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  2. Peptide bond - Wikipedia

    en.wikipedia.org/wiki/Peptide_bond

    Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.

  3. Amide - Wikipedia

    en.wikipedia.org/wiki/Amide

    [4] [5] The amide group is called a peptide bond when it is part of the main chain of a protein, and an isopeptide bond when it occurs in a side chain, as in asparagine and glutamine. It can be viewed as a derivative of a carboxylic acid ( R−C(=O)−OH ) with the hydroxyl group ( −OH ) replaced by an amine group ( −NR′R″ ); or ...

  4. Isopeptide bond - Wikipedia

    en.wikipedia.org/wiki/Isopeptide_bond

    Amide bonds, and thus isopeptide bonds, are stabilized by resonance (electron delocalization) between the carbonyl oxygen, the carbonyl carbon, and the nitrogen atom. The bond strength of an isopeptide bond is similar to that of a peptide due to the similar bonding type. The bond strength of a peptide bond is around 300 kJ/mol, or about 70 kcal ...

  5. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.

  6. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    Drosomycin, an example of a peptide. Peptides are short chains of amino acids linked by peptide bonds. [1] [2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. [4]

  7. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    However, additional molecular interactions may render the amide form less stable; the amino group is expelled instead, resulting in an ester (Ser/Thr) or thioester (Cys) bond in place of the peptide bond. This chemical reaction is called an N-O acyl shift. The ester/thioester bond can be resolved in several ways:

  8. Dipeptide - Wikipedia

    en.wikipedia.org/wiki/Dipeptide

    Diphenylalanine is the most studied building block in peptide nanotechnology; Kyotorphin (L-tyrosyl-L-arginine) is a neuroactive dipeptide which plays a role in pain regulation in the brain. Balenine (or ophidine) (beta-alanyl-N tau-methyl histidine) has been identified in the muscles of several species of mammal (including man), and the chicken.

  9. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    When proline is bound as an amide in a peptide bond, its nitrogen is not bound to any hydrogen, meaning it cannot act as a hydrogen bond donor, but can be a hydrogen bond acceptor. Peptide bond formation with incoming Pro-tRNA Pro in the ribosome is considerably slower than with any other tRNAs, which is a general feature of N-alkylamino acids ...