Search results
Results from the WOW.Com Content Network
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]
Given its greater H + concentration, the formula yields a lower pH value for the weak base. However, pH of bases is usually calculated in terms of the OH − concentration. This is done because the H + concentration is not a part of the reaction, whereas the OH − concentration is. The pOH is defined as:
Mass fraction can also be expressed, with a denominator of 100, as percentage by mass (in commercial contexts often called percentage by weight, abbreviated wt.% or % w/w; see mass versus weight). It is one way of expressing the composition of a mixture in a dimensionless size ; mole fraction (percentage by moles , mol%) and volume fraction ...
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]
Conversely, when pH = pK a, the concentration of HA is equal to the concentration of A −. The buffer region extends over the approximate range pK a ± 2. Buffering is weak outside the range pK a ± 1. At pH ≤ pK a − 2 the substance is said to be fully protonated and at pH ≥ pK a + 2 it is fully dissociated (deprotonated).
Molar concentration or molarity is most commonly expressed in units of moles of solute per litre of solution. [1] For use in broader applications, it is defined as amount of substance of solute per unit volume of solution, or per unit volume available to the species, represented by lowercase c {\displaystyle c} : [ 2 ]
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 p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...
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 ...