मराठी
कर्नाटक बोर्ड पी.यू.सी.पीयूसी विज्ञान 2nd PUC Class 12

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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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

MCQ
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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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पाठ 14: Biomolecules - Multiple Choice Questions (Type - I) [पृष्ठ २०३]

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एनसीईआरटी एक्झांप्लर Chemistry Exemplar [English] Class 12
पाठ 14 Biomolecules
Multiple Choice Questions (Type - I) | Q 5 | पृष्ठ २०३

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


Which of the following statement is correct:


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

(I)
(II)
(III)

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.


The main structural feature of proteins is


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 ______.


Explain formation of peptide linkage in protein with an example.


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 correct structure of Ruhemann's Purple, the compound formed in the reaction of ninhydrin with proteins is:


An α-helix is a structural feature of ______.


Proteins are polymers of ______.


What is the effect of denaturation on the structure of proteins?


Match List I with List II:

List I List II
A. GLUT-4 I. Hormone
B. Insulin II. Enzyme
C. Trypsin III. Intercellular ground substance
D. Collagen IV. Enables glucose transport into cells

Choose the correct answer from the options given below:


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:


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