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In chemistry, protonation (or hydronation) is the adding of a proton (or hydron, or hydrogen cation), usually denoted by H +, to an atom, molecule, or ion, forming a conjugate acid. [1] The complementary process, when a proton is removed from a Brønsted–Lowry acid , is deprotonation .)
Similarly, a base such as spermine has more than one site where protonation can occur. For example, mono-protonation can occur at a terminal −NH 2 group or at internal −NH− groups. The K b values for dissociation of spermine protonated at one or other of the sites are examples of micro-constants.
Acid catalysis is mainly used for organic chemical reactions. Many acids can function as sources for the protons. Acid used for acid catalysis include hydrofluoric acid (in the alkylation process), phosphoric acid, toluenesulfonic acid, polystyrene sulfonate, heteropoly acids, zeolites.
Extreme acidity, heat, and dehydrating conditions are usually required. Other hydrocarbon oxonium ions are formed by protonation or alkylation of alcohols or ethers (R−C− + −R 1 R 2). Secondary oxonium ions have the formula R 2 OH +, an example being protonated ethers. Tertiary oxonium ions have the formula R 3 O +, an example being ...
In chemistry and biochemistry, the Henderson–Hasselbalch equation = + ([] []) relates the pH of a chemical solution of a weak acid to the numerical value of the acid dissociation constant, K a, of acid and the ratio of the concentrations, [] [] of the acid and its conjugate base in an equilibrium.
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The catalytically competent protonation state is the catalytically active protonation state of an enzyme.An enzyme is a protein, which catalyzes a chemical reaction.. Proteins and enzymes consist of amino acids, some of which are titratable (i.e., they can alter their charge when the pH of the solution changes), and an enzyme commonly needs a set of specific residues in its active site to ...
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