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प्रश्न
How are proteins classified on the basis of molecular shapes?
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उत्तर
On the basis of molecular shape, proteins are classified into two types—fibrous proteins and globular proteins.
- Fibrous proteins:- They are insoluble in water, long, thread-like and tend to lie side by side to form fibres. The polypeptide chains are held together by hydrogen bonds. Examples: Collagen in tendons; keratin in hair, skin, nails, horn and feathers; myosin in muscle; fibroin in silk
- Globular proteins:- They are soluble in water and aqueous solutions of bases, acids and salts. They are folded to form a spherical shape, have intramolecular hydrogen bonding and have weak intermolecular forces as compared to fibrous proteins.
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संबंधित प्रश्न
What is peptide linkage?
How is tripeptide formed?
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?
Differentiate between the following:
Fibrous proteins and Globular proteins
Differentiate between the following :
Peptide linkage and Glycosidic linkage
Which of the following biomolecules is insoluble in water?
The protein responsible for blood clotting is ____________.
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.
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?
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 ______.
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?
Write a classification of proteins with an example.
