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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:
विकल्प
Peptide bonds
van der Waals forces
Hydrogen bonds
Dipole-dipole interactions
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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.
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संबंधित प्रश्न
How are proteins classified on the basis of molecular shapes?
What is peptide linkage?
How is tripeptide formed?
Define the following as related to proteins:
Peptide linkage
Differentiate between the following:
Fibrous proteins and Globular proteins
Write one difference between α-helix and β-pleated structures of proteins.
Which of the following biomolecules is insoluble in water?
Which of the following statement is correct:
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?
Structures of glycine and alanine are given below. Show the peptide linkage in glycylalanine.
\[\ce{\underset{(Glycine)}{H2N - CH2 - COOH}}\];
\[\begin{array}{cc}
\ce{H2N - CH2 - COOH}\\
|\phantom{......}\\
\ce{\underset{(Alanine)}{CH3}\phantom{...}}
\end{array}\]
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.
Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?
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 ______.
Explain formation of peptide linkage in protein with an example.
The total number of negative charge in the tetrapeptide, Gly-Glu-Asp-Tyr at pH 12.5 will be ______. (Integer answers)
Proteins are polymers of ______.
