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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
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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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संबंधित प्रश्न
What is peptide linkage?
How is tripeptide formed?
Discuss the optical activity of lactic acid.
What type of bonding helps in stabilising the α-helix structure of proteins?
Differentiate between the following :
Peptide linkage and Glycosidic linkage
The helical structure of protein is stabilized by:
Which functional group participates in disulphide bond formation in proteins?
Dinucleotide is obtained by joining two nucleotides together by phosphodiester linkage. Between which carbon atoms of pentose sugars of nucleotides are these linkages present?
Optical rotations of some compounds along with their structures are given below which of them have D configuration.
| (I) | ![]() |
| (II) | ![]() |
| (III) | ![]() |
Proteins can be classified into two types on the basis of their molecular shape i.e., fibrous proteins and globular proteins. Examples of globular proteins are:
(i) Insulin
(ii) Keratin
(iii) Albumin
(iv) Myosin
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
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?
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:
Explain formation of peptide linkage in protein with an example.
β-pleated sheet structure in proteins refers to ______.
Write a classification of proteins with an example.



