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  2. Peptide bond - Wikipedia

    en.wikipedia.org/wiki/Peptide_bond

    Peptide bond. In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid and N2 (nitrogen number two) of another, along a peptide or protein chain.

  3. Amide - Wikipedia

    en.wikipedia.org/wiki/Amide

    The stability of amide bonds has biological implications, since the amino acids that make up proteins are linked with amide bonds. Amide bonds are resistant enough to hydrolysis to maintain protein structure in aqueous environments but are susceptible to catalyzed hydrolysis. [citation needed] Primary and secondary amides do not react usefully ...

  4. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    A polypeptide is a single linear chain of many amino acids (any length), held together by amide bonds. A protein consists of one or more polypeptides (more than about 50 amino acids long). An oligopeptide consists of only a few amino acids (between two and twenty).

  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. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    For completeness, the proposal that proteins contained amide linkages was made as early as 1882 by the French chemist E. Grimaux. [6] Despite these data and later evidence that proteolytically digested proteins yielded only oligopeptides, the idea that proteins were linear, unbranched polymers of amino acids was not accepted immediately.

  7. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    The standard hydrogen-bond definition for secondary structure is that of DSSP, which is a purely electrostatic model. It assigns charges of ±q 1 ≈ 0.42e to the carbonyl carbon and oxygen, respectively, and charges of ±q 2 ≈ 0.20e to the amide hydrogen and nitrogen, respectively. The electrostatic energy is

  8. Myristoylation - Wikipedia

    en.wikipedia.org/wiki/Myristoylation

    Co-translational addition of myristic acid by N-myristoyltransferase to N-terminal glycine of a nascent protein. Myristoylation is a lipidation modification where a myristoyl group, derived from myristic acid, is covalently attached by an amide bond to the alpha-amino group of an N-terminal glycine residue. [1]

  9. Nonribosomal peptide - Wikipedia

    en.wikipedia.org/wiki/Nonribosomal_peptide

    PCP: Thiolation and peptide carrier protein with attached 4'-phospho-pantetheine (required in a module) C: Condensation forming the amide bond (required in a module) Cy: Cyclization into thiazoline or oxazolines (optional) Ox: Oxidation of thiazolines or oxazolines to thiazoles or oxazoles (optional)