Question

Peptide bond formation is an example of: A. saponification. B. electrophilic addition. C. bimolecular elimination. D. dehydration.

Short answer

D. Dehydration.

Step-by-step solution

- Understand the Question

Identify the chemical process involved in peptide bond formation.

- Recall Key Concepts

Peptide bond formation is a process where amino acids are linked together by a covalent bond.

- Identify the Nature of the Reaction

During peptide bond formation, a molecule of water is released as a byproduct. This process involves the removal of a water molecule (H₂O).

- Match with Answer Choices

Consider the definitions of each of the given processes: A. Saponification - Reaction of fats with a base to form soap. B. Electrophilic Addition - Addition of an electrophile to a multiple bond. C. Bimolecular Elimination - Removal of two substituents to form a double bond D. Dehydration - Removal of a water molecule (H₂O).Given that peptide bond formation involves the release of a water molecule, the correct answer is D. Dehydration.

Key concepts

Covalent Bonds in Biochemistry

Covalent bonds are essential in biochemistry as they help form stable structures in living organisms. A covalent bond occurs when two atoms share pairs of electrons. In the context of biochemistry, these bonds typically form between non-metal atoms. Sharing electrons allows each atom to achieve a more stable electron configuration, which is crucial for building the complex molecules needed for life.
Peptide bonds are a specific kind of covalent bond. They form between amino acids, which are the building blocks of proteins. The bond forms between the carboxyl group of one amino acid and the amino group of another, linking them together and creating a stable chain. This stability is crucial for the proper functioning of proteins in our bodies.
Some characteristics of covalent bonds in biochemistry include:

• Strong and stable bonds
• Formation of molecular structures like proteins
• Involvement in metabolic reactions

Understanding covalent bonds' role in biological systems helps us grasp how life itself is structured and maintained.

Dehydration Reaction

A dehydration reaction is a chemical reaction where water is removed from the reacting molecules. This process is crucial in forming many biomolecules, including proteins and carbohydrates. During peptide bond formation, a dehydration reaction occurs.
The process involves removing a water molecule (H₂O) from the amino acids linking together. This removal happens as follows: the hydroxyl group (-OH) from the carboxyl group of one amino acid and a hydrogen atom (H) from the amino group of another amino acid come together to release a water molecule.
Key aspects of dehydration reactions include:

• Formation of complex molecules like proteins
• Release of water as a byproduct
• Essential for constructing macromolecules in living organisms

Thus, dehydration reactions play a pivotal role in synthesizing large biological molecules necessary for life.

Amino Acids Linkage

Amino acids linkage is vital in the formation of proteins, one of the most important classes of biomolecules. Proteins perform various functions, including transport, catalyzing reactions, and structural support. Linking amino acids via peptide bonds is fundamental for these proteins to function.
When amino acids bond during protein formation, this linkage happens through a peptide bond. The carboxyl group of one amino acid forms a covalent bond with the amino group of another. This bond formation releases a molecule of water, which is characteristic of a dehydration reaction.
Insights into amino acid linkage include:

• Foundational for protein synthesis
• Involves the formation of peptide bonds
• Critical for various protein functions in the body

Understanding how amino acids link to form proteins allows us to appreciate the complex machinery of life and the role proteins play in maintaining it.