What is a peptide linkage?

Short Answer

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A peptide linkage, also known as a peptide bond, is a covalent bond formed between two amino acids in a polypeptide chain through a condensation reaction, where a water molecule is eliminated. The bond is formed when the carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH2) of another, resulting in the bond: -CO-NH-. Peptide linkages are essential for forming proteins, determining their structure, and allowing for specific interactions like hydrogen bonding.

Step by step solution

01

Definition of Peptide Linkage

A peptide linkage, also known as a peptide bond, is a covalent bond formed between two amino acids that connects them in a polypeptide chain. In this bond, the carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH2) of another amino acid, resulting in the formation of a peptide linkage.
02

Formation of Peptide Linkage

The formation of a peptide linkage occurs through a condensation reaction, where a molecule of water is eliminated in the process. Here's a step-by-step description of the peptide linkage formation: 1. The carboxyl group (-COOH) of the first amino acid reacts with the amino group (-NH2) of the second amino acid. 2. A water molecule is released: -OH from the carboxyl group and -H from the amino group combine to form H2O. 3. The remaining CO and NH elements form a covalent bond, known as the peptide bond: -CO-NH-
03

Significance of Peptide Linkage

Peptide linkages are crucial for the formation of proteins, which are essential for various biological functions within an organism. The particular sequence of amino acids in a polypeptide chain, connected by peptide linkages, determines the protein's structure and function. Furthermore, the peptide bond has unique characteristics that allow it to participate in specific interactions, such as hydrogen bonding, that contribute to the protein's overall structure.

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