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प्रश्न
How is tripeptide formed?
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उत्तर
b. The reaction of the COOH group of one amino acid molecule and NH2 group of the neighbouring amino acid molecule forms peptide having -CO-NH- linkage by
elimination of water
The dipeptide formed reacts with another molecule of amino acid to form tripeptide
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संबंधित प्रश्न
How are proteins classified on the basis of molecular shapes?
What is peptide linkage?
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?
Write one difference between α-helix and β-pleated structures of proteins.
The correct statement for protein haemoglobin.
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:
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) |  |
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
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:
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 ______.
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.
What is the effect of denaturation on the structure of proteins?
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:
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:
