Final answer:
At a pH above its pKa(side chain), the epsilon-amino group of lysine is deprotonated.
Step-by-step explanation:
At a pH above its pKa(side chain), the epsilon-amino group of lysine is deprotonated.
In its side chain, lysine has an epsilon-amino group (-NH2) that is basic. When the pH is above the pKa of the side chain, the epsilon-amino group will lose a proton and become negatively charged, resulting in deprotonation.
For example, at a pH of 7.4, which is higher than the pKa of lysine's side chain, the epsilon-amino group will be deprotonated and exist as -NH3+