A peptide bonds forms between the _ and the of another amino acid
The correct answer and explanation is:
A peptide bond forms between the carboxyl group of one amino acid and the amino group of another amino acid.
Explanation:
A peptide bond is a type of covalent bond that links amino acids together to form proteins. Each amino acid contains two key functional groups important in peptide bond formation: an amino group (-NH2) and a carboxyl group (-COOH). When two amino acids join, the carboxyl group of one amino acid reacts with the amino group of another.
During this process, a dehydration synthesis (condensation) reaction occurs. This means a molecule of water (H2O) is removed. Specifically, the hydroxyl group (-OH) from the carboxyl end of one amino acid combines with a hydrogen atom (H) from the amino group of the other amino acid to release water.
As a result, a new bond forms between the carbon atom of the carboxyl group and the nitrogen atom of the amino group. This bond is called a peptide bond or amide bond and is responsible for linking amino acids in a linear chain known as a polypeptide.
The formation of peptide bonds is essential in protein synthesis because proteins are made up of long chains of amino acids connected by these bonds. The sequence and number of amino acids in the chain determine the protein’s structure and function.
Peptide bonds have partial double-bond character due to resonance, which makes the bond rigid and planar. This rigidity influences the folding and three-dimensional structure of proteins, which are vital for their biological activity.
In summary, peptide bonds form between the carboxyl group of one amino acid and the amino group of another through the removal of water, creating the backbone linkage that holds proteins together.