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Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?

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प्रश्न

Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?

दीर्घउत्तर
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उत्तर

Primary structure of proteins: Proteins may have one or more polypeptide chains. Each polypeptide in a protein has amino acids linked with each other in a specific sequence and it is this sequence of amino acids that is said to be the primary structure of that protein. Any change in this primary structure i.e., the sequence of amino acids creates a different protein.

Secondary structure of proteins: The secondary structure of protein refers to the shape in which a long polypeptide chain. The secondary can exist. They are found to exist in two different types of structures viz. α-helix and β-pleated sheet structure. These structures arise due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between carbonyl group and –NH– groups of the peptide bond. α-Helix is one of the most common ways in which a polypeptide chain forms all possible hydrogen bonds by twisting into a right-handed screw (helix) with the carbonyl and –NH group of each amino acid residue hydrogen-bonded to the (>C = O) of an adjacent turn of the helix. In β-structure all people chains are stretched out to nearly maximum extension and then laid side by side which are held together by intermolecular hydrogen bonds.

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अध्याय 14: Biomolecules - Multiple Choice Questions (Type - I) [पृष्ठ २१३]

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एनसीईआरटी एक्झांप्लर Chemistry Exemplar [English] Class 12
अध्याय 14 Biomolecules
Multiple Choice Questions (Type - I) | Q 70 | पृष्ठ २१३

संबंधित प्रश्न

What is peptide linkage?


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 functional group participates in disulphide bond formation in proteins?


Which of the following statement is correct:


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:


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.


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 ______.


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.


β-pleated sheet structure in proteins refers to ______.


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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