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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

    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]

  4. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    In this modification, an asparagine or aspartate side chain attacks the following peptide bond, forming a symmetrical succinimide intermediate. Hydrolysis of the intermediate produces either aspartate or the β-amino acid, iso(Asp). For asparagine, either product results in the loss of the amide group, hence "deamidation". hydroxylation

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    The folding is driven by the non-specific hydrophobic interactions, the burial of hydrophobic residues from water, but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds.

  6. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    Thiol protecting groups used in peptide synthesis requiring later regioselective disulfide bond formation must possess multiple characteristics. [43] [44] First, they must be reversible with conditions that do not affect the unprotected side chains. Second, the protecting group must be able to withstand the conditions of solid-phase synthesis.

  7. N-terminus - Wikipedia

    en.wikipedia.org/wiki/N-terminus

    Amino acids link to one another by peptide bonds which form through a dehydration reaction that joins the carboxyl group of one amino acid to the amine group of the next in a head-to-tail manner to form a polypeptide chain. The chain has two ends – an amine group, the N-terminus, and an unbound carboxyl group, the C-terminus. [2]

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    www.aol.com/women-bond-over-using-weight...

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  9. 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.