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  2. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a ...

  3. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    The endothelial protease vasohibin [f] uses a cysteine as the nucleophile, but a serine to coordinate the histidine base. [43] [44] Despite the serine being a poor acid, it is still effective in orienting the histidine in the catalytic triad. [43] Some homologues alternatively have a threonine instead of serine at the acid location. [43]

  4. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    Continuing with the T4 lysozyme example, a titration curve is obtained through observation of a shift in the C2 proton of histidine 31 (Figure 5). Figure 5 shows the shift in the titration curve between the wild-type and the mutant in which Asp70 is Asn. The salt bridge formed is between the deprotonated Asp70 and protonated His31.

  5. Triosephosphate isomerase - Wikipedia

    en.wikipedia.org/wiki/Triosephosphate_isomerase

    The nucleophilic glutamate 165 residue of TPI deprotonates the substrate, [4] and the electrophilic histidine 95 residue donates a proton to form the enediol intermediate. [5] [6] When deprotonated, the enediolate then collapses and, abstracting a proton from protonated glutamate 165, forms the GAP product. Catalysis of the reverse reaction ...

  6. RNA hydrolysis - Wikipedia

    en.wikipedia.org/wiki/RNA_hydrolysis

    RNA hydrolysis occurs when the deprotonated 2’ OH of the ribose, acting as a nucleophile, attacks the adjacent phosphorus in the phosphodiester bond of the sugar-phosphate backbone of the RNA. [1] There is a transition state (shown above), where the phosphorus is bonded to five oxygen atoms. [ 2 ]

  7. Deprotonation - Wikipedia

    en.wikipedia.org/wiki/Deprotonation

    To determine whether or not a given base will be sufficient to deprotonate a specific acid, compare the conjugate base with the original base. A conjugate base is formed when the acid is deprotonated by the base. In the image above, hydroxide acts as a base to deprotonate the carboxylic acid. The conjugate base is the carboxylate salt.

  8. His-tag - Wikipedia

    en.wikipedia.org/wiki/His-tag

    Imidazole is the side chain of histidine and is typically used at a concentration of 150 - 500 mM for elution. Histidine or histamine can also be used. Decrease in pH; When the pH decreases, the histidine residue is protonated and can no longer coordinate the metal tag, allowing the protein to be eluted.

  9. Cysteine protease - Wikipedia

    en.wikipedia.org/wiki/Cysteine_protease

    The next step is nucleophilic attack by the deprotonated cysteine's anionic sulfur on the substrate carbonyl carbon. In this step, a fragment of the substrate is released with an amine terminus, the histidine residue in the protease is restored to its deprotonated form, and a thioester intermediate linking the new carboxy-terminus of the ...