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  2. Gelatin - Wikipedia

    en.wikipedia.org/wiki/Gelatin

    Common examples of foods that contain gelatin are gelatin desserts, trifles, aspic, marshmallows, candy corn, and confections such as Peeps, gummy bears, fruit snacks, and jelly babies. [34] Gelatin may be used as a stabilizer , thickener, or texturizer in foods such as yogurt, cream cheese , and margarine ; it is used, as well, in fat-reduced ...

  3. 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.

  4. Dipeptide - Wikipedia

    en.wikipedia.org/wiki/Dipeptide

    Diphenylalanine is the most studied building block in peptide nanotechnology; Kyotorphin (L-tyrosyl-L-arginine) is a neuroactive dipeptide which plays a role in pain regulation in the brain. Balenine (or ophidine) (beta-alanyl-N tau-methyl histidine) has been identified in the muscles of several species of mammal (including man), and the chicken.

  5. Casein - Wikipedia

    en.wikipedia.org/wiki/Casein

    Sheep and cow milk have a higher casein content than other types of milk with human milk having a particularly low casein content. [2] Casein is the primary emulsifier in milk, that is, it helps in mixing oils, fats, and water in milk. [3] Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive. [4]

  6. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond. [6] All peptides except cyclic peptides have an N-terminal (amine group) and C-terminal (carboxyl group) residue at the end of the peptide (as shown for the tetrapeptide in the image).

  7. The #1 Breakfast to Improve Insulin Resistance, According to ...

    www.aol.com/lifestyle/1-breakfast-improve...

    Some examples include whole wheat bread, oats, corn tortillas or quinoa. Incorporate Protein, Fiber and Fat. Carbs like whole grains are essential for energy, but when eaten alone they can quickly ...

  8. 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.

  9. Leucine - Wikipedia

    en.wikipedia.org/wiki/Leucine

    Leucine (symbol Leu or L) [3] is an essential amino acid that is used in the biosynthesis of proteins.Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isobutyl group, making it a non ...