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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
How are proteins classified on the basis of molecular shapes?
How is tripeptide formed?
Define the following as related to proteins:
Peptide linkage
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.
Peptide linkage is:
The total number of negative charge in the tetrapeptide, Gly-Glu-Asp-Tyr at pH 12.5 will be ______. (Integer answers)
β-pleated sheet structure in proteins refers to ______.
