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प्रश्न
Write a classification of proteins with an example.
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उत्तर
- Globular Proteins: Molecules of globular proteins have spherical shape. This shape results from coiling around of the polypeptide chain of protein. Globular proteins are usually soluble in water.
For example: insulin, egg albumin, serum albumin, legumelin (protein in pulses) -
Fibrous Proteins: Molecules of fibrous proteins have an elongated, rod-like shape. This shape is the result of holding the polypeptide chains of protein parallel to each other. Hydrogen bonds and disulfide bonds are responsible for this shape. Fibrous proteins are insoluble. in water.
For example: keratin (present in hair, nails, and wool); myosin (protein of muscles).
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संबंधित प्रश्न
Discuss the optical activity of lactic acid.
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) |  |
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?
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.
Which moieties of nucleosides are involved in the formation of phosphodiester linkages present in dinucleotides? What does the word diester in the name of linkage indicate? Which acid is involved in the formation of this linkage?
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:
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 ______.
β-pleated sheet structure in proteins refers to ______.
What is the effect of denaturation on the structure of proteins?
