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प्रश्न
Define the following as related to proteins:
Peptide linkage
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उत्तर
Chemically, peptide linkage is an amide formed between the –COOH group and –NH2 group. The reaction between two molecules of similar or different amino acids proceeds through the combination of the amino group of one molecule with the carboxyl group of the other. This results in the elimination of a water molecule and the formation of a peptide bond –CO–NH–. The product of the reaction is called a dipeptide because it is made up of two amino acids.
For example, when the carboxyl group of glycine combines with the amino group of alanine, we get a dipeptide, glycylalanine.
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संबंधित प्रश्न
What is 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?
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:
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:
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
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
Peptide linkage is:
Explain formation of peptide linkage in protein with an example.
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?
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)
Write a classification of proteins with an example.
Statement I: A protein is imagined as a line, the left end represented by first amino acid (C-terminal) and the right end represented by last amino acid (Nterminal).
Statement II: Adult human haemoglobin, consists of 4 subunits (two subunits of a type and two subunits β type.)
In the light of the above statements, choose the correct answer from the options given below:
