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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 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.

  4. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    A peptide bond forms between the amino acid attached to the tRNA in the P site and the amino acid attached to a tRNA in the A site. The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids.

  5. 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 ...

  6. 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:

  7. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    Proteases, which are themselves proteins, come in several types according to the particular peptide bonds that they cleave as well as their tendency to cleave peptide bonds at the terminus of a protein (exopeptidases) vs peptide bonds at the interior of the protein (endopeptidases). [107] Pepsin is an endopeptidase in the stomach.

  8. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    The ribosomes catalyze the formation of covalent peptide bonds between the encoded amino acids to form a polypeptide chain. [citation needed] Following translation the polypeptide chain must fold to form a functional protein; for example, to function as an enzyme the polypeptide chain must fold correctly to produce a functional active site.

  9. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    These secondary structures are defined by patterns of hydrogen bonds between the main-chain peptide groups. They have a regular geometry, being constrained to specific values of the dihedral angles ψ and φ on the Ramachandran plot. Both the α-helix and the β-sheet represent a way of saturating all the hydrogen bond donors and acceptors in ...