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Multiple Choice
Which process makes the peptide bonds of proteins accessible to digestive enzymes during protein digestion?
A
Phosphorylation
B
Denaturation
C
Glycosylation
D
Transamination
Verified step by step guidance
1
Understand the context of protein digestion: Proteins are large macromolecules composed of amino acids linked by peptide bonds. Digestive enzymes, such as pepsin and trypsin, break these bonds to release amino acids for absorption.
Recognize that peptide bonds are typically buried within the folded structure of proteins. To make these bonds accessible to digestive enzymes, the protein's structure must be altered.
Learn about denaturation: Denaturation is the process by which a protein loses its native three-dimensional structure due to external factors such as heat, pH changes, or chemical agents. This unfolds the protein, exposing the peptide bonds.
Compare denaturation to other processes listed: Phosphorylation, glycosylation, and transamination are biochemical modifications that do not directly unfold proteins or expose peptide bonds for digestion. Denaturation is the correct process for this purpose.
Conclude that denaturation is essential for protein digestion because it makes the peptide bonds accessible to digestive enzymes, enabling the breakdown of proteins into amino acids.