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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 structu - Chemistry

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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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पाठ 14: Biomolecules - Multiple Choice Questions (Type - I) [पृष्ठ २१०]

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एनसीईआरटी एक्झांप्लर Chemistry [English] Class 12
पाठ 14 Biomolecules
Multiple Choice Questions (Type - I) | Q 39 | पृष्ठ २१०

संबंधित प्रश्‍न

How are proteins classified on the basis of molecular shapes?


What is peptide linkage?


Discuss the optical activity of lactic acid.


Define the following as related to proteins:

Peptide linkage


What are the common types of secondary structure of proteins?


What type of bonding helps in stabilising the α-helix structure of proteins?


Differentiate between  the following:

Fibrous proteins and Globular proteins


The correct statement for protein haemoglobin.


Which of the following statement is correct:


Dinucleotide is obtained by joining two nucleotides together by phosphodiester linkage. Between which carbon atoms of pentose sugars of nucleotides are these linkages present?


Which of the following are purine bases?

(i) Guanine

(ii) Adenine

(iii) Thymine

(iv) Uracil


Structures of glycine and alanine are given below. Show the peptide linkage in glycylalanine.

\[\ce{\underset{(Glycine)}{H2N - CH2 - COOH}}\]; 

\[\begin{array}{cc}
\ce{H2N - CH2 - COOH}\\
|\phantom{......}\\
\ce{\underset{(Alanine)}{CH3}\phantom{...}}
\end{array}\]


Protein found in a biological system with a unique three-dimensional structure and biological activity is called a native protein. When a protein in its native form, is subjected to a physical change like change in temperature or a chemical change like, change in pH, denaturation of protein takes place. Explain the cause.


Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?


The main structural feature of proteins is


Given below are two statements labelled as Assertion (A) and Reason (R).

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.


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