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Nitric acid, with a pK value of around −1.7, behaves as a strong acid in aqueous solutions with a pH greater than 1. [23] At lower pH values it behaves as a weak acid. pK a values for strong acids have been estimated by theoretical means. [24] For example, the pK a value of aqueous HCl has been estimated as −9.3.
Examples of acidic functional groups include carboxylic acids (-COOH), sulfonic acids (-SO 3 H), phosphonic acids, and boronic acids. Polyacids accept protons at low pH values. At higher pH values, they deprotonate and become negatively charged. [1] The negative charges create a repulsion that causes the polymer to swell.
The pH range is commonly given as zero to 14, but a pH value can be less than 0 for very concentrated strong acids or greater than 14 for very concentrated strong bases. [ 2 ] The pH scale is traceable to a set of standard solutions whose pH is established by international agreement. [ 3 ]
The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The pK a values of an amino acid side chain in solution is typically inferred from the pK a values of model compounds (compounds that are similar to the ...
An acid with pK a = −2 would be 99 % dissociated at pH 0, that is, in a 1 M HCl solution. Any acid with a pK a less than about −2 is said to be a strong acid. Strong acids are said to be fully dissociated. There is no precise pK a value that distinguishes between strong and weak acids because strong acids, such as sulfuric acid, are ...
The Henderson–Hasselbalch equation can be used to model these equilibria. It is important to maintain this pH of 7.4 to ensure enzymes are able to work optimally. [10] Life threatening Acidosis (a low blood pH resulting in nausea, headaches, and even coma, and convulsions) is due to a lack of functioning of enzymes at a low pH. [10]
The buffering region is dependent upon the pKa, and is typically +/- 1.0 pH units of the pKa. The pKa of KHP is 5.4, so its pH buffering range would be 4.4 to 6.4; however, due to the presence of the second acidic group that bears the potassium ion, the first pKa also contributes to the buffering range well below pH 4.0, which is why KHP is a ...
Buffer capacity falls to 33% of the maximum value at pH = pK a ± 1, to 10% at pH = pK a ± 1.5 and to 1% at pH = pK a ± 2. For this reason the most useful range is approximately pK a ± 1. When choosing a buffer for use at a specific pH, it should have a pK a value as close as possible to that pH. [2]