Concept explainers
(a)
Interpretation:
The a-keratin and hemoglobin should be compared on the basis of secondary structure.
Concept Introduction:
The primary structure of a protein is the sequence of amino acids. The a-helix and β-sheet structures are the secondary structures. Similarly, tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds, etc. which get altered after heating or in the presence of certain chemicals. Hence, these structures get changed during the denaturation of the protein.
(b)
Interpretation:
The a-keratin and hemoglobin should be compared on the basis of water solubility.
Concept Introduction:
The primary structure of a protein is the sequence of amino acids. The a-helix and β-sheet structures are the secondary structures. Similarly, tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds, etc. which get altered after heating or in the presence of certain chemicals. Hence, these structures get changed during the denaturation of the protein.
(c)
Interpretation:
The a-keratin and hemoglobin should be compared on the basis of the function.
Concept Introduction:
The primary structure of a protein is the sequence of amino acids. The a-helix and β-sheet structures are the secondary structures. Similarly, tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds, etc. which get altered after heating or in the presence of certain chemicals. Hence, these structures get changed during the denaturation of the protein.
(d)
Interpretation:
The a-keratin and hemoglobin should be compared on the basis of location in the body.
Concept Introduction:
The primary structure of protein is the sequence of amino acids. The a-helix and β-sheet structure are the secondary structures. Similarly tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds, etc. which get altered after heating or in the presence of certain chemicals. Hence these structures get changed during denaturation of the protein.
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