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Multiple Choice
In proteins, how are peptide bonds formed between two amino acids?
A
By hydrolysis of an existing amide bond, consuming to link the amino acids
B
By a condensation (dehydration) reaction between the carboxyl group of one amino acid and the amino group of another, releasing
C
By an oxidation reaction that creates a disulfide bond between two cysteine side chains
D
By formation of an ionic (salt) bridge between the amino and carboxyl groups without loss of any small molecule
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Verified step by step guidance
1
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 bonds are formed through a condensation (dehydration) reaction, which means a molecule of water (H\_2O) is released during the process.
Write the general reaction where the hydroxyl group (-OH) from the carboxyl group and a hydrogen atom (H) from the amino group are removed to form water:
Recognize that the bond formed between the carbon atom of the carboxyl group and the nitrogen atom of the amino group is called a peptide bond (an amide bond).
Note that this process is not hydrolysis (which breaks peptide bonds by adding water), nor is it an oxidation or ionic interaction; it specifically involves the removal of water to link amino acids covalently.