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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. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    A neuropeptide is a peptide that is active in association with neural tissue. A lipopeptide is a peptide that has a lipid connected to it, and pepducins are lipopeptides that interact with GPCRs. A peptide hormone is a peptide that acts as a hormone. A proteose is a mixture of peptides produced by the hydrolysis of proteins. The term is ...

  4. Amino acid activation - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_activation

    Peptide bond formation is an endergonic, thermodynamically unfavorable process, so amino acids must be activated by covalent linkage to tRNA molecules. The energy stored within the aminoacyl-tRNA bond is used to drive peptide bond formation. Activation thus enhances the reactivity of the amino acid and drives peptide bond synthesis.

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    It is attached to the polypeptide C-terminus through an amide linkage that then connects to ethanolamine, thence to sundry sugars and finally to the phosphatidylinositol lipid moiety. Finally, the peptide side chains can also be modified covalently, e.g., phosphorylation

  6. Chemical ligation - Wikipedia

    en.wikipedia.org/wiki/Chemical_ligation

    The "chemical ligation" concept was introduced by Kent in the early 1990s. [1] It consisted of a novel approach to the covalent condensation of unprotected peptide segments by means of "unique, mutually reactive functionalities, one on each reacting peptide segment, designed to react only with each other and not with any of the functional groups found in (native) peptides".

  7. Glycopeptide - Wikipedia

    en.wikipedia.org/wiki/Glycopeptide

    Glycopeptides are peptides that contain carbohydrate moieties covalently attached to the side chains of the amino acid residues that constitute the peptide.. Over the past few decades it has been recognised that glycans on cell surface (attached to membrane proteins or lipids) and those bound to proteins (glycoproteins) play a critical role in biology.

  8. Turn (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Turn_(biochemistry)

    According to one definition, a turn is a structural motif where the C α atoms of two residues separated by a few (usually 1 to 5) peptide bonds are close (less than 7 Å [0.70 nm]). [1] The proximity of the terminal C α atoms often correlates with formation of an inter main chain hydrogen bond between the corresponding residues. Such hydrogen ...

  9. Peptidyl transferase center - Wikipedia

    en.wikipedia.org/wiki/Peptidyl_transferase_center

    The peptidyl transferase center (EC 2.3.2.12) is an aminoacyltransferase ribozyme (RNA enzyme) located in the large subunit of the ribosome.It forms peptide bonds between adjacent amino acids during the translation process of protein biosynthesis. [1]