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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?
Discuss the optical activity of lactic acid.
Define the following as related to proteins:
Peptide linkage
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.
The protein responsible for blood clotting is ____________.
The helical structure of protein is stabilized by:
The correct statement for protein haemoglobin.
Which functional group participates in disulphide bond formation in proteins?
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:
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
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?
Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?
Peptide linkage is:
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 ______.
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?
