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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
Discuss the optical activity of lactic acid.
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?
The protein responsible for blood clotting is ____________.
The correct statement for protein haemoglobin.
Which functional group participates in disulphide bond formation in proteins?
Optical rotations of some compounds along with their structures are given below which of them have D configuration.
| (I) |  |
| (II) |  |
| (III) |  |
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.
Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?
Explain formation of peptide linkage in protein with an example.
Out of the following, which type of interaction is responsible for the stabilisation of the α-helix structure of proteins?
The correct structure of Ruhemann's Purple, the compound formed in the reaction of ninhydrin with proteins is:
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 ______.
What is the effect of denaturation on the structure of proteins?
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:
