Advertisements
Advertisements
प्रश्न
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:
पर्याय
Peptide bonds
van der Waals forces
Hydrogen bonds
Dipole-dipole interactions
Advertisements
उत्तर
Hydrogen bonds
Explanation:
These structures arise due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between > C – O and N – H – group 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 > C = O of an adjacent turn of helix.
APPEARS IN
संबंधित प्रश्न
What is peptide linkage?
What are the common types of secondary 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 of the following biomolecules is insoluble in water?
The protein responsible for blood clotting is ____________.
Which functional group participates in disulphide bond formation in proteins?
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 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?
Assertion: β-glycosidic linkage is present in maltose,
Reason: Maltose is composed of two glucose units in which C–1 of one glucose unit is linked to C–4 of another glucose unit.
The main structural feature of proteins is
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:
An α-helix is a structural feature of ______.
Proteins are polymers of ______.
