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Description

A peptide bond is also known as a bond. Is formed between the alpha nitrogen atom of amino acid and the second carbonyl carbon.

The so-called isopeptide bond refers to the amide bond between the side chain amine or a carbonyl group. Not the α-amine or α-carbonyl group. For example, in glutathione, the γ-carboxyl group of glutamic acid is combined with the α-amino group of cysteine.

During translation, peptide bonds are formed by the removal of water from the amino (N) terminus to the carboxy (C) terminals. And is catalyzed by RNAs that are part of the ribosome called the ribosome. .37 Peptides can also be synthesized in vitro for therapeutic and experimental purposes. Chemical peptide synthesis proceeds from the C-terminus to the N-terminus. Using N-protected amino acids and is catalyzed by N, N’-dicyclohexylurea. 38.39

Amino Acid:

  1. The amino acids coexist in the condensation reaction to form the dipeptide and water.
  2. Homologous bonds between amino acids are called peptide bonds, and therefore long chains of homologously linked amino acids are called polypeptides.
  3. Polypeptide chains can be broken down through a hydrolysis reaction that requires water to reverse this process.

Electron sharing in the amide bond

In an amide bond (also known as a bond), the electron exchange is delocalized, effectively preventing rotation around the bond. Such bonds are stable in the plane. The conformational flexibility of the peptide backbone is purely the result of the rotation of the two bonds to the బంధ carbon axis. The angle of rotation around these bonds is called the Ramachandran angle.

In theory, free rotation around these joints allows angles from -180 to 180 degrees. In fact, stearic acid and energy factors limit possible combinations. These bond angles play a key role in regulating the secondary structure of proteins. For example, the values in the alpha spiral  ‌ are -60 and -45 degrees, respectively. The secondary structure will be discussed more fully later in this chapter.

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