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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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What are the common types of secondary structure of proteins?
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Peptide linkage and Glycosidic linkage
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Which of the following statement is correct:
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:
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Given below are two statements labelled as Assertion (A) and Reason (R).
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Reason (R): The secondary structure of proteins is stabilized by hydrogen bonding.
Select the most appropriate answer from the options given below:
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The total number of negative charge in the tetrapeptide, Gly-Glu-Asp-Tyr at pH 12.5 will be ______. (Integer answers)
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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.
Statement I: A protein is imagined as a line, the left end represented by first amino acid (C-terminal) and the right end represented by last amino acid (Nterminal).
Statement II: Adult human haemoglobin, consists of 4 subunits (two subunits of a type and two subunits β type.)
In the light of the above statements, choose the correct answer from the options given below:
