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

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

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प्रश्न

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.

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उत्तर

Due to physical or chemical change, hydrogen bonding and various other attractive forces are disturbed, globules unfold and helix gets uncoiled to form a thread like molecule. Therefore, secondary and tertiary structure of protein loses all or part of their biological activity. This is called denaturation of proteins.

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पाठ 14: Biomolecules - Multiple Choice Questions (Type - I) [पृष्ठ २११]

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एनसीईआरटी एक्झांप्लर Chemistry Exemplar [English] Class 12
पाठ 14 Biomolecules
Multiple Choice Questions (Type - I) | Q 48 | पृष्ठ २११

संबंधित प्रश्‍न

What is peptide linkage?


What are the common types of secondary structure of proteins?


Write one difference between α-helix and β-pleated structures of proteins.


The protein responsible for blood clotting is ____________.


The helical structure of protein is stabilized by:


Which of the following statement is correct:


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?


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:


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 ______.


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 ______.


Write a classification of proteins with an example.


Match List I with List II:

List I List II
A. GLUT-4 I. Hormone
B. Insulin II. Enzyme
C. Trypsin III. Intercellular ground substance
D. Collagen IV. Enables glucose transport into cells

Choose the correct answer from the options given below:


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