Multiple Choice
In proteins, what is the primary role of a peptide bond?
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4. Protein Structure
Peptide Bond
Multiple Choice
In proteins, how is a peptide bond formed between two amino acids?
A
By a hydrolysis reaction that consumes to join the carboxyl and amino groups
B
By forming a disulfide bond between the side chains of two cysteine residues
C
By an ionic attraction (salt bridge) between a protonated amino group and a deprotonated carboxyl group
D
By a condensation (dehydration) reaction in which the carboxyl group of one amino acid reacts with the amino group of another, releasing and forming an amide linkage
Verified step by step guidance1
Identify the functional groups involved in peptide bond formation: the carboxyl group (-COOH) of one amino acid and the amino group (-NH2) of another amino acid.
Understand that peptide bond formation is a condensation (dehydration) reaction, meaning it involves the removal of a water molecule (H2O).
Write the reaction where the hydroxyl group (-OH) from the carboxyl group and a hydrogen atom (H) from the amino group are removed to form water (H2O).
Recognize that the removal of water allows the carbon atom of the carboxyl group to form a covalent bond with the nitrogen atom of the amino group, creating an amide linkage known as a peptide bond.
Summarize that this peptide bond links the two amino acids together, forming a dipeptide and releasing water as a byproduct.
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