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प्रश्न
Differentiate between the following:
Fibrous proteins and Globular proteins
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उत्तर १
| Fibrous protein | Globular protein |
| It is a fibre-like structure formed by the polypeptide chain. These proteins are held together by strong hydrogen and disulphide bonds. | The polypeptide chain in this protein is folded around itself, giving rise to a spherical structure. |
| It is usually insoluble in water. | It is usually soluble in water. |
| Fibrous proteins are usually used for structural purposes. For example, keratin is present in nails and hair; collagen in tendons; and myosin in muscles. | All enzymes are globular proteins. Some hormones such as insulin are also globular proteins. |
उत्तर २
Fibrous proteins: These proteins consist of linear thread like molecules which tend to lie side by side (parallel) to form fibres. The polypeptide chains in them are held together usually at many points by hydrogen bonds and some disulphide bonds. As a result,intermolecular forces of attraction are very’ strong and hence fibrous proteins are insoluble in water. Further, these proteins are stable to moderate changes in temperature and pH. Fibrous proteins serve as the chief structural material of animal tissues.For example, keratin in skin, hair, nails and wool, collagen in tendons, fibrosis in silk and myosin in muscles.
Globular proteins: The polypeptide chain in these proteins is folded around itself in such a way so as to give the entire protein molecule an almost spheroidal shape. The folding takes place in such a manner that hydrophobic (non-polar) parts are pushed inwards and hydrophilic (polar) parts are pushed outwards. As a result, water molecules interact strongly with the polar groups and hence globular protein are water soluble. As compared to fibrous proteins, these are very sensitive to small changes of temperature and pH. This class of proteins include all enzymes, many hormones such as insulin from pancreas, thyroglobulin from thyroid gland, etc.
संबंधित प्रश्न
What is peptide linkage?
How is tripeptide formed?
Define the following as related to proteins:
Peptide linkage
Write one difference between α-helix and β-pleated structures of proteins.
Which of the following biomolecules is insoluble in water?
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) | ![]() |
Which moieties of nucleosides are involved in the formation of phosphodiester linkages present in dinucleotides? What does the word diester in the name of linkage indicate? Which acid is involved in the formation of this linkage?
Peptide linkage is:
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)
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.
What is the effect of denaturation on the structure of proteins?
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:



