If ph of buffer is greater than pka, then protein will be
Answers
Answer:
The ability of a buffer solution to maintain a nearly constant pH when a small amount of acid or base is added to the solution is greatest at the pKa and diminishes as the pH of the solution goes above or below the pKa. A rule-of-thumb is to use a buffer within 1 pH unit of the pKa to maximize its buffering capacity (see the Henderson-Hasselbach equation provided by Aziz Habibi-Yangjeh for the math).
However, if there is a desire to use a particular buffer outside of its preferred pH range, the buffering capacity of the solution can be increased by increasing the concentration of the buffer. Ammonium acetate (pKa 4.8) (also ammonium bicarbonate and ammonium formate) is used for mass spectrometry because it is volatile. Such a high concentration as 200 mM ensures that the pH will not change unless a substantial amount of acid or base is added. If no acid or base is going to be added, then the pH will not change from where it started, so the weak buffering isn't a problem.
Answer:
If the pH is lower than the pKa, then the compound will be protonated. If the pH is higher than the pKa, then the compound will be deprotonated. A further consideration is the charge on the compound. Acids are neutral when protonated and negatively charged (ionized) when deprotonated.