In: Chemistry
a. The glutamate side chain has a pKa of 4.4. Calculate the percentage of glu that is unprotonated at a pH of 4.7.
pH is the negative log of the hydrogen ion concentration in a solution. Similarly pKA is the negative log of the acid dissociation constant for an amino acid side chain.
pH = -Log [H+]
pKa = - Log Ka
In solution, if pH < pKA, then the protonated form of an amino acid side chain predominates according to the Henderson-Hasselbalch equation . If pH > pKA, then the deprotonated form of the amino acid side chain predominates. The charge on an acidic side chain can therefore vary between -1 (when pH << pKA) and 0 ( when pH >> pKA).
In case of glutamate, with a side chain pKA = 4.4.
When the pH = pKA, the concentration of the protonated and deprotonated forms is equal and the charge is -0.5.
When pH = 6.4, the glutamate is about 99% deprotonated, leading to a charge of -0.99. When pH = 2.4, the glutamate is about 99% protonated, leading to a charge of -0.01.
If we consider at pH= 4.7 concentration of protonated form reduce by 5% then we can use Henderson-Hasselbalch equation as follows,
pH = pKa + log [Deprotonated form]/[Protonated form]
4.7 = 4.4 + log (X/45)
X = 89.78% approximately
Concentration of deprotonated form at pH 4.7 will be 89.78% approximately