bonds.
