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प्रश्न
Explain formation of peptide linkage in protein with an example.
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उत्तर
Proteins are polymers of α-amino acid, and a huge number of α-amino acid peptide bonds connect them (amide bond).
A peptide bond is a chemical link produced between two molecules when one of their carboxyl groups combines with the amino group of the other releasing a water molecule (H2O). This is a dehydration synthesis reaction (also known as a condensation reaction) that happens most commonly between amino acids.
For example:
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संबंधित प्रश्न
How are proteins classified on the basis of molecular shapes?
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.
Which of the following biomolecules is insoluble in water?
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:
Optical rotations of some compounds along with their structures are given below which of them have D configuration.
| (I) |  |
| (II) |  |
| (III) |  |
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
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.
Assertion: β-glycosidic linkage is present in maltose,
Reason: Maltose is composed of two glucose units in which C–1 of one glucose unit is linked to C–4 of another glucose unit.
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 ______.
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?
An α-helix is a structural feature of ______.
Proteins are polymers 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.
β-pleated sheet structure in proteins refers to ______.
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:
