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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:

विकल्प

  • 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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अध्याय 14: Biomolecules - Multiple Choice Questions (Type - I) [पृष्ठ २०३]

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

संबंधित प्रश्न

How is tripeptide formed?


What are the common types of secondary structure of proteins?


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


Differentiate between the following :

Peptide linkage and Glycosidic linkage 


Which of the following biomolecules is insoluble in water?


The protein responsible for blood clotting is ____________.


The helical structure of protein is stabilized by:


In fibrous proteins, polypeptide chains are held together by:

(i) van der Waals forces

(ii) disulphide linkage

(iii) electrostatic forces of attraction

(iv) hydrogen bonds


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?


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.


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:


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?


An α-helix is a structural feature of ______.


Proteins are polymers of ______.


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