PKa = -log Ka
so if you multiply across by -1 and then taking the antilog you can get Ka
Ka.Kb = Kw where Kw = 1.0 x 10^14
PKa + PKb = PKw = 14
that should give you a start.
pKa of drug can be determined from Handerson Hasselbatch equation., when conc. of salt become equal to acid i.e. at equivalence point when pH=pka then in H-H equn, pH=pka
the pH of ethanol can be calculated using its pKa value (pKa 15.9) and the Henderson-Hasselbalch equation. pH = pKa - log [AH/A] where [AH/A] the ratio of disassociated versus undisassociated species in solution.
A pKa value is a measurement used for bases and acids. The measurement pH applies to hydronium ion concentrations that are in a solution, whereas pKa only applies to determining the amount of dissociation an acid wants to do in a solution.
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The advantage of knowing the pKa of an acid-base indicator is that it tells you the approximate pH value at which the color of the indicator changes. For example, if the pKa of an indicator is 5, then it means that it's going to change colors at around pH 5.
pKa of drug can be determined from Handerson Hasselbatch equation., when conc. of salt become equal to acid i.e. at equivalence point when pH=pka then in H-H equn, pH=pka
By following + or - 2 pH to the pKa value
the pH of ethanol can be calculated using its pKa value (pKa 15.9) and the Henderson-Hasselbalch equation. pH = pKa - log [AH/A] where [AH/A] the ratio of disassociated versus undisassociated species in solution.
A pKa value is a measurement used for bases and acids. The measurement pH applies to hydronium ion concentrations that are in a solution, whereas pKa only applies to determining the amount of dissociation an acid wants to do in a solution.
Its an equation you can use to find the pH of a solution. it is.... --- pH = pKa + log (Base/Acid) --- these may help too Ka = 10^-pKa Kw = Ka*Kb
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How can you calculate pka valve if ph is given?
The pKA of enzyme affects its ionization which could alter enzyme activity. For pH < pKa, the value of vmax is constant and that for pH > pKa, vmax decreases; ie. enzyme activity starts to decline.
The advantage of knowing the pKa of an acid-base indicator is that it tells you the approximate pH value at which the color of the indicator changes. For example, if the pKa of an indicator is 5, then it means that it's going to change colors at around pH 5.
Each buffer will only be of sufficient capacity within a pH interval of pKa+1 > pH > pKa-1 so the optimal buffer pH-range is maximum 2 units.
At 'half way' point the pH is equal to the pKa value of the acid: pH = pKa - log[cA/cB] because at that point cA = cB . So pH = pKa = - log(5.2*10-6) = 5.3
The effective range should be the pKa +/- 1. Therefore, the range should be 1.15 to 3.15.