Advertisements
Advertisements
प्रश्न
What are the common types of secondary structure of proteins?
Advertisements
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
APPEARS IN
संबंधित प्रश्न
Define the following as related to proteins:
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.
Differentiate between the following :
Peptide linkage and Glycosidic linkage
Which functional group participates in disulphide bond formation in proteins?
Which of the following statement is correct:
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?
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:
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.
What is the effect of denaturation on the structure of proteins?
Write a classification of proteins with an example.
