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  2. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    Cysteine (/ ˈ s ɪ s t ɪ iː n /; [5] symbol Cys or C [6]) is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine ...

  3. Thiol - Wikipedia

    en.wikipedia.org/wiki/Thiol

    In organic chemistry, a thiol (/ ˈ θ aɪ ɒ l /; [1] from Ancient Greek θεῖον (theion) ' sulfur ' [2]), or thiol derivative, is any organosulfur compound of the form R−SH, where R represents an alkyl or other organic substituent. The −SH functional group itself is referred to as either a thiol group or a sulfhydryl group, or a ...

  4. 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 ...

  5. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    The most commonly used nucleophiles are the hydroxyl (OH) of serine and the thiol/thiolate ion (SH/S −) of cysteine. [2] Alternatively, threonine proteases use the secondary hydroxyl of threonine, however due to steric hindrance of the side chain's extra methyl group , such proteases use their N -terminal amide as the base rather than a ...

  6. Cystine - Wikipedia

    en.wikipedia.org/wiki/Cystine

    Cystine is the oxidized derivative of the amino acid cysteine and has the formula (SCH 2 CH(NH 2)CO 2 H) 2.It is a white solid that is poorly soluble in water. As a residue in proteins, cystine serves two functions: a site of redox reactions and a mechanical linkage that allows proteins to retain their three-dimensional structure.

  7. Strecker amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Strecker_amino_acid_synthesis

    A 1,2-diamino-diol is then formed after proton exchange and a nucleophilic attack of water to the former nitrile carbon. Ammonia is subsequently eliminated after the protonation of the amino group, and finally the deprotonation of a hydroxyl group produces an amino acid. Mechanism of the Strecker synthesis

  8. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    However, due to the chemical lability of these phosphorylated residues, and in marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated histidine (and other non-canonical amino acids) using standard biochemical and mass spectrometric approaches is much more challenging [16] [17] [18] and special procedures and ...

  9. Iodoacetamide - Wikipedia

    en.wikipedia.org/wiki/Iodoacetamide

    Iodoacetamide (IAA) is an organic compound with the chemical formula I C H 2 CO NH 2. It is an alkylating agent used for peptide mapping purposes. Its actions are similar to those of iodoacetate. It is commonly used to bind covalently with the thiol group of cysteine so the protein cannot form disulfide bonds.