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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: - Chemistry

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

संबंधित प्रश्न

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 


The protein responsible for blood clotting is ____________.


The correct statement for protein haemoglobin.


Which functional group participates in disulphide bond formation in proteins?


Which of the following statement is correct:


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


Which of the following are purine bases?

(i) Guanine

(ii) Adenine

(iii) Thymine

(iv) Uracil


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.


Which moieties of nucleosides are involved in the formation of phosphodiester linkages present in dinucleotides? What does the word diester in the name of linkage indicate? Which acid is involved in the formation of this linkage?


Peptide linkage is:


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


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 ______.


β-pleated sheet structure in proteins refers to ______.


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