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What are the common types of secondary structure of proteins? - Chemistry

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प्रश्न

What are the common types of secondary structure of proteins?

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सविस्तर उत्तर
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उत्तर

The secondary structure of protein refers to the shape in which a long polypeptide chain can exist. They are found to exist in two different types of structures, viz., an α-helix and a β-pleated sheet structure. These structures arise due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between \[\begin{array}{cc}\ce{O}\\||\\\ce{-C-}\end{array}\] 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 –NH group of each amino acid residue hydrogen bonded to the \[\begin{array}{cc}\backslash\phantom{.....}\\\ce{C=O}\\/\phantom{......}\end{array}\] of an adjacent turn of the helix as shown in the figure.


    α-Helix structure of proteins

In β-pleated sheet structure, all peptide chains are stretched out to nearly maximum extension and then laid side by side, which are held together by intermolecular hydrogen bonds. The structure resembles the pleated folds of drapery and therefore is known as a β-pleated sheet.


β-Pleated sheet structure of proteins

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पाठ 10: Biomolecules - Exercises [पृष्ठ ३०२]

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एनसीईआरटी Chemistry Part 1 and 2 [English] Class 12
पाठ 10 Biomolecules
Exercises | Q 10.13 | पृष्ठ ३०२

संबंधित प्रश्‍न

Discuss the optical activity of lactic acid.


Differentiate between the following :

Peptide linkage and Glycosidic linkage 


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?


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


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.


The main structural feature of proteins is


Explain formation of peptide linkage in protein with an example.


Presence of disulphide link gives rise to which structure of protein?


The correct structure of Ruhemann's Purple, the compound formed in the reaction of ninhydrin with proteins is:


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 ______.


What is the effect of denaturation on the structure of proteins?


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