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  2. Oligopeptide - Wikipedia

    en.wikipedia.org/wiki/Oligopeptide

    An oligopeptide (oligo-, "a few"), is a peptide consisting of two to twenty amino acids, including dipeptides, tripeptides, tetrapeptides, and other polypeptides. Some of the major classes of naturally occurring oligopeptides include aeruginosins , cyanopeptolins , microcystins , microviridins , microginins , anabaenopeptins , and cyclamides .

  3. Peptide - Wikipedia

    en.wikipedia.org/wiki/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] Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.

  4. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    A first kinetically controlled product rearranges to form the amide bond. The most common form of native chemical ligation uses a peptide thioester that reacts with a terminal cysteine residue. [58] Other methods applicable for covalently linking polypeptides in aqueous solution include the use of split inteins, [59] spontaneous isopeptide bond ...

  5. 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.

  6. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide , rather than a protein. [ 1 ]

  7. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Intramolecular transesterification, resulting in a branched polypeptide. In inteins, the new ester bond is broken by an intramolecular attack by the soon-to-be C-terminal asparagine. Intermolecular transesterification can transfer a whole segment from one polypeptide to another, as is seen in the Hedgehog protein autoprocessing.

  8. Oligomer - Wikipedia

    en.wikipedia.org/wiki/Oligomer

    An oligomer of amino acids is called an oligopeptide or just a peptide. An oligosaccharide is an oligomer of monosaccharides (simple sugars). An oligonucleotide is a short single-stranded fragment of nucleic acid such as DNA or RNA, or similar fragments of analogs of nucleic acids such as peptide nucleic acid or Morpholinos.

  9. Oligopeptidase - Wikipedia

    en.wikipedia.org/wiki/Oligopeptidase

    The prolyl-oligopeptidase or prolyl endopeptidase (POP) is a good example of how an oligopeptidase interacts with and metabolizes an oligopeptide. The peptide has first to penetrate into a 4 Å hole on the surface of the enzyme in order to reach an 8,500Å 3 internal cavity, where the active site is located.