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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 are proteins classified on the basis of molecular shapes?


What is peptide linkage?


How is tripeptide formed?


Discuss the optical activity of lactic acid.


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


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:


Dinucleotide is obtained by joining two nucleotides together by phosphodiester linkage. Between which carbon atoms of pentose sugars of nucleotides are these linkages present?


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


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?


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


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:


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


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


β-pleated sheet structure in proteins refers to ______.


Write a classification of proteins with an example.


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:


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