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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. Transition metal amino acid complexes - Wikipedia

    en.wikipedia.org/wiki/Transition_metal_amino...

    Amino acids are prevalent in nature, and all of them function as ligands toward the transition metals. [1] Not included in this article are complexes of the amides (including peptide) and ester derivatives of amino acids. Also excluded are the polyamino acids including the chelating agents EDTA and NTA.

  4. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    The first and third scales are derived from the physiochemical properties of the amino acid side chains. These scales result mainly from inspection of the amino acid structures. [14] [1] Biswas et al., divided the scales based on the method used to obtain the scale into five different categories. [3]

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    The existing specialized amino acid sequence compressors are low compared with that of DNA sequence compressors, mainly because of the characteristics of the data. For example, modeling inversions is harder because of the reverse information loss (from amino acids to DNA sequence).

  6. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Among the tightest known protein–protein complexes is that between the enzyme angiogenin and ribonuclease inhibitor; the dissociation constant for the human proteins is 5x10 −16 mol/L. [3] [4] Another biological example is the binding protein streptavidin, which has extraordinarily high affinity for biotin (vitamin B7/H, dissociation ...

  7. Isopeptide bond - Wikipedia

    en.wikipedia.org/wiki/Isopeptide_bond

    Amino acids such as lysine, glutamic acid, glutamine, aspartic acid, and asparagine can form isopeptide bonds because they all contain an amino or carboxyl group on their side chain. For example, the formation of an isopeptide bond between the sidechains of lysine and glutamine is as follows: Gln−(C=O)NH 2 + Lys-NH 3 + → Gln−(C=O)NH−Lys ...

  8. Chemical specificity - Wikipedia

    en.wikipedia.org/wiki/Chemical_specificity

    If a given enzyme has a high chemical specificity, this means that the set of ligands to which it binds is limited, such that neither binding events nor catalysis can occur at an appreciable rate with additional molecules. An example of a protein-ligand pair whose binding activity can be highly specific is the antibody-antigen system. [2]

  9. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids.