Advertisements
Advertisements
Question
Explain formation of peptide linkage in protein with an example.
Advertisements
Solution
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:

APPEARS IN
RELATED QUESTIONS
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
Write one difference between α-helix and β-pleated structures of proteins.
The protein responsible for blood clotting is ____________.
The helical structure of protein is stabilized by:
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?
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
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.
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
Peptide linkage is:
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:
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 ______.
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.



