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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
How is tripeptide formed?
Define the following as related to proteins:
Peptide linkage
What are the common types of secondary structure of proteins?
What type of bonding helps in stabilising the α-helix structure of proteins?
Differentiate between the following:
Fibrous proteins and Globular proteins
Write one difference between α-helix and β-pleated structures of proteins.
Which of the following biomolecules is insoluble in water?
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:
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
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?
The main structural feature of proteins is
Each polypeptide in a protein has amino acids linked with each other in a specific sequence. This sequence of amino acids is said to be ______.
Peptide linkage 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?
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.
Write a classification of proteins with an example.
Statement I: A protein is imagined as a line, the left end represented by first amino acid (C-terminal) and the right end represented by last amino acid (Nterminal).
Statement II: Adult human haemoglobin, consists of 4 subunits (two subunits of a type and two subunits β type.)
In the light of the above statements, choose the correct answer from the options given below:
