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  2. Non-proteinogenic amino acids - Wikipedia

    en.wikipedia.org/wiki/Non-proteinogenic_amino_acids

    Lysine. Technically, any organic compound with an amine (–NH 2) and a carboxylic acid (–COOH) functional group is an amino acid. The proteinogenic amino acids are a small subset of this group that possess a central carbon atom (α- or 2-) bearing an amino group, a carboxyl group, a side chain and an α-hydrogen levo conformation, with the exception of glycine, which is achiral, and proline ...

  3. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    Cysteine is chiral, but both D and L-cysteine are found in nature. L‑Cysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. [8] Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Greek κύστις kýstis, "bladder". [9]

  4. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Used in proteins and as a storage for ammonia, it is the most abundant amino acid in the body. Arginine: R Arg Functionally similar to lysine. Serine: S Ser Serine and threonine have a short group ended with a hydroxyl group. Its hydrogen is easy to remove, so serine and threonine often act as hydrogen donors in enzymes.

  5. Thiol - Wikipedia

    en.wikipedia.org/wiki/Thiol

    As the functional group of the amino acid cysteine, the thiol group plays a very important role in biology. When the thiol groups of two cysteine residues (as in monomers or constituent units) are brought near each other in the course of protein folding, an oxidation reaction can generate a cystine unit with a disulfide bond (−S−S−).

  6. Conservative replacement - Wikipedia

    en.wikipedia.org/wiki/Conservative_replacement

    A conservative replacement (also called a conservative mutation or a conservative substitution or a homologous replacement) is an amino acid replacement in a protein that changes a given amino acid to a different amino acid with similar biochemical properties (e.g. charge, hydrophobicity and size).

  7. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    [51] [52] When the nucleophile of TEV protease was converted from cysteine to serine, it protease activity was strongly reduced, but was able to be restored by directed evolution. [55] Non-catalytic proteins have been used as scaffolds, having catalytic triads inserted into them which were then improved by directed evolution.

  8. YcaO - Wikipedia

    en.wikipedia.org/wiki/YcaO

    YcaO is a protein found in bacteria which is involved in the synthesis ... The Thiol group in cysteine and the hydroxyl group of serine and ... a non-profit ...

  9. Iodoacetamide - Wikipedia

    en.wikipedia.org/wiki/Iodoacetamide

    Iodoacetamide is an irreversible inhibitor of all cysteine peptidases, with the mechanism of inhibition occurring from alkylation of the catalytic cysteine residue (see schematic). In comparison with its acid derivative, iodoacetate, iodoacetamide reacts substantially faster.