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प्रश्न
Presence of disulphide link gives rise to which structure of protein?
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उत्तर
Tertiary structure of protein
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संबंधित प्रश्न
How are proteins classified on the basis of molecular shapes?
How is tripeptide formed?
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.
Differentiate between the following :
Peptide linkage and Glycosidic linkage
Which of the following biomolecules is insoluble in water?
The correct statement for protein haemoglobin.
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
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 ______.
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)
Proteins are polymers of ______.
β-pleated sheet structure in proteins refers to ______.
