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प्रश्न
Write one difference between α-helix and β-pleated structures of proteins.
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उत्तर
| α -helix | β -pleated sheet |
| The α -helix results from coiling of the protein chain such that the peptide bonds making up the backbone are able to form hydrogen bonds between each other. | The β -pleated sheet is a layering of protein chains one on the top of another. |
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संबंधित प्रश्न
Define the following as related to proteins:
Peptide linkage
What are the common types of secondary structure of proteins?
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) |  |
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 ______.
Explain formation of peptide linkage in protein with an example.
The correct structure of Ruhemann's Purple, the compound formed in the reaction of ninhydrin with proteins is:
