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One use of conjugate acids and bases lies in buffering systems, which include a buffer solution. In a buffer, a weak acid and its conjugate base (in the form of a salt), or a weak base and its conjugate acid, are used in order to limit the pH change during a titration process. Buffers have both organic and non-organic chemical applications.
The silicon plays the key role in stabilizing the carbocation of carbon at the β-position. Hosomi-Sakurai reaction is also applicable for other functional groups such as enones, where conjugate addition is usually seen. In figure 2, the Hosomi- Sakurai reaction has been shown using a cinnamoyl ketone.
The utility of the Cu(I)-catalyzed click reaction has also been demonstrated in the polymerization reaction of a bis-azide and a bis-alkyne with copper(I) and TBTA to a conjugated fluorene based polymer. [8] The degree of polymerization easily exceeds 50. With a stopper molecule such as phenyl azide, well-defined phenyl end-groups are obtained.
Other interference may come from the buffer used when preparing the protein sample. A high concentration of buffer will cause an overestimated protein concentration due to depletion of free protons from the solution by conjugate base from the buffer. This will not be a problem if a low concentration of protein (subsequently the buffer) is used. [6]
Dynamic kinetic resolution of 1,4 conjugate reduction. The rate-limiting step is the copper complex interaction with the double bond and the transfer of hydrogen. 1,4 conjugate reduction to cyclic enones. Copper proved to be an excellent metal in this reaction due to its ability to complex with the oxygen when the hydrogen was added.
In chemistry, azide (/ ˈ eɪ z aɪ d /, AY-zyd) is a linear, polyatomic anion with the formula N − 3 and structure − N=N + =N −.It is the conjugate base of hydrazoic acid HN 3. Organic azides are organic compounds with the formula RN 3, containing the azide functional group. [1]
The nucleophilic lysine residue is commonly targeted site in protein bioconjugation, typically through amine-reactive N-hydroxysuccinimidyl (NHS) esters. [3] To obtain optimal number of deprotonated lysine residues, the pH of the aqueous solution must be below the pKa of the lysine ammonium group, which is around 10.5, so the typical pH of the reaction is about 8 and 9.
A compound is a carbon acid if deprotonation results in loss of a proton from a carbon atom. Compared to compounds typically considered to be acids (e.g., mineral acids like nitric acid , or carboxylic acids like acetic acid ), carbon acids are typically many orders of magnitude weaker, although exceptions exist (see below).