When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    The cysteine sulfhydryl group is nucleophilic and easily oxidized. The reactivity is enhanced when the thiol is ionized, and cysteine residues in proteins have pK a values close to neutrality, so are often in their reactive thiolate form in the cell. [23] Because of its high reactivity, the sulfhydryl group of cysteine has numerous biological ...

  3. Thiol - Wikipedia

    en.wikipedia.org/wiki/Thiol

    The −SH functional group itself is referred to as either a thiol group or a sulfhydryl group, or a sulfanyl group. Thiols are the sulfur analogue of alcohols (that is, sulfur takes the place of oxygen in the hydroxyl ( −OH ) group of an alcohol), and the word is a blend of " thio- " with "alcohol".

  4. Helenalin - Wikipedia

    en.wikipedia.org/wiki/Helenalin

    [3] [4] The double bond in the carbonyl group can undergo a Michael addition with a thiol group, also called a sulfhydryl group. Therefore, helenalin can interact with proteins by forming covalent bonds to the thiol groups of cysteine-containing proteins/peptides, such as glutathione. This effect can disrupt the molecule's biological function. [2]

  5. Keyhole limpet hemocyanin - Wikipedia

    en.wikipedia.org/wiki/Keyhole_limpet_hemocyanin

    A sulfhydryl-containing hapten can then be reacted with the KLH to complete the immunogen without causing polymerization. The specificity of this reaction is ideal for situations where the cysteine is located away from the desired epitope (e.g. in peptides where a terminal cysteine can be added to either end of the peptide).

  6. Disulfide - Wikipedia

    en.wikipedia.org/wiki/Disulfide

    A unique intramolecular cysteine disulfide bonds in the ATP-binding domain of SrrAB TCs found in Staphylococcus aureus is a good example of disulfides in regulatory proteins, which the redox state of SrrB molecule is controlled by cysteine disulfide bonds, leading to the modification of SrrA activity including gene regulation.

  7. Transition metal thiolate complex - Wikipedia

    en.wikipedia.org/wiki/Transition_metal_thiolate...

    The amino acid cysteine has a thiol functional group, consequently many cofactors in proteins and enzymes feature cysteinate-metal cofactors. [ 1 ] The zinc finger motif, which is found in transcription factors , is a metal thiolate complex.

  8. Ellman's reagent - Wikipedia

    en.wikipedia.org/wiki/Ellman's_reagent

    This reaction is rapid and stoichiometric, with the addition of one mole of thiol releasing one mole of TNB. The TNB 2− is quantified in a spectrophotometer by measuring the absorbance of visible light at 412 nm, using an extinction coefficient of 14,150 M −1 cm −1 for dilute buffer solutions, [4] [5] and a coefficient of 13,700 M −1 cm −1 for high salt concentrations, such as 6 M ...

  9. Mesna - Wikipedia

    en.wikipedia.org/wiki/Mesna

    Mesna assists to detoxify these metabolites by reaction of its sulfhydryl group with α,β-unsaturated carbonyl containing compounds such as acrolein. [5] This reaction is known as a Michael addition. Mesna also increases urinary excretion of cysteine.