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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?
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?
Write one difference between α-helix and β-pleated structures of proteins.
Differentiate between the following :
Peptide linkage and Glycosidic linkage
The protein responsible for blood clotting is ____________.
The helical structure of protein is stabilized by:
The correct statement for protein haemoglobin.
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:
Optical rotations of some compounds along with their structures are given below which of them have D configuration.
| (I) | ![]() |
| (II) | ![]() |
| (III) | ![]() |
Which of the following are purine bases?
(i) Guanine
(ii) Adenine
(iii) Thymine
(iv) Uracil
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?
Structures of glycine and alanine are given below. Show the peptide linkage in glycylalanine.
\[\ce{\underset{(Glycine)}{H2N - CH2 - COOH}}\];
\[\begin{array}{cc}
\ce{H2N - CH2 - COOH}\\
|\phantom{......}\\
\ce{\underset{(Alanine)}{CH3}\phantom{...}}
\end{array}\]
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.
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.
Each polypeptide in a protein has amino acids linked with each other in a specific sequence. This sequence of amino acids is said to be ______.
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)
An α-helix is a structural feature of ______.
Proteins are polymers 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.



