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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

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

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

संबंधित प्रश्न

How is tripeptide formed?


Define the following as related to proteins:

Peptide linkage


What are the common types of secondary structure of proteins?


Differentiate between  the following:

Fibrous proteins and Globular proteins


Write one difference between α-helix and β-pleated structures of proteins.


Differentiate between the following :

Peptide linkage and Glycosidic linkage 


The protein responsible for blood clotting is ____________.


The correct statement for protein haemoglobin.


Which functional group participates in disulphide bond formation in proteins?


Optical rotations of some compounds along with their structures are given below which of them have D configuration.

(I)
(II)
(III)

Which of the following are purine bases?

(i) Guanine

(ii) Adenine

(iii) Thymine

(iv) Uracil


Each polypeptide in a protein has amino acids linked with each other in a specific sequence. This sequence of amino acids is said to be ______.


Peptide linkage 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:


Presence of disulphide link gives rise to which structure of protein?


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)


An α-helix is a structural feature of ______.


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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