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महाराष्ट्र राज्य शिक्षण मंडळएचएससी विज्ञान (सामान्य) इयत्ता १२ वी

Explain formation of peptide linkage in protein with an example.

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प्रश्न

Explain formation of peptide linkage in protein with an example.

टीपा लिहा
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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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2021-2022 (March) Set 1

संबंधित प्रश्‍न

How is tripeptide formed?


Define the following as related to proteins:

Peptide linkage


What are the common types of secondary structure of proteins?


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


Differentiate between  the following:

Fibrous proteins and Globular 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 correct statement for protein haemoglobin.


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:


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


Which of the following are purine bases?

(i) Guanine

(ii) Adenine

(iii) Thymine

(iv) Uracil


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?


Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?


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?


The total number of negative charge in the tetrapeptide, Gly-Glu-Asp-Tyr at pH 12.5 will be ______. (Integer answers)


An α-helix is a structural feature of ______.


β-pleated sheet structure in proteins refers to ______.


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


Write a classification of proteins with an example.


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