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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 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 somewhat archaic. A peptidergic agent (or drug) is a chemical which functions to directly modulate the peptide systems in the body or brain. An example is opioidergics, which are neuropeptidergics.

  4. 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:

  5. 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 ≈ 0.42 e to the carbonyl carbon and oxygen, respectively, and charges of ± q 2 ≈ 0.20 e to the amide hydrogen and nitrogen, respectively.

  6. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions. Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains.

  7. Translation (biology) - Wikipedia

    en.wikipedia.org/wiki/Translation_(biology)

    An example of this is the expression of AMPK in various cancers; its activation triggers a cascade that can ultimately allow the cancer to escape apoptosis (programmed cell death) triggered by nutrition deprivation. Future cancer therapies may involve disrupting the translation machinery of the cell to counter the downstream effects of cancer.

  8. From Bundled Deals to Bigger Snacks: How America Ate in 2024

    www.aol.com/bundled-deals-bigger-snacks-america...

    For example, Thanksgiving will have indulgent dishes, maybe [some] made a little bit fresher or healthier. But if that’s not possible, I’m not going to apologize for my full-fat recipes.”

  9. Tripeptide - Wikipedia

    en.wikipedia.org/wiki/Tripeptide

    A tripeptide (example Val-Gly-Ala) with green marked amino end (L-Valine) and blue marked carboxyl end (L-Alanine) A tripeptide is a peptide derived from three amino acids joined by two or sometimes three peptide bonds. [1] As for proteins, the function of peptides is determined by the constituent amino acids and their sequence.