Advertisements
Advertisements
Question
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:
Options
Peptide bonds
van der Waals forces
Hydrogen bonds
Dipole-dipole interactions
Solution
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
RELATED QUESTIONS
What is peptide linkage?
How is tripeptide formed?
What are the common types of secondary structure of proteins?
What type of bonding helps in stabilising the ∝-helix structure of proteins?
Differentiate between the following :
Fibrous proteins and Globular proteins
The protein responsible for blood clotting is ____________.
Which of the following are purine bases?
(i) Guanine
(ii) Adenine
(iii) Thymine
(iv) Uracil
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.
