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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
What is peptide linkage?
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 helical structure of protein is stabilized by:
The correct statement for protein haemoglobin.
Which functional group participates in disulphide bond formation in proteins?
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:
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
Which of the following are purine bases?
(i) Guanine
(ii) Adenine
(iii) Thymine
(iv) Uracil
Peptide linkage is:
Presence of disulphide link gives rise to which structure of protein?
Out of the following, which type of interaction is responsible for the stabilisation of the α-helix structure of proteins?
The correct structure of Ruhemann's Purple, the compound formed in the reaction of ninhydrin with proteins is:
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 ______.
Proteins are polymers of ______.
β-pleated sheet structure in proteins refers to ______.
What is the effect of denaturation on the structure of proteins?
