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कर्नाटक बोर्ड पी.यू.सी.पीयूसी विज्ञान 2nd PUC Class 12

Differentiate between the following: Fibrous proteins and Globular proteins

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प्रश्न

Differentiate between  the following:

Fibrous proteins and Globular proteins

फरक स्पष्ट करा
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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.
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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.

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पाठ 10: Biomolecules - Exercises [पृष्ठ ३०२]

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एनसीईआरटी Chemistry Part 1 and 2 [English] Class 12
पाठ 10 Biomolecules
Exercises | Q 10.15 | पृष्ठ ३०२

संबंधित प्रश्‍न

What type of bonding helps in stabilising the α-helix 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:


Dinucleotide is obtained by joining two nucleotides together by phosphodiester linkage. Between which carbon atoms of pentose sugars of nucleotides are these linkages present?


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


Which of the following are purine bases?

(i) Guanine

(ii) Adenine

(iii) Thymine

(iv) Uracil


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?


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.


The main structural feature of proteins is


Explain formation of peptide linkage in protein with an example.


Given below are two statements labelled as Assertion (A) and Reason (R).

Assertion (A): Proteins are found to have two different types of secondary structures viz alpha-helix and beta-pleated sheet structure.

Reason (R): The secondary structure of proteins is stabilized by hydrogen bonding.

Select the most appropriate answer from the options given below:


Presence of disulphide link gives rise to which structure of protein?


Out of the following, which type of interaction is responsible for the stabilisation of the α-helix structure of proteins?


An α-helix is a structural feature of ______.


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.


β-pleated sheet structure in proteins refers to ______.


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